id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-001251-forh7lw4	Jank, Johanna M.	The Domain-Specific and Temperature-Dependent Protein Misfolding Phenotype of Variant Medium-Chain acyl-CoA Dehydrogenase	2014-04-09		.txt	text/plain	7785	553	51	Here we established a comprehensive experimental setup to analyze the structural consequences of eight ACADM missense mutations (p.Ala52Val, p.Tyr67His, p.Tyr158His, p.Arg206Cys, p.Asp266Gly, p.Lys329Glu, p.Arg334Lys, p.Arg413Ser) identified after newborn screening and linked the corresponding protein misfolding phenotype to the site of side-chain replacement with respect to the domain. In a previous study, we provided first experimental evidence for the impact of eight additional ACADM mutations identified in NBS on MCAD structure and function and all of these were clearly associated with conformational derangement and decreased protein stability [16] . Moreover, we summarized and quantified the structural data and visualized the molecular protein misfolding phenotype of the variant MCAD proteins in a 3D plot comparing them to the wild-type, to p.Lys329Glu, the classical severe mutation, and to p.Tyr67His, discussed to be a mild mutation. To visualize results from experiments investigating thermal stability, kinetic stability, and conformation of MCAD wild-type and variants, we combined data and developed relative scores assessing the severity of mutation-induced changes.	./cache/cord-001251-forh7lw4.txt	./txt/cord-001251-forh7lw4.txt