Summary of your 'study carrel' ============================== This is a summary of your Distant Reader 'study carrel'. The Distant Reader harvested & cached your content into a collection/corpus. It then applied sets of natural language processing and text mining against the collection. The results of this process was reduced to a database file -- a 'study carrel'. The study carrel can then be queried, thus bringing light specific characteristics for your collection. These characteristics can help you summarize the collection as well as enumerate things you might want to investigate more closely. This report is a terse narrative report, and when processing is complete you will be linked to a more complete narrative report. Eric Lease Morgan Number of items in the collection; 'How big is my corpus?' ---------------------------------------------------------- 65 Average length of all items measured in words; "More or less, how big is each item?" ------------------------------------------------------------------------------------ 9156 Average readability score of all items (0 = difficult; 100 = easy) ------------------------------------------------------------------ 49 Top 50 statistically significant keywords; "What is my collection about?" ------------------------------------------------------------------------- 65 Golgi 21 protein 14 Fig 13 cell 9 TGN 8 membrane 7 BFA 6 RNA 6 MHV 3 secretory 3 SARS 2 virus 2 vesicle 2 transport 2 oligosaccharide 2 inhibitor 2 glycoprotein 2 figure 2 VSV 2 Man 2 DPPIV 2 DPAP 2 COPI 2 Arf1 2 ARF1 1 viral 1 tube 1 transporter 1 structure 1 snare 1 signal 1 section 1 s33d 1 rhodopsin 1 replication 1 ras 1 peptide 1 p63 1 monensin 1 mg-160 1 lipid 1 link 1 granule 1 glycosyltransferase 1 gene 1 ganglioside 1 enzyme 1 effect 1 domain 1 dna Top 50 lemmatized nouns; "What is discussed?" --------------------------------------------- 8148 protein 5816 cell 4194 membrane 1939 virus 1596 domain 1400 vesicle 1358 transport 1203 complex 1191 pathway 1178 structure 1032 compartment 992 signal 917 glycoprotein 901 surface 894 receptor 894 enzyme 884 study 857 apparatus 849 type 849 formation 846 site 833 acid 819 lipid 809 % 780 sequence 773 role 763 localization 742 function 740 replication 728 interaction 722 residue 703 gene 668 region 658 activity 654 plasma 617 result 598 oligosaccharide 590 c 587 effect 581 antibody 580 sorting 577 infection 569 chain 553 fusion 552 mechanism 548 factor 547 coronavirus 543 retention 536 reticulum 531 molecule Top 50 proper nouns; "What are the names of persons or places?" -------------------------------------------------------------- 4927 Golgi 4474 al 3796 . 3642 et 1475 ER 1166 Fig 717 M 597 TGN 532 BFA 511 A 455 trans 433 RNA 426 MHV 416 II 355 C 349 - 330 S 311 N 295 cis 260 COPI 247 GA 244 DPAP 232 pH 231 SARS 231 IC 230 G 229 cisternae 227 B 226 VSV 219 Arf 196 GlcNAc 195 Kexlp 193 ras 184 monensin 179 SDS 174 Kre2p 167 H 162 A59 154 ALP 153 ARF1 151 GBF1 149 Arf1 146 K 145 PBS 139 vacuolar 137 HeLa 135 D 134 CoV 133 GTPase 132 IBV Top 50 personal pronouns nouns; "To whom are things referred?" ------------------------------------------------------------- 1538 it 847 we 607 they 445 i 128 them 82 itself 60 us 52 one 32 themselves 17 he 5 grasp55 4 me 3 rab8 3 p450s 3 earlier\ 2 tgn38 2 tbarf1 2 s 2 kre2p 1 tr]mt 1 s189 1 rab1b 1 ptdlns(4,5)p2 1 pp38-gfp 1 pmt3p 1 pis]methionine 1 p58 1 oneself 1 ofisgs 1 mrnas 1 mannose\ 1 log1 1 k(x)kxx 1 ile8 1 i"i20 1 her 1 hapg5p 1 gln37?ile 1 gate16 1 di(c24:)pc 1 connexin-26 1 clear^it 1 c16:0,c18:1)pc 1 apkb 1 -t3 Top 50 lemmatized verbs; "What do things do?" --------------------------------------------- 19380 be 3149 have 1444 show 1199 contain 1105 use 917 bind 797 require 757 suggest 756 do 700 involve 643 associate 618 link 607 find 575 form 547 indicate 520 occur 507 target 505 induce 486 inhibit 473 see 471 express 468 appear 464 mediate 447 describe 426 regulate 422 localize 412 determine 394 result 382 observe 373 include 372 follow 368 cause 366 label 350 demonstrate 350 bud 348 know 335 provide 327 sort 317 identify 316 interact 300 affect 298 infect 293 treat 292 synthesize 290 encode 288 lead 288 detect 275 block 270 produce 261 increase Top 50 lemmatized adjectives and adverbs; "How are things described?" --------------------------------------------------------------------- 2107 not 1404 also 1098 - 1071 secretory 965 viral 927 other 665 cytoplasmic 648 such 637 however 633 specific 593 different 581 only 511 more 502 intracellular 479 then 473 high 469 human 451 early 424 cellular 419 small 407 similar 393 large 390 complex 386 thus 384 same 383 well 375 structural 367 most 366 first 364 present 343 vesicular 343 molecular 342 further 340 dependent 333 several 313 important 305 as 302 distinct 291 anti 279 many 278 low 276 lysosomal 274 mutant 272 functional 266 therefore 253 mammalian 247 hydrophobic 244 single 232 major 227 like Top 50 lemmatized superlative adjectives; "How are things described to the extreme?" ------------------------------------------------------------------------- 152 most 83 least 35 Most 18 high 15 good 13 simple 11 large 8 strong 8 great 7 early 6 small 5 outermost 5 low 3 near 2 short 2 long 2 close 2 # 1 ~onophore 1 ~5-D 1 warm 1 rabaptin 1 rab7 1 mannose-6~hosphate 1 light 1 innermost 1 fast 1 easy 1 clear 1 OsO4 1 /Cpe 1 -which Top 50 lemmatized superlative adverbs; "How do things do to the extreme?" ------------------------------------------------------------------------ 215 most 67 least 23 well 1 early Top 50 Internet domains; "What Webbed places are alluded to in this corpus?" ---------------------------------------------------------------------------- 1 www.who.int 1 www.synapse-web.org 1 www.mbio.ncsu.edu 1 www.drugbank.ca 1 pbil.univ-lyon1.fr 1 lsbr.niams.nih.gov 1 doi.org 1 blast.ncbi.nlm.nih.gov 1 biorender.com 1 amira.zib.de 1 cran.r-project.org Top 50 URLs; "What is hyperlinked from this corpus?" ---------------------------------------------------- 1 http://www.who.int 1 http://www.synapse-web.org/tools/index.stm/ 1 http://www.mbio.ncsu.edu/bioedit/bioedit.html 1 http://www.drugbank.ca/ 1 http://pbil.univ-lyon1.fr/ 1 http://lsbr.niams.nih.gov/bsoft/ 1 http://doi.org/10.1083/jcb.202006005 1 http://blast.ncbi.nlm.nih.gov/Blast.cgi 1 http://biorender.com 1 http://amira.zib.de 1 http://CRAN.R-project.org/package=drc Top 50 email addresses; "Who are you gonna call?" ------------------------------------------------- 1 t.wileman@uea.ac.uk Top 50 positive assertions; "What sentences are in the shape of noun-verb-noun?" ------------------------------------------------------------------------------- 27 cells were then 16 proteins do not 12 protein was not 11 protein does not 11 protein is not 10 proteins are also 10 proteins did not 9 domain is sufficient 9 proteins are not 8 cells were pulse 7 cells expressing gml 6 complex requires only 5 cells expressing myc::sseg 5 complexes do not 5 domain is not 5 membrane is not 5 proteins were not 4 cells did not 4 cells do not 4 cells expressing s33d 4 cells were further 4 cells were transiently 4 domain was not 4 protein did not 4 protein is present 4 protein requires polar 4 protein was also 4 sites are not 4 sites is sufficient 4 vesicles mediating biosynthetic 3 cells are not 3 cells expressing s64d 3 cells were first 3 cells were subsequently 3 complex is not 3 complexes are freely 3 domain determine trans 3 domain did not 3 domain is important 3 er is not 3 pathway is not 3 protein has also 3 protein has not 3 protein was present 3 protein was still 3 proteins are more 3 proteins are selectively 3 proteins have not 3 proteins induce membrane 3 receptor mediated endocytosis Top 50 negative assertions; "What sentences are in the shape of noun-verb-no|not-noun?" --------------------------------------------------------------------------------------- 2 domain is not sufficient 2 receptors is not necessary 1 acid have not usually 1 cell is not too 1 cells are not able 1 cells was not artificially 1 cells was not significantly 1 complex are no longer 1 complex is not only 1 complex is not structurally 1 complexes were no longer 1 domain are not able 1 domain are not so 1 domain is not essential 1 domain was not critical 1 domain were not sufficient 1 domains show no sequence 1 enzymes have not yet 1 enzymes were not terminally 1 er is not evenly 1 formation are not easily 1 formation was not completely 1 glycoprotein was not necessary 1 golgi was not greatly 1 membrane is not absolute 1 membrane is not clear 1 membrane is not much 1 pathway is not essential 1 protein are not yet 1 protein does not nonspecifically 1 protein has no genuine 1 protein is not entirely 1 protein is not essential 1 protein is not necessary 1 protein is not present 1 protein showed no surface 1 protein was not aberrantly 1 protein was not detectably 1 proteins are no longer 1 proteins are not m 1 proteins are not rigid 1 proteins are not simply 1 proteins are not sufficient 1 proteins are not terminally 1 proteins do not transiently 1 proteins has no e}ect 1 proteins have no double 1 proteins have not yet 1 proteins show no evidence 1 proteins were not initially A rudimentary bibliography -------------------------- id = cord-272467-8heg5iql author = Armstrong, John title = Expression of coronavirus E1 and rotavirus VP10 membrane proteins from synthetic RNA date = 2004-02-19 keywords = Golgi; protein summary = We have expressed the cloned cDNA for glycoproteins from two such viruses, the E1 protein of coronavirus, which buds in the Golgi region, and VP10 protein of rotavirus, which assembles in the endoplasmic reticulum. We are investigating two viral model proteins, one for the endoplasmic reticulum and one for the Golgi complex, with a view to determining the features of each molecule responsible for its correct localisation. RNAs prepared by this method for VPlO and E l were translated efficiencly in reticulocyte lysates, Xenopus oocytes, and cultured CVl cells (Figs. However, not all of the viral protein is restricted to the flattened cisternae of the Golgi complex; some at least is found in smooth membranes which are in the same region of the cell but are in fact continuous with the rough endoplasmic reticulum [ 12, 221 . doi = 10.1002/jcb.240350206 id = cord-017866-h5ttoo0z author = Bowman, Grant R. title = Biogenesis of Dense-Core Secretory Granules date = 2010-05-27 keywords = DCG; Golgi; ISG; TGN; cell; granule; protein; secretory summary = For such regulated exocytosis, the vesicles that carry newly-synthesized protein from the TGN accumulate in the cytoplasm until specific extracellular events trigger their fusion with the plasma membrane, resulting in the release of vesicle contents.f The vesicles involved are called dense-core granules (DCGs), the name reflecting the fact that the contents are so highly condensed that they form a large electron-dense plug in the vesicle lumen. In support of this hypothesis, recent studies have suggested that prohormone convertases 1 and 2, which are responsible for proteolytic cleavageof lumenal proteins during granule maturation, are sorted to ISGs by virtue of C-terminal membrane raft-associated tails, which are by themselves necessary and sufficient for targeting to DCGs,uo 120 Additionally, cytoplasmic signals on some transmembrane proteins appear to play important roles in sorting, but the mechanisms are unknown. doi = 10.1007/978-0-387-93877-6_10 id = cord-104241-cqvnxsbo author = Bryant, Nia J. title = Two Separate Signals Act Independently to Localize a Yeast Late Golgi Membrane Protein through a Combination of Retrieval and Retention date = 1997-01-27 keywords = ALP; DPAP; Golgi; TGN summary = The yeast TGN is defined as the compartment where proteins destined for the cell surface are sorted from those destined for delivery to the vacuole, and contains the three processing proteinases involved in the maturation of the mating pheromone ␣ -factor (Kex2p, Kex1p, and Ste13p; also called dipeptidyl aminopeptidase A [DPAP A] 1 ; Bryant and Boyd, 1993; Nothwehr et al., 1993) , as well as the vacuolar protein sorting receptor (Vps10p; Marcusson et al., 1994; Cereghino et al., 1995; Cooper and Stevens, 1996) . By contrast, (⌬68-106)A-ALP behaved just like (F/A)A-ALP in that it localized to vacuolar membranes (Nothwehr et al., 1993; our unpublished results) and was processed with halftimes of ‫56-06ف‬ min in both wild-type and vps27 mutant cells ( Fig. 8 and Table III) presumably since it contains information to slow exit from the TGN. doi = nan id = cord-255981-3zvwu5bd author = Bui, Quynh Trang title = Large Arf1 guanine nucleotide exchange factors: evolution, domain structure, and roles in membrane trafficking and human disease date = 2009-08-11 keywords = Arf1; GBF; Gea; Golgi; Sec7 summary = The majority of these Arf1 GEFs are high molecular weight proteins, on the order of 200 kDa, and for this reason they have been referred to as the large Arf GEFs. The GBF/Gea and BIG/ Sec7 Arf1 GEFs function in internal membrane systems such as the Golgi apparatus, the trans-Golgi network (TGN) and endosomal pathways (Zhao et al. In this review, we will discuss the evolution of these Arf1 GEFs, and present an analysis of conserved domains that are common to both subfamilies as well as those that are speciWc to either the GBF/Gea or BIG/Sec7 proteins. As described previously, the large Arf1 GEFs have Wve major sequence homology domains that are common to members of both the GBF/Gea and the BIG/Sec7 subfamilies (Mouratou et al. The highly conserved sequence homology domains of the GBF/Gea and the BIG/Sec7 Arf1 GEFs suggest that they have important, conserved functions in evolution, and are likely to be involved in protein-protein interactions. doi = 10.1007/s00438-009-0473-3 id = cord-001082-sufwsu77 author = Bär, Séverine title = Vesicular Transport of Progeny Parvovirus Particles through ER and Golgi Regulates Maturation and Cytolysis date = 2013-09-19 keywords = Fig; Golgi; MVM summary = By colocalization with cellular marker proteins and specific modulation of the pathways through over-expression of variant effector genes transduced by recombinant adeno-associated virus vectors, we show that progeny PV particles become engulfed into COPII-vesicles in the endoplasmic reticulum (ER) and are transported through the Golgi to the plasma membrane. Moreover, a very limited reduction of secreted particles was observed with dnRab11, and nothing at all upon inhibition of Rab8, suggesting that PV particles take a different route from the Golgi apparatus to the plasma membrane as compared to GLuc. Due to their impact on MVM plaque morphology in A9 cells, the ERM family proteins moesin (Moe) and radixin (Rdx) have been implicated in the spreading capacity of this parvovirus [38] . doi = 10.1371/journal.ppat.1003605 id = cord-298251-u36lb44w author = Donaldson, Julie G. title = Arf Family G Proteins and their regulators: roles in membrane transport, development and disease date = 2011-05-18 keywords = ARF1; ARF6; GEF; Golgi; arf; protein summary = doi = 10.1038/nrm3117 id = cord-022313-2675sjlf author = Elbein, Alan D. title = The Use of Glycosylation Inhibitors to Study Glycoconjugate Function date = 2012-12-02 keywords = Golgi; Man; cell; inhibitor; link; oligosaccharide summary = Perhaps one control for some of these studies would be to use other inhibitors (i.e., cycloheximide or puromycin) that are known to block protein synthesis but do not affect carbohydrate synthesis or addition, or some other inhibitors that mod ify the structure of the carbohydrate chain, and compare the effects of these compounds with those of tunicamycin on the function of the particular glycoprotein. When various cultured animal cells are grown or incubated in the presence of this alkaloid, the processing of N-linked glycoproteins is blocked at the first step in the pathway (see Fig. 3 ), and the asparaginelinked glycoproteins have oligosaccharides mostly of the Glc 3 Man 7 _ 9 (GlcNAc) 2 structure. The sugar analog, 2-fluoro-2-deoxyglucose, which was previously shown to inhibit dolichyl-P-mannose formation and lipid-linked oligosaccha rides (154) , also altered the synthesis of the GPI-anchored protein alka line phosphatase in JEG-3 cells and caused the accumulation of a proform of the enzyme. doi = 10.1016/b978-0-12-589630-6.50009-5 id = cord-026010-61j07gq3 author = Elbein, Alan D. title = Alkaloid Glycosidase Inhibitors date = 2010-06-03 keywords = Golgi; Man; alkaloid; cell; glycoprotein; inhibitor; oligosaccharide summary = or b!mannosidase but instead proved to be an e}ective inhibitor of a!glucosidase\ with a level of activity only slightly less than that of castanospermine[ 21 Numerous additional examples of inhibitory speci_cities due to both naturally occurring alkaloids and synthetic analogues have further undermined this empirical approach and it is obvious that structureÐactivity correlations can only be developed with the aid of sophisticated molecular modeling techniques[ Molecular orbital calculations and molecular modeling have been applied to a series of known mannosidase inhibitors and others which were expected to inhibit but failed to do so[ The results showed that good inhibitors _t closely with a single low!energy conformer of the mannosyl cation and demonstrated that 5!epi!castanospermine did not comply with the structural requirements[ 65\66 The electronegative binding groups present in the inhibitor necessary for speci_city and activity were established\ as were those which were of little signi_cance[ Additional studies of this type should provide valuable information regarding the receptor sites on the various enzymes but the inhibition data available is compromised by the variability in enzymes and the conditions under which measurements have been made[ A comprehensive screening program using standardized conditions would provide much more useful information for structureÐactivity correlations and consequently the design of speci_c and potent inhibitors[ doi = 10.1016/b978-0-08-091283-7.00098-9 id = cord-102964-zh737cjk author = Ferraro, Francesco title = Modulation of endothelial organelle size as an antithrombotic strategy date = 2020-05-17 keywords = Ferraro; Golgi; VWF; WPB summary = Out of 1280 human licensed drugs we found 58 compounds fitting our criteria, with a variety of mechanisms of action consistent suggesting a number of pathways that influence biogenesis of WPBs. A quantitative high-throughput microscopy-based workflow, dubbed highthroughput morphometry (HTM), allows rapid quantification of the size of tens to hundreds of thousands of WPBs within thousands of endothelial cells (Ferraro et al., 2014) . We have previously shown that treatment of endothelial cells with two statins, simvastatin and fluvastatin, induces WPB size shortening, resulting in reduced adhesive properties of the VWF released by activated endothelial cells (HUVEC), measured by the reduced size of platelet-decorated VWF strings and by the recruitment of VWF from a flowing plasma pool (Ferraro et al., 2016) . Further to the potential toxicity associated with administration of drugs at high concentrations, we note that in vitro combination of WPB-size reducing treatments, acting through different mechanisms, can display synergy in the abatement of plasma VWF recruitment to the endothelial surface (Supplemental Figure 1) . doi = 10.1101/2020.05.16.099580 id = cord-293038-pjjvfdnq author = Fontana, Juan title = The unique architecture of Bunyamwera virus factories around the Golgi complex date = 2008-06-10 keywords = Fig; Golgi; RNA; tube; viral summary = We propose that this new structure, unique among enveloped viruses, assembles in association with the most stable component of Golgi stacks, the actin‐containing matrix scaffold, connecting viral replication and morphogenesis inside viral factories. Modified membranes harbouring viral replication complexes (RCs) frequently integrate into a complex structure known as the ''viral factory'' where the cytoskeleton participates, cell organelles are recruited and the different steps of the virus life cycle are sequentially connected. We propose that this new multifunctional structure associates with the actin-containing matrix of the Golgi stacks providing a stable scaffold for viral replication and early morphogenesis. LtA and CyD had very little or no effect, respectively, on viral replication and assembly as determined by measurement of infectious viral particles released to the culture supernatants at 6 and 10 h p.i. Complete tubes, virus budding profiles and viral particles assembled in Golgi stacks of cells treated with LtA, as observed in thin sections of treated cells studied by EM (not shown). doi = 10.1111/j.1462-5822.2008.01184.x id = cord-326015-ky4y2xjt author = Füllekrug, Joachim title = Protein sorting in the Golgi complex date = 1998-08-14 keywords = Golgi; protein summary = In this review, we will discuss sorting of resident proteins in the Golgi complex mainly in the context of cisternal maturation [1, 2] . An essential feature of this maturation model is the prediction that Golgi resident proteins are more concentrated in retrograde vesicles than they are in the cisternae of the Golgi apparatus. This shows that Golgi resident enzymes do form gradients across the pathway and that these are unique to the particular protein. The surprising ¢nding that the membrane spanning domain (MSD) of Golgi residents su¤ced to localise reporter molecules to the appropriate part of the pathway suggested that this domain harboured important sorting information (for review, see [22] ). As this form of coatomer is found on Golgi associated transport vesicles [50] , COP I vesicles constitute RTCs. The presence of K(X)KXX or related signals on membrane proteins other than ER residents allows for the possibility that this motif also acts later in the pathway. doi = 10.1016/s0167-4889(98)00048-2 id = cord-005034-wyipzwo4 author = Gleeson, Paul A. title = Targeting of proteins to the Golgi apparatus date = 1994 keywords = Golgi; TGN; domain; protein summary = These cytoplasmic domain sorting signals mediate interactions with coat structures of budding vesicles and thereby allow the selective vesicular transport of these membrane proteins between a variety of compartments [ 19] . Interestingly, the localization of ERGIC-53 (p53), a type I membrane protein of the intermediate compartment or CGN, requires a KKXX ER retention motif, again suggesting that the CGN may be an extension Overall, the localization signals of non-Golgi proteins are hydrophilic motifs located on either the cytoplasmic or luminal domains of the protein, and some of these signals have been shown to interact specifically with receptor molecules or with protein coats of budding vesicles. A common strategy has been employed by all groups to identify a putative Golgi retention signal(s) by analysing the localization, in transfected mammalian cells, of hybrid molecules containing limited sequences derived from Golgi glycosyltransferases. doi = 10.1007/bf00731273 id = cord-020788-a33vcapl author = Gottardi, Cara J. title = Signals and Mechanisms of Sorting in Epithelial Polarity date = 2008-05-22 keywords = Golgi; MDCK; cell; membrane; protein; signal summary = doi = 10.1016/s1569-2558(08)60020-x id = cord-022354-aqtceqqo author = HUNTER, ERIC title = Membrane Insertion and Transport of Viral Glycoproteins: A Mutational Analysis date = 2012-12-02 keywords = Golgi; RSV; membrane; protein; virus summary = doi = 10.1016/b978-0-12-203460-2.50007-x id = cord-352854-che3iwu3 author = Hart, Kristen C title = Derivatives of activated H-ras lacking C-terminal lipid modifications retain transforming ability if targeted to the correct subcellular location date = 1997-12-18 keywords = 61L; Golgi; ras summary = However, when examined in focus formation assays, transformation of NIH3T3 cells were seen with derivatives of ras(61L) containing a mutated E1 targeting sequence that results in plasma membrane localization. These results demonstrate that: (1) activated ras targeted to Golgi membranes is unable to cause transformation; (2) lipid modifications at the C-terminus are not required for the transforming activity of plasma membrane-anchored ras(61L) derivatives, and serve primarily a targeting function; (3) a transmembrane domain can effectively substitute for C-terminal modifications that would normally target ras to the inner surface of the plasma membrane, indicating that ras(61L) does not need to reversibly dissociate from the membrane as might be allowed by the normal lipidation; and (4) in order to function properly, there exists a critical distance that the ras protein must reside from the plasma membrane. doi = 10.1038/sj.onc.1200908 id = cord-271501-yjobthaj author = Hirschberg, Carlos B. title = Transporters of nucleotide sugars, nucleotide sulfate and ATP in the Golgi apparatus membrane: Where next? date = 1997-02-17 keywords = Golgi; transporter summary = UMP is the antiporter for all undine containing nucleotide sugars (Hirschberg and Snider, 1987; Waldman and Rudnick, 1990; Milla et al., 1992) ; thus, one would expect all these uridine nucleotide sugar transporters to have common structural features facing the lumenal and cytosolic side of the membrane. Recent evidence in mammals and yeast suggests that Golgi membrane transporters play a regulatory role in determining which macromolecules undergo specific posttranslational modifications in the lumen of the Golgi apparatus (Abeijon et al., 1993; Toma et al., 1996) . A combination of genetics and overexpression of wild-type and mutant transporter proteins followed by reconstitution into liposomes should allow determination of structural motifs required for membrane insertion, nucleotide recognition, and specific sugar translocation. What structural features determine that these transporters become localized in the Golgi apparatus and/or the endoplasmic reticulum and not another organelle? doi = 10.1093/glycob/7.2.169 id = cord-264996-og3sg0qw author = Howell, Gareth J. title = Cell Biology of Membrane Trafficking in Human Disease date = 2006-09-17 keywords = COPII; Golgi; TGN; cell; disease; gene; membrane; protein; snare; transport; vesicle summary = Many of these transport intermediates or vesicles, whether derived from the ER, other internal organelles, or the plasma membrane, are ''''coated'''' with unique protein complexes, tethering factors, and regulatory factors that ensure correct targeting to an acceptor compartment. Breast cancer Caveolin-1 Deletion or dominant negative mutation of caveolin-1 promotes tumor progression Breast cancer (Bouras et al., 2004; Williams and Lisanti, 2005) (Hayasaka et al., 1993; Matsuyama et al., 2002) Chediak-Higashi syndrome (CHS) CHS1/Lyst Lyst involved in regulation of protein secretion from lysosomes -enlarged lysosomes Partial albinism, recurrent bacterial infections, impaired chemotaxis and abnormal natural killer cell function (Shiflett et al., 2002; Ward et al., 2003) 214500 Choroideremia (CHM) Rab Escort Protein 1 (REP1) RAB27a remains cytosolic due to defective geranylgeranyl modification in CHM lymphoblasts X-linked form of retinal degeneration 303100 Various mechanisms control the traYcking of proteins from the TGN by the formation and delivery of membrane-derived transport vesicles to the plasma membrane, endosomes, or lysosomal structures (Ponnambalam and Baldwin, 2003) . doi = 10.1016/s0074-7696(06)52005-4 id = cord-306067-ldn17pj8 author = Inoue, Satoshi title = Assembly of the silk fibroin elementary unit in endoplasmic reticulum and a role of L‐chain for protection of α1,2‐mannose residues in N‐linked oligosaccharide chains of fibrohexamerin/P25 date = 2003-12-19 keywords = Golgi; P25 summary = These results suggest that the 30-kDa component is the ER form of fhx/P25 and the 27-kDa component represents fhx/P25 whose N-linked oligosaccharide chains lost their terminal a1,2-mannose residues by digestion with a1,2-manosidases in Golgi complex, and further imply that fhx/P25 in the elementary unit of the normal-level fibroin-producing breeds is largely resistant to the action of a1,2-mannosidases in Golgi complex and secreted as the ER-type 30-kDa form. It is thus conceivable that in the Nd-s D mutant silkworm, fhx/P25 in the L-chain-free H 6 fhx 1 -type elementary unit (Table 2) is processed efficiently by the action of Golgi a1,2-mannosidases to yield only the 27-kDa molecule in the secreted fibroin. In order to examine a role of L-chain in the protection of a1,2-mannose residues of fhx/P25 in the elementary unit, the Nd-s D mutant silkworm was subjected to transgenesis with the normal L-chain promoter/cDNA sequence together with a marker gene of DsRed2 (Fig. 4A) , and two transgenic lines L6 · 7 and L7-4 were selected. doi = 10.1046/j.1432-1033.2003.03934.x id = cord-018572-e2qq4ngq author = Jackson, Catherine L. title = Arf Proteins and Their Regulators: At the Interface Between Membrane Lipids and the Protein Trafficking Machinery date = 2014-05-22 keywords = Arf; Arf1; Arf6; COPI; Golgi summary = This feature is conserved in modern organisms, for example, in humans, which have only 5 Arf proteins, yet at least 15 GEFs and 31 GAPs. Perhaps a clue as to the Arf4 TGN VxPx targeting motif AP adaptor protein, BAR Bin/Amphiphysin/Rvs, CC coiled-coil, COP coatomer protein, ER endoplasmic reticulum, ERGIC ER-Golgi intermediate compartment, GAT GGA (Golgi-localized, γ-adaptin homologous, ADP-ribosylation factor-binding protein) and TOM1 homologous, GRAB GRIP (golgin-97/RabBP2α/Imh1p/p230)-related Arf binding, PM plasma membrane, TGN trans-Golgi network; ND, not determined nature of the primordial Arf protein comes from the protozoan parasite Trypanosoma brucei, which expresses a single Arf protein that has characteristics of both Class I and Class III mammalian Arfs. How a single Arf protein can recruit multiple coats to different membrane sites in cells is still not fully understood, but one important contribution to specificity comes from the Arf GEFs. In both mammalian and yeast cells, GBF1 and Gea1/2, respectively, interact directly with COPI (Deng et al. doi = 10.1007/978-3-319-07761-1_8 id = cord-255027-xsuialnn author = Kellokumpu, Sakari title = Glycosyltransferase complexes in eukaryotes: long-known, prevalent but still unrecognized date = 2015-10-17 keywords = Golgi; complex; enzyme; glycosyltransferase summary = One of the first examples of these was the observation that a soluble lactose synthase (LS, EC 2.4.1.22, for enzyme names and definitions, see Table 1 ) typically found in bovine milk consists of two The term ''''complex'''' is used in this review to define a functional assembly of two or more similar (homomer) or dissimilar (heteromer) glycosyltransferases that interact with each other and in the case of the latter, typically act sequentially during glycan synthesis. Yeast N-glycosyltransferase complexes The yeast N-glycosylation pathway shows a high degree of pathway conservation with higher eukaryotes, involving similar oligosaccharide-dolichol precursor synthesis, glycan transfer to nascent proteins by an oligosaccharyltransferase (OST) complex, and removal in the endoplasmic reticulum (ER) of the three glucoses and the central-arm a1,2-linked Man from the newly transferred Glc 3 Man 9 GlcNAc 2 [1, 2, [13] [14] [15] . doi = 10.1007/s00018-015-2066-0 id = cord-309384-vlk8cebh author = Kolter, Thomas title = Ganglioside Biochemistry date = 2012-12-19 keywords = GM1; GM2; GM3; Golgi; Tay; acid; cell; figure; ganglioside; membrane; protein summary = A principal difference between ganglioside biosynthesis in the Golgi apparatus and degradation in the endolysosomal compartment is that during GSL formation, membranebound glycosyltransferases interact with their membranebound glycolipid substrates by diffusion within the twodimensional plane of the lipid bilayer. As glycosidase substrates, GSLs with four carbohydrate residues or less require the additional presence of small lipid binding glycoproteins, either the GM2 activator protein or one of the four saposins A-D. In vitro, in addition to enzymes and activator proteins, also an appropriate membrane-lipid composition of the ganglioside-containing membrane is required for degradation [222] . Due to the deficiency of two enzyme activities, β-hexosaminidases A and B, storage of negatively charged glycolipids characteristic for Tay-Sachs disease and, in addition, of uncharged substrates such as GA2 in the brain and globoside in visceral organs (Figure 16 ) is observed. doi = 10.5402/2012/506160 id = cord-296416-q0rsfzgw author = LAVI, EHUD title = Syncytia Formation Induced by Coronavirus Infection Is Associated with Fragmentation and Rearrangement of the Golgi Apparatus date = 1996-07-15 keywords = BFA; Golgi; MHV summary = In many 3-5 hr after infection, individual elements of the GA, cells the secretion blocker Brefeldin A (BFA) reversibly which are associated initially with separate microtubuleredistributes membranes and enzymes of the GA back organizing centers in perinuclear areas of fused cells, into the RER, but does not inhibit endocytosis (Doms et congregate in the center of syncytia and form an exal., 1989; Lippincott-Schwartz et al., 1989; Johnston et al., tended network of nondisrupted intact Golgi complexes 1994). In this study, we used organ-Immunohistochemistry elle-specific antibodies, immunohistochemistry, and transmission electron microscopy to examine the fate of Cells, grown on poly-D-lysine-treated coverslips, were the GA during cell fusion and syncytia formation in mouse fixed with 2% paraformaldehyde for 20 min at room tem-L-2 cells infected with MHV-A59 and fusion defective perature, washed three times in PBS, then incubated for mutants. doi = 10.1006/viro.1996.0382 id = cord-007353-qg2pb884 author = Lavi, Ehud title = Polarity of processes with Golgi apparatus in a subpopulation of type I astrocytes date = 1994-06-06 keywords = BFA; Golgi; mg-160 summary = In order to further investigate which type of astrocytes contain GA in processes we conducted the present study using primary cultures of rat astrocytes and organelle specific antibodies against the GA and the rough endoplasmic reticulum (RER). In a previous ultrastructural, immunocytochemical study from this laboratory, using affinity-purified polyclonal sera specific for the GA, elements of the organelle were detected in peripheral segments of some astrocytic processes in sections of rat brains [68] . Over 95% of the cultured cells stained with the monoclonal antibody against GFAP [43] , an astrocyte specific intermediate filament protein. Staining of MG-160 in processes in rat astrocyte enriched cultures was detected by immunohistochemistry and immunofluorescence with both polyclonal and monoclonal antibodies against MG-160. To confirm that cells which expressed MG-160 in processes were astrocytes, double-labeling immunofluorescence with anti-MG-160 and astrocytic-specific intermediate filament marker (GFAP) antibodies were performed. doi = 10.1016/0006-8993(94)91327-7 id = cord-323331-80d01l6f author = Li, Jie title = Golgi Structure and Function in Health, Stress, and Diseases date = 2019-01-01 keywords = GM130; GRASP65; Golgi; TGN; Wang; protein summary = Mechanistically, GRASP proteins form homodimers via the N-terminal PDZ domains, and dimers from adjacent Golgi cisternae further oligomerize in trans and function as the "glue" that tethers the cisternae into a stack (Wang et al. Other than the well-studied GRASP65-GM130 and GM130-p115-giantin complexes, the GRIP domain containing golgins are another group of proteins associated with the Golgi structure. Depletion of αSNAP in p53 null or Bax null cells still results in apoptosis, indicating that the anti-apoptotic function is independent of p53 and Bax. Interestingly, αSNAP depletion induces apoptosis independent of the cleavage of Golgi proteins such as GRASP65, golgin-160, and p115 but rather by dysregulation of ER-Golgi vesicle cycling and possibly through ER stress (Naydenov et al. The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis doi = 10.1007/978-3-030-23173-6_19 id = cord-003761-ikni2acz author = Li, Zengbin title = Biological Function and Application of Picornaviral 2B Protein: A New Target for Antiviral Drug Development date = 2019-06-04 keywords = FMDV; Golgi; protein summary = In this review, we mainly summarize recent research data on the viroporin or viroporin-like activity of 2B proteins, which affects the biological function of the membrane, regulates cell death, and affects the host immune response. In particular, the 2B protein may change the Ca 2+ concentration to regulate autophagy and apoptosiswhich are distinct cell death mechanisms controlled by the virus to effectively evade the host immunity, thereby promoting viral replication and release [48] [49] [50] [51] [52] . Thus, the main points of focus for research on the structure and function of the 2B protein toward ultimate drug development are: (1) mechanism of increasing membrane permeability to disturb the ion balance, (2) regulation of autophagy and apoptosis, (3) inhibition of the host immune response, and (4) promotion of viral replication and release. doi = 10.3390/v11060510 id = cord-322516-wekvet6f author = Maceyka, Michael title = Ceramide Accumulation Uncovers a Cycling Pathway for the cis-Golgi Network Marker, Infectious Bronchitis Virus M Protein date = 1997-12-15 keywords = Golgi; IBV; PDMP summary = Short-term treatment with two inhibitors of sphingolipid synthesis had no effect on localization of IBV M or other Golgi markers. Treatment of cells with 100 M PDMP for 1 h had no effect on the localization of either protein (Fig. 4) , suggesting that the morphology of the Golgi was not greatly altered. Pretreatment with the earlier inhibitors reduced the PDMP-induced slowing of anterograde traffic by about half, suggesting that accumulation of newly synthesized ceramide at least partially mediates this effect. The pretreatment experiments suggested that increased levels of ceramide mediate the PDMP-induced effects on IBV M localization. However, neither ␤CA nor FB1 had an effect on the rate of anterograde traffic of VSV G or the localization of IC, CGN, or Golgi stack proteins. However, the glucosylceramide analogue PDMP, at a concentration that inhibits both GlcCer and SM synthases, causes a redistribution of IBV M to the ER and a slowing of anterograde traffic in BHK-21 cells. doi = nan id = cord-022499-7d58f1k3 author = Mall, Sanjay title = Transmembrane α helices date = 2004-01-07 keywords = Golgi; bilayer; lipid; peptide; protein summary = For example, if effects were averaged over three shells of lipids, changes in fatty acyl chain lengths by 4 and 10 carbons from that giving optimal interaction would decrease lipid-protein binding constants by factors of 1.6 and 21, respectively. These results suggest that the effects of charge on the interactions between phospholipids and transmembrane ot helices will often be rather small and will be strongly dependent on the detailed structure of the peptide and its orientation in the membrane. However, there is evidence for the presence of a small number of "special" anionic phospholipids binding to some membrane proteins, acting as "cofactors." An example is provided by cytochrome c oxidase, whose crystal structure shows the presence of a lipid molecule bound between the transmembrane a helices (Iwata et al., 1995) . It could therefore be that matching of the thickness of the lipid bilayer and the transmembrane length of the protein is important in retention in ER, as was suggested for the Golgi complex. doi = 10.1016/s1063-5823(02)52014-7 id = cord-004521-25t4s7fr author = Marie, M. title = Membrane traffic in the secretory pathway: Take the ’A’ train: on fast tracks to the cell surface date = 2008-08-26 keywords = BFA; Golgi; TGN; cell summary = Typical for this transport is (i) its insensitivity to brefeldin A (BFA), which dissociates selected coat complexes from membranes, resulting in the disassembly of the Golgi apparatus; (ii) its rapid kinetics as compared to the classical secretory pathway; and (iii) its role in the trafficking of lipid raft components. COPII coats function at ER exit sites in the initial export of cargo from the ER [22, 23] , COPI coats operate in forward transport and recycling in the IC and cis-Golgi membranes [24] , while clathrin and associated adaptor proteins (AP1, AP3, AP4, GGA) localize variably to trans-Golgi/TGN and endosomes [25] . However, since different cargo proteins display variable localization in the 20 o C-treated cells, it remained unclear whether they are arrested in a specialized trans-Golgi secretory organelle, or within a complex membrane system located at the crossroads of the exocytic and endocytic pathways [127, 130, 9a] . doi = 10.1007/s00018-008-8355-0 id = cord-287815-alv30uk5 author = Mellman, Ira title = The Golgi complex: In vitro veritas? date = 1992-03-06 keywords = CGN; Golgi; TGN; transport summary = As we have seen, there are three key elements underlying our general view of the Golgi: that the Golgi consists of several discrete compartments (cis, medial, trans, and TGN) corresponding to individual or groups of cisternae; that transit between these compartments occurs viavesicular carriers; and that the transport process is inherently nonselective with respect to the passenger proteins. While distinct from the CGN or TGN, we assume that the medial cisternae represent a single functionally continuous compartment, irrespective of the actual number of physically separate cisternal elements in any one Golgi complex. Given that VSV G protein in early Golgi compartments was transported with the highest efficiency (Fries and Rothman, 1981) the transport event assayed was postulated to reflect the formation of vesicles from cis (early) cisternae and the fusion of these vesicles with medial cisternae (which contain the GlcNAc transferase) (Rothman and Orci, 1990) (Figure 4) . doi = 10.1016/0092-8674(92)90027-a id = cord-016971-7esuj4ye author = Mironov, Alexander A. title = The Golgi apparatus and main discoveries in the field of intracellular transport date = 2008 keywords = Golgi summary = 1964) 1964 GERL concept (Novikoff 1964) 1964 Isolation of Golgi membranes from cells (Morr e and Mollenhauer 1964) 1964 The process of sulphation in the GA (Godman and Lane 1964) 1966 The sugar-nucleotide transport from the cytosol to the Golgi lumen across the Golgi membranes, the role of the GA in glycosylation (Neutra and Leblond 1966) 1966 The origin of lysosomes and the function of clathrin-coated vesicles during protein absorption (Bainton and Farquhar 1966; Friend and Farquhar 1967) 1967 The intracellular transport (Jamieson and Palade 1967a,b) 1969 Galactosyltransferase as a Golgi marker (Whur et al. 1990 ) 1990 The main genes involved in intracellular transport, the genetic evidence in favour of the vesicular model of the transport in yeast (Kaiser and Schekman 1990) 1991 A Golgi retention signal in the membrane-spanning domain (Swift and Machamer 1991) 1993 The role of oligomerization for the retention of Golgi enzymes (Weisz et al. doi = 10.1007/978-3-211-76310-0_2 id = cord-009371-ub4p4ngr author = Mollenhauer, Hilton H. title = Alteration of intracellular traffic by monensin; mechanism, specificity and relationship to toxicity date = 1990-05-07 keywords = Clsternae; Golgi; apparatus; cell; effect; membrane; monensin summary = doi = 10.1016/0304-4157(90)90008-z id = cord-022774-wasdp2gh author = Morré, D. James title = Identification of the 16°C compartment of the endoplasmic reticulum in rat liver and cultured hamster kidney cells date = 2012-02-07 keywords = Golgi summary = The findings show parallel responses between the temperature dependency of transition vesicle formation in vitro and in situ and suggest that a subpopulation of the transitional endoplasmic reticulum may be morphologically and functionally homologous to the 16°C compartment observed in virally‐infected cell lines grown at low temperatures. Studies were then conducted with isolated transitional endoplasmic reticulum fractions from rat liver to determine if a similar mechanism of control by temperature of transition vesicle formation could be duplicated in the cell-free system. With further increases in temperature, the numbers of transition vesicles appeared to be increased slightly but the tubular elements of the endoplasmic reticulum did not reappear within the Golgi apparatus zone. Numbers of transition vesicles were approximately doubled relative to the control preparations and the peripheral cytoplasm contained numerous tubular transition elements of the endoplasmic reticulum similar in appearance to those observed with incubation at 16°C (Fig. 7A) . doi = 10.1111/j.1768-322x.1989.tb03009.x id = cord-265887-g5zhoyo9 author = Mukherjee, Shruti title = Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain date = 2020-08-11 keywords = Golgi; SARS; membrane; protein summary = (56) Apart from these highly conserved sequences throughout the genus, there are distinct potent glycosylation sites along the stretch that can serve as chaperone interacting motifs to help in the protein folding and/or aid in J o u r n a l P r e -p r o o f Journal Pre-proof trafficking along with the cellular machinery.(57) Glycosylation of particular asparagine residues (Asn 45, Asn 48, Asn 64, and Asn 68) in the SARS-CoV has been shown to be crucial in maintaining the proteinoligomerization events associated with the host membranes. (41) The formation of a disulfide bond may also play a crucial role in the oligomerization of the E protein, forming stable dimers, trimers, and pentamers depending on its functional requirement.(105) Thus even though the TMD spans the lipid bilayer, the CxxC motif could serve as an essential key to defining the membrane-associated oligomerization events-providing newer targets for preemptive therapeutic intervention. doi = 10.1016/j.bpc.2020.106452 id = cord-007261-b5fgb9wf author = Murakami, Kazuya title = The Transmembrane Region of Microsomal Cytochrome P450 Identified as the Endoplasmic Reticulum Retention Signal(1) date = 1994-07-17 keywords = Golgi; Sec summary = Another chimeric protein construct in which carboxyesterase Sec was connected to the C-terminal region of rat UDP-glucuronosyltransferase (UDP-GT), that contained a double-lysin ER retention motif, was also located in the ER, as determined from the endo H sensitivity and immunofluorescence staining. As a control, other types of fusion proteins were constructed in which the C-terminal portion of UDPglucronosyltransferase, which contains the double-lysine motif for the ER retention, was attached to carboxyesterase Sec. The fusion proteins were expressed in COS cells, and the subcellular localization of the fusion proteins was determined. To determine whether P450s are retained permanently in the ER or recycled between the ER and post-ER compartments through the "export and retrieval" process, we chose a lysosomal enzyme, cathepsin D, as a reporter, which was fused to the N-terminus of P450 at the DNA level and the fusion protein was expressed in COS cells. doi = 10.1093/oxfordjournals.jbchem.a124489 id = cord-253466-7gpije5d author = Netherton, Christopher title = A Guide to Viral Inclusions, Membrane Rearrangements, Factories, and Viroplasm Produced During Virus Replication date = 2007-08-31 keywords = ASFV; Fig; Golgi; Poliovirus; RNA; african; dna; protein; replication; virus summary = Significantly, Poliovirus infection causes enrichment of GEFs in membranes containing replicase proteins, and this would provide a mechanism for increasing levels of Arf1-GTP at sites of virus replication. There is evidence that Tobacco mosaic virus also uses the ER as a site of replication because the replicase enzyme and viral RNA are located on the ER of infected cells, and infection causes major changes in ER morphology (Reichel and Beachy, 1998) , including ER aggregation and formation of lamella structures. Even though these viruses infect a diverse range of hosts from different phyla, including vertebrates [poxviruses, African swine fever virus (ASFV)], arthropods (entomopox, ASFV, chloriridoviruses), amphibians and fish (Ranavirus, Megalocytivirus, and Lymphocystivirus genera of the Iridoviridae family), marine algae (phycodnaviruses), and protozoa (mimivirus), they all generate cytoplasmic factories as major sites of virus assembly and replication (illustrated in Fig. 4 ). Formation of DNA replication structures in herpes virus-infected cells requires a viral DNA binding protein doi = 10.1016/s0065-3527(07)70004-0 id = cord-276358-so390gp4 author = Nieto-Torres, Jose L. title = Severe acute respiratory syndrome coronavirus E protein transports calcium ions and activates the NLRP3 inflammasome date = 2015-11-30 keywords = Golgi; SARS summary = title: Severe acute respiratory syndrome coronavirus E protein transports calcium ions and activates the NLRP3 inflammasome In this report, we demonstrate that SARS-CoV E protein forms protein–lipid channels in ERGIC/Golgi membranes that are permeable to calcium ions, a highly relevant feature never reported before. Previously, we reported that SARS-CoV E protein showed mild selectivity for cations (Na þ and K þ ) when reconstituted in ERGIC/ Golgi membranes, mostly conferred by the negative charges of the lipids (Verdia-Baguena et al., 2012 . Synthetic peptides representing the full-length SARS-CoV E protein, or its transmembrane domain (amino acids 7-38) containing point mutations that inhibited ion channel activity (N15A and V25F), were generated by standard phase synthesis and purified by HPLC, as previously described (Verdia-Baguena et al., 2012) . Severe acute respiratory syndrome-associated coronavirus 3a protein forms an ion channel and modulates virus release Severe acute respiratory syndrome coronavirus envelope protein ion channel activity promotes virus fitness and pathogenesis doi = 10.1016/j.virol.2015.08.010 id = cord-332484-qy8vj6uu author = Pierini, Roberto title = Modulation of membrane traffic between endoplasmic reticulum, ERGIC and Golgi to generate compartments for the replication of bacteria and viruses date = 2009-04-01 keywords = Golgi; RNA summary = This review describes examples where both intracellular bacteria (Salmonella, Chlamydia and Legionella) and viruses (picornaviruses and hepatitis C) recruit membrane vesicles to sites of replication by modulating proteins that control the secretory pathway. Intracellular bacteria remain within membrane-bound vacuoles to avoid delivery to lysosomes and then recruit vesicles from the secretory pathway to provide nutrients necessary for microbial growth and cell division. Many viruses generate densely packed membrane vesicles to shield them from recognition by cellular defence pathways that recognise double-stranded RNA, and at the same time the membranes provide a platform to recruit viral and host proteins required for replication [3] [4] [5] . This review describes how recent work on intracellular bacteria such as Salmonella, Chlamydia and Leigionella draws parallels with studies on (+) strand RNA viruses where microbial proteins recruit membranes by modulating proteins that control the secretory pathway. doi = 10.1016/j.semcdb.2009.03.015 id = cord-022235-6ircruag author = Pugsley, Anthony P. title = Later stages in the eukaryotic secretory pathway date = 2012-12-02 keywords = Golgi; TGN; cell; protein; secretory; section summary = doi = 10.1016/b978-0-12-566770-8.50009-4 id = cord-257754-pqxkyg8z author = Reggiori, Fulvio title = Membrane Origin for Autophagy date = 2006-07-21 keywords = Cvt; Golgi; Klionsky; Reggiori; membrane summary = In addition, a study analyzing conditional knock-out mice defective for autophagy has revealed that the mutant animal accumulates numerous ubiquitinated aggregates in the cytosol, suggesting that this covalent protein modification could serve to specifically target to autophagosomes large structures that have to be eliminated (Komatsu et al., 2005) . In contrast to mammalian cells where several isolation membranes can be simultaneously activated, a single perivacuolar site of organization for double-membrane vesicle formation (named the pre-autophagosomal structure, PAS) is observed in the yeast S. Because the three mammalian Atg8 homologs are diVerently expressed in various tissues (Tanida et al., 2004) , another intriguing option is that these proteins are involved in supplying the autophagosome with membranes derived from diVerent compartments depending on the cell type; for example, GATE-16 from the Golgi complex and GABARAP from the same organelle as well as the synaptic cisternae (Kittler et al., 2001; Kneussel et al., 2000; Sagiv et al., 2000) . doi = 10.1016/s0070-2153(06)74001-7 id = cord-264468-3oxzzxnd author = Salcedo, Suzana P. title = SseG, a virulence protein that targets Salmonella to the Golgi network date = 2003-10-01 keywords = BFA; Golgi; SCV; Salmonella; figure summary = Similar results were obtained using an antibody against TGN46, a glycoprotein the subcellular localization of GFP-expressing wild-type S.typhimurium (wt-GFP, green) in relation to the cis-Golgi protein giantin (red), and the host cell (DIC in merged image), 8 h after invasion. Since SseG is required for both Golgi localization of bacteria and intracellular replication, we hypothesized that the Golgi network might be exploited by Confocal immuno¯uorescence microscopy of HeLa cells infected for 10 h by GFP-expressing wild-type strain or the sseG mutant as a control. The protein was concentrated in a perinuclear region, where it co-localized extensively with Golgi markers including giantin (data not shown) and Cells expressing a myc-tagged version of SseG (green) were co-labelled with an antibody against TGN46 (red), and examined by confocal microscopy. HeLa cells expressing myc::SseG were incubated with BFA and ®xed for immuno¯uorescence The translocation of the SPI-2 TTSS effector SifA is required for recruitment of lgp-containing vesicles and the formation of Sifs, while SseG localizes SCVs to the Golgi network. doi = 10.1093/emboj/cdg517 id = cord-298503-l60cdllh author = Saraste, J. title = Intermediate Compartment: A Sorting Station between the Endoplasmic Reticulum and the Golgi Apparatus date = 2015-08-20 keywords = COPI; ERGIC-53; Golgi summary = doi = 10.1016/b978-0-12-394447-4.20013-8 id = cord-287477-aios0h8s author = Sicari, Daria title = Role of the early secretory pathway in SARS-CoV-2 infection date = 2020-07-28 keywords = Golgi; SARS; protein summary = CoV-2 infection starts when its spike (S) protein binds to angiotensin I-converting enzyme 2 (ACE2) receptors on the host cell membrane (Lake, 2020; Letko et al., 2020) . Thus, virion spread critically depends on recruiting the most efficient secretory machineries of host cells (Su et al., 2016; Proteins of the early secretory pathway bound by SARS-CoV-2 As the entire world asks for ways to stop CoV-2, many laboratories are investigating the virus''s Achilles heel(s). The role of glycosylation and protein quality control in SARS-CoV-2 infections Most CoVs bud at the ERGIC level ( Fig. 1) and are then transported along the exocytic pathway (Klumperman et al., 1994; Stertz et al., 2007) . We observed enrichment for five host-derived virus-interacting proteins (GOLGB1, PDE4DIP, TOR1A, HMOX1, and HYOU1) involved in different processes and related to quality control and ER-Golgi homeostasis maintenance. doi = 10.1083/jcb.202006005 id = cord-268527-wbfnhedy author = Smith, Sylvia B. title = Transient hyperglycosylation of rhodopsin with galactose date = 1991-10-31 keywords = Golgi; RCA; ROS; rhodopsin summary = doi = 10.1016/0014-4835(91)90170-j id = cord-008590-xivnsldf author = Tartakoff, Alan M. title = The Confined Function Model of the Golgi Complex: Center for Ordered Processing of Biosynthetic Products of the Rough Endoplasmic Reticulum date = 2008-04-14 keywords = Golgi; ICT; RER; cell summary = These cisternae, in conjunction with other associated smoothsurfaced membranes, are responsible for executing net unidirectional intracellular transport (ICT) from the rough endoplasmic reticulum (RER) toward more distally located structures, e.g., lysosomes and the cell surface (24, 35, 40, 47, 85, 1 1 1, 134) . If they do not, given appropriate control experiments, they may be assigned to relatively late sub compartment^.^ The first indications that the site of interruption of ICT by monensin lies only part way across the GC came from study of the progress of N-linked oligosaccharide maturation of Ig (139) ; however, a recent use of monensin should be mentioned since it adds independent support for this idea (37) . The approaches used involved study of the effect of agents which block secretory protein exit from the RER (e.g., uncouplers) (130), correlation between the kinetics of ICT and cleavage, or, best of all, analysis of smooth microsomal or Golgi-enriched subcellular fractions [e.g., of hepatocytes (92, 102) or virally infected cells (68) ]. doi = 10.1016/s0074-7696(08)62374-8 id = cord-292688-w4zvfkyl author = Tooze, Sharon A title = Biogenesis of secretory granules in the trans-Golgi network of neuroendocrine and endocrine cells date = 1998-08-14 keywords = Golgi; TGN; protein; secretory summary = An alternative hypothesis is that there is very little constitutive secretion originating from the TGN of regulated cells, and that most molecules in the biosynthetic pathway exit into ISGs. In the ISG, the non-secretory granule proteins would presumably be sorted from the regulated secretory proteins via interaction with a receptor and removed from the ISG in constitutive-like vesicles. Depending on the cargo, distinct mechanisms could be used for selection to increase the e¤ciency of removal of nonsecretory granule proteins from the maturing ISGs. While the mechanisms involved in the formation of both constitutive and regulated secretory vesicles from the TGN is largely unknown there have been recent reports which suggest that both these budding reactions maybe unique in that they function independently of known coat proteins. In the PC12 cell assay, the same e¡ect was observed with [AlF 4 ] À and several other lines of evidence demonstrated that heterotrimeric GTP-binding proteins are involved in the regulation of post-Golgi vesicle formation (see [71] for review). doi = 10.1016/s0167-4889(98)00059-7 id = cord-303153-z7bdiuvx author = Ulasli, Mustafa title = Qualitative and quantitative ultrastructural analysis of the membrane rearrangements induced by coronavirus date = 2010-01-20 keywords = Fig; Golgi; MHV; RNA summary = doi = 10.1111/j.1462-5822.2010.01437.x id = cord-277566-j3ehiwn9 author = Verheije, Monique H. title = Mouse Hepatitis Coronavirus RNA Replication Depends on GBF1-Mediated ARF1 Activation date = 2008-06-13 keywords = ARF1; BFA; GBF1; Golgi; MHV; RNA summary = Here, we study the involvement of the secretory pathway in mouse hepatitis coronavirus (MHV) replication by using the drug brefeldin A (BFA), which is known to interfere with ER-Golgi membrane traffic by inhibiting the activation of ADP-ribosylation factor (ARF) small GTPases. Therefore, LR7 cells infected with MHV-A59 were treated with BFA for 30 minutes starting 5.5 h p.i. They were subsequently fixed and processed for immunofluorescence using antibodies both against nsp8, which served as a protein marker for the MHV replication sites [50, 51] , and against the viral structural protein M, known to reside in the Golgi [52] . In complete agreement with the luciferase expression data shown above, this result demonstrates that BFA inhibits, but does not completely block, the formation of RCs. To study the effects of BFA on the DMVs at an ultrastructural level, MHV-infected LR7 cells were fixed at 6 h p.i. and embedded in Epon resin in order to be analyzed by electron microscopy. doi = 10.1371/journal.ppat.1000088 id = cord-313694-p2sgaypq author = West, Christopher M. title = Current ideas on the significance of protein glycosylation date = 1986 keywords = Golgi; carbohydrate; cell; glycoprotein; protein; structure summary = The alternate view is that carbohydrate structures participate in numerous specific interactions with discrete protein receptors, and that these interactions lead to predictable modifications in the localization or activity of the glycoprotein. The notion of a ''non-specific'' role for carbohydrate has received perhaps its strongest support from studies on cells whose glycosylation processes have been globally altered by mutation or drugs. Consideration of the possible role of carbohydrate in other molecular associations with the plasma membrane will be considered below in sections on hormone-receptor interactions and cellsubstratum (e.g., extracellular matrix) and cell-cell adhesion. Considerable evidence has been adduced that various parasites such as viruses, bacteria, protozoa, etc., possess carbohydrate binding proteins which can interact with sugar structures on the surfaces of cells with which the parasites associate (167, 168, (116) (117) (118) (119) . In any case, antibodies and lectins may model potential receptors in cells which might specifically recognize carbohydrate-associated structures. doi = 10.1007/bf00230632 id = cord-269011-230p8rsf author = de Haan, Cornelis A.M. title = Molecular Interactions in the Assembly of Coronaviruses date = 2005-08-31 keywords = Golgi; MHV; RNA; protein summary = Biochemical and theoretical studies led to a topological model for the MHV M protein Rottier et al., 1984 Rottier et al., , 1986 , in which the polypeptide spans the lipid bilayer three times, leaving a small amino-terminal domain (15-35 residues) in the lumen of intracellular organelles (or outside the virus), whereas the carboxyterminal half of the protein is located on the cytoplasmic side of the membrane (or inside the virion). Using a mutational approach including deletions, insertions, and substitutions, both the transmembrane domain and the cysteine-rich region immediately downstream thereof, but not the carboxy-terminal part of the cytoplasmic tail, were shown to be important for MHV S protein-induced cell-cell fusion (Bos et al., 1995; Chang and Gombold, 2001; Chang et al., 2000) The cleavage requirements of the S proteins for the biological activities of the coronavirus spike remain enigmatic. doi = 10.1016/s0065-3527(05)64006-7 id = cord-104223-ht3ry9i0 author = nan title = Sorting within the regulated secretory pathway occurs in the trans- Golgi network date = 1990-01-01 keywords = ELH; Fig; Golgi; vesicle summary = Bioactive peptides cleaved from the egg-laying hormone precursor in the bag cell neurons of Aplysia are sorted into distinct dense core vesicle classes (DCVs). All other changes were minor in comparison, and in the compartments important in these studies-small and large immature vesicles, clear vesicles, and Golgi apparatus-the results between calculations at three HD values differ by no more than 5 % in any experiment. Both amino and carboxy terminal-associated radioactivity are transported through the Golgi stacks and enter small immature DCVs (defined by membrane extensions, connection to tubules, or nonspherical morphology) and clear vesicles after a 30-min pulse and 30-min chase (Fig. 4 B, Fig. 5 , and Table I ). After the initial cleavage event, the ELH-containing carboxy-terminal intermediate condenses in one region of the TGN (small immature vesicles) and the amino-terminal bag cell peptide-containing intermediate condenses in another region of the TGN (large immature vesicles). doi = nan id = cord-104231-fi8pskod author = nan title = The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network date = 1994-04-02 keywords = CD4; CD8; Fig; Golgi; TGN38 summary = Unlike CD8-C (see Fig. 3 C) , the CD8-AC hybrid protein was not in the Golgi apparatus but exhibited a cell surface staining pattern and additional accumulation in intracel* The two categories of transfected cells, low "expressers" (<) and high "expressers ~ (>), were defined as described in Materials and Methods. At higher levels of expression (>60 gold particles/cell section) the percentage of labeling over the Golgi apparatus fell (to 60 5:7 %) and rose over endosomes (to 29 5:7 %) and the plasma membrane (to 11 + 7%) ( Table I) . At higher levels of expression (>50 gold particles/cell section) the percentage of total labeling over the Golgi apparatus fell (to 61 5: 8%) and rose over endosomes (to 35 + 8%) and plasma membrane (to 4 + 3%) ( Table I) . doi = nan id = cord-104239-xxlcdbqi author = nan title = The organization of endoplasmic reticulum export complexes date = 1996-10-01 keywords = Fig; Golgi; VSV; bud; cell summary = While the formation of ER to Golgi carrier vesicles in secretory tissues is largely confined to the transitional region facing the juxtanuclear Golgi apparatus (Palade, 1975) , studies in other cell lines have shown that export from the ER can originate from multiple sites that appear randomly distributed throughout the cytoplasm and, in most instances, distant from the Golgi complex. The local density of buds on individual cisternae associated with export complexes was determined as follows: using a stack of sequential serial sections, we followed one continuous bud-bearing zone of ER membrane that contained at least four buds. In the presence of the Sarl mutant, VSV-G reached a density of 700 _+ 200 gold particles per ~m 2 in a planar projection of the cluster (Fig. 10 E) , reinforcing our previous observations that the budding activity associated with export complexes involves concentration. doi = nan id = cord-104268-q1jx0n0l author = nan title = Localization and targeting of the Saccharomyces cerevisiae Kre2p/Mnt1p alpha 1,2-mannosyltransferase to a medial-Golgi compartment date = 1995-11-02 keywords = Fig; Golgi; TMD summary = doi = nan id = cord-104269-9r7rqqqk author = nan title = Sorting signals in the MHC class II invariant chain cytoplasmic tail and transmembrane region determine trafficking to an endocytic processing compartment date = 1994-07-02 keywords = Golgi; Iicr summary = title: Sorting signals in the MHC class II invariant chain cytoplasmic tail and transmembrane region determine trafficking to an endocytic processing compartment Ii-TR chimera containing the Ii cytoplasmic tail and transmembrane region is delivered directly to the endocytic pathway by an intracellular route, implying that the Ii sorting signals are efficiently recognized by sorting machinery located in the trans-Golgi. Ii-TR chimera containing the Ii cytoplasmic tail and transmembrane region is delivered directly to the endocytic pathway by an intracellular route, implying that the Ii sorting signals are efficiently recognized by sorting machinery located in the trans-Golgi. Further, the rate of synthesis of the Iicx and Iicr+m chimeras was 4-and 8-fold higher, respectively, than that of wild-type TR even though the chimeric receptors were expressed in lower amounts on the cell surface suggesting most of the chimeric molecules were trafficking by a direct intracellular route to the endocytic compartment where they were degraded. doi = nan id = cord-104279-choywmwd author = nan title = Membrane protein sorting in the yeast secretory pathway: evidence that the vacuole may be the default compartment date = 1992-10-01 keywords = DPAP; Fig; Golgi; membrane; protein summary = First, to determine if the lumenal domain was sorted to the vacuole when expressed in the secretory pathway as a soluble protein, a gene fusion was used to create the protein ctFss-B, consisting of the NH2-terminal ER-targeting signal sequence of prepro-t~ factor fused to the lumenal domain of DPAP B at residue 49 ( Fig. 1 B) . To ad-dress the possibility that the mutant constructs analyzed in this study were mislocalized to the plasma membrane followed by rapid endocytic uptake to the vacuole, indirect immunofluorescence experiments were performed on BB-Inv, B-A-B, A20-BB, and/x22-AA-B expressed in a secl strain at 34~ As a positive control for accumulation in secretory vesicles, the localization of the fusion protein Fusl-LacZp was analyzed (Trueheart et al., 1987) . doi = nan id = cord-289710-ucguzgdm author = nan title = Yeast Kex1p is a Golgi-associated membrane protein: deletions in a cytoplasmic targeting domain result in mislocalization to the vacuolar membrane date = 1992-12-02 keywords = Bussey; Golgi; Hpa; Kexlp; protein summary = In addition to soluble proteins, the cell surface appears to be the default destination for mammalian ER, Golgi, and lysosomal membrane proteins as removal of their respective retention/targeting signals results in their delivery to the plasma membrane (Machamer and Rose, 1987; Jackson et al., 1990; Williams and Fukuda, 1990) . Kexlp is predicted to be a type I transmembrane protein with a large amino-terminal protease domain in the lumen of the secretory pathway, a single membrane-spanning domain, and a smaller carboxy-terminai domain positioned cytoplasmicaUy. The observation that KEX/cells intracellularly retain Kexlp activity prompted an analysis to determine in which secretory compartment Kexlp resided, and how it achieved such retention. The above results indicated that Kexlp-Hpa was membrane associated, had received glycosyl modifications in the Golgi apparatus, gave wild-type levels of total activity, and was retained intracellularly; yet processed the K1 killer toxin precursor to a lesser extent than Kexlp. doi = nan id = cord-299281-5z1xminb author = nan title = Oligomerization of a membrane protein correlates with its retention in the Golgi complex date = 1993-09-02 keywords = Fig; Gml; Golgi; SDS; VSV summary = Our data suggest that SDS-resistant oligomers form as newly synthesized molecules of Gml arrive at the Golgi complex and may interact (directly or indirectly) with an actinbased cytoskeletal matrix. Together, these observations suggest that SDS-resistant oligomer formation is an intrinsic property of Gml and mutant Gml proteins that are retained in the Golgi complex, but not of mutants that efficiently reach the plasma membrane. HeLa cells expressing Gml were metabolically labeled for 5 min, chased for the indicated times, solubilized, and immunoprecipitated with anti-VSV G antibody (Fig. 3) . HeLa cells expressing Gml or VSV G were metabolically radiolabeled for 5 min, and then chased for 0 or 60 rain, and microsomes prepared as described in Materials and Methods. On sucrose gradients, Gml solubilized from cytochalasin D-treated cells migrated as an SDS-sensitive oligomer (in the pellet), and VSV G trimerization was unaffected (data not shown). doi = nan id = cord-317070-awip52k7 author = nan title = Molecular characterization of two human autoantigens: unique cDNAs encoding 95- and 160-kD proteins of a putative family in the Golgi complex date = 1993-07-01 keywords = Fig; Golgi; SY2 summary = Changes to the structure and distribution of the Golgi complex antigens were followed by indirect immunoperoxidase staining (47) using the prototype serum SY, rabbit antibodies to the recombinant SY2, SY10, and SYll proteins, and affnity-pufifed antibodies as described above. When antibodies from the prototype serum were affinity purified on nitrocellulose filters containing 5 x 104 phage-expressing SY2 and SYll recombinant proteins, all reproduced the Golgi pattern of immunofluorescence on HEp-2 cells (Fig. 1 b) . The 35S-labeled in vitro translation product of SYll cDNA migrated in SDS-PAGE at 95 kD ( Fig. 8 b, lane I) and was immunoprecipitated by the original human anti-Golgi serum (Fig. 8 b, lane 3) . Evidence that the rabbit antiserum raised by immunization with recombinant SY11 recognized the same protein as the prototype human serum was shown when the rabbit antiserum immunoprecipitated the in vitro translation product in an identical manner to human Golgi sera (Fig. 8 b, compare lanes 3 and 5 with lane 4). doi = nan id = cord-319626-f1b3ygg0 author = nan title = Site of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59 date = 1988-05-01 keywords = Fig; Golgi summary = After synthesis in the rough ER this protein is transported to a smooth membrane compartment between the rough ER and Golgi stack where it accumulates allowing nucleocapsids in the cytoplasm to bind which results in the formation of a virion (Holmes et al., 1981a; Tooze et al., 1984) . The observed increases in molecular mass must be due to the addition of O-linked oligosaccharides (Holmes et al., 1981a; Niemann and Klenk, 1981; Rottier et al., 1981) , which is the only known posttranslational modification of El. The intermediate form EI~ has not, however, been previously detected and the heterogeneity of mature forms resolved in Fig. 1 was not seen in previous work with the same virus propagated in a different cell line (e.g., Niemann et al., 1982) . doi = nan id = cord-328082-7c7slfbp author = nan title = Effect of caffeine and reduced temperature (20 degrees C) on the organization of the pre-Golgi and the Golgi stack membranes date = 1993-03-02 keywords = BFA; Golgi summary = This caffeine-induced effect on the Golgi complex was different from that induced by BFA, since mannosidase II, a Golgi stack marker, remained perinuclearly located and the Golgi stack coat protein, beta-COP, was not detached from Golgi membranes in the presence of 10 mM caffeine at 20 degrees C. Further, caffeine at reduced temperature did not inhibit the retrograde movement of Golgi stack membranes observed in BFA-treated cells. In control cells, the glycoproteins were transported to the trans-Golgi region already at 200C as described earlier (Marlin and Simons, 1983; Saraste and Kuismanen, 1984) , and at higher temperatures increased labeling of the plasma membrane was observed (data not shown). Because of the effective inhibition of membrane traffic out of the ER at 20~ and the translocation of p58 to the periphery of the cell in the presence of caffeine, it was of great interest to study whether the morphology of the Golgi stack is affected under the conditions used. doi = nan id = cord-329515-ra20actc author = nan title = Retention of p63 in an ER-Golgi intermediate compartment depends on the presence of all three of its domains and on its ability to form oligomers date = 1994-07-01 keywords = A24; DPPIV; Fig; Golgi; p63 summary = Recently, oligomerization of a chimeric protein containing the first membrane-spanning domain of the M glycoprotein of avian coronavirus has been correlated to its retention in the Golgi apparatus (Weisz et al., 1993) . When COS cells transfected with this mutant were permeabilized, the predominant staining pattern was characteristic for the ER and the Golgi apparatus indicating that/,16-101,6-12A had lost p63wt localization (Fig. 6 c) . To further analyze the role of the cytoplasmic tail of p63 in retention and to determine whether the transmembrane and lumenal domains of this protein contribute to proper intracellular localization, we substituted each of these domains with the corresponding domains of the cell surface protein human DPPIV (Fig. 9) . A similar result was obtained with a construct that only contained the lumenal domain of p63 (DDP; DPPIV cytoplasmic; DPPIV transmembrane, p63 lumenal; Fig. 9 ) except that most of the ER staining was now replaced by cell surface expression (data not shown). doi = nan id = cord-329553-93tbgn2b author = nan title = The 17-residue transmembrane domain of beta-galactoside alpha 2,6- sialyltransferase is sufficient for Golgi retention date = 1992-04-02 keywords = DPPIV; Golgi; S10; s33d summary = A series of experiments has shown that the 17-residue transmembrane domain of ST is sufficient to confer localization to the Golgi apparatus when transferred to the corresponding region of a cell surface type II integral membrane protein. In this report, we have fused different regions of the NH2-terminal ST sequence to the ectodomain of dipeptidyl peptidase IV (DPPIV), a type 11 surface membrane protein (Hong and Doyle, 1990; Ogato et al ., 1989) to study their abilities in conferring Golgi localization ofthe chimeric proteins. To determine the minimum sequence ofthe N112-terminal region of ST that is sufficient for membrane anchorage and Golgi localization, we have constructed a series of chimeric cDNAs which encode different fusion proteins ( Fig. 1 B) , with decreasing lengths of the N112-terminal ST sequence fused to the ectodomain of DPPIV . doi = nan id = cord-351964-hduv0ur4 author = nan title = Sorting of progeny coronavirus from condensed secretory proteins at the exit from the trans-Golgi network of AtT20 cells date = 1987-09-01 keywords = A59; Golgi; MHV; cell summary = The virus, which buds into pre-Golgi compartments, moves through the Golgi cisternae and exploits vesicles of the constitutive exocytic pathway of these fibroblastic hosts, which lack a regulated pathway, to reach the cell surface; the post-Golgi vesicles filled with progeny virions that can be seen near the cell surface apparently fuse with the plasma membrane to release the virus into the medium (for review see Dubois-Dalcq et al., 1984) . Condensation of secretory proteins and the formation of secretory granules of the regulated exocytic pathway occurs exclusively in the trans-Golgi network in uninfected AtT20 cells . B shows, near the lower surface of a cell growing on ECM, one of the extremely rare classes of post-Golgi transport vesicles which contain both virions (arrows) and a clump of condensed secretory protein that labels heavily with anti-ACTH antibody (arrowhead). In AtT20 cells, at 7-10-h postinfection with MHV-A59, both progeny virions and condensing secretory proteins accumulate in the trans-Golgi network. doi = nan id = cord-354726-b9xvycyk author = nan title = Envelope glycoprotein interactions in coronavirus assembly date = 1995-10-02 keywords = Golgi; MHV summary = Using coimmunoprecipitation analysis we demonstrated that the M and S proteins of mouse hepatitis virus (MHV) interact specifically forming heteromultimeric complexes in infected cells. Yet, the self-association of the MHV envelope glycoproteins into higher order complexes is indicative of its role in the sorting of the viral membrane proteins and in driving the formation of the viral lipoprotein coat in virus assembly. Yet, the self-association of the MHV envelope glycoproteins into higher order complexes is indicative of its role in the sorting of the viral membrane proteins and in driving the formation of the viral lipoprotein coat in virus assembly. We have shown previously that neither of the envelope glycoproteins accumulates at the site of budding when expressed independently: the M protein alone localizes to the Golgi complex (Rottier and Rose, 1987; Krijnse Locker et al., 1992a; Klumperman et al., 1994) , whereas the S protein is transported to the plasma membrane (Vennema, H., and P. doi = nan id = cord-355580-4pv1zu1g author = nan title = O-glycosylation of intact and truncated ribophorins in brefeldin A- treated cells: newly synthesized intact ribophorins are only transiently accessible to the relocated glycosyltransferases date = 1992-06-01 keywords = BFA; Fig; Golgi summary = In the same cells, intact ribophorins I and II also underwent O-linked glycosylation in the presence of BFA, but these molecules were modified only during a short time period immediately after their synthesis was completed, and the modification affected only a fraction of the newly synthesized polypeptides. In the same cells, intact ribophorins I and II also underwent O-linked glycosylation in the presence of BFA, but these molecules were modified only during a short time period immediately after their synthesis was completed, and the modification affected only a fraction of the newly synthesized polypeptides. To determine whether the apparent increase in the molecular masses of the truncated ribophorin I molecules that appear in BFA-treated cells reflects a processing of the N-linked oligosaccharide chain, the effect of endo H treatment on this protein was examined. doi = nan