id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-336394-1xf2sxtv	Li, Yu	The MERS-CoV receptor DPP4 as a candidate binding target of the SARS-CoV-2 spike	2020-05-13		.txt	text/plain	1175	76	57	Here, bioinformatics approaches combining human-virus protein interaction prediction and protein docking based on crystal structures have revealed the high affinity between human dipeptidyl peptidase 4 (DPP4) and the spike (S) receptor-binding domain of SARS-CoV-2. The atomic interaction details of the 145 binding interface showed that almost all of the contacting residues of DPP4 with 146 SARS-CoV-2-S RBD were consistent with those for binding with MERS-CoV-S 147 RBD (Table S1 ) (Song et al., 2014) . In addition, the models evaluated the 228 binding potential, interface residues and structures that were consistent with those 229 Comparison of the key residues between human and pangolin DPP4 protein 471 Identification of residues on human receptor DPP4 critical for MERS-CoV binding 401 and entry Structure of MERS-CoV spike receptor-binding domain 417 complexed with human receptor DPP4 SARS-CoV-2 spike receptor-binding domain has a potentially high affinity with DPP4	./cache/cord-336394-1xf2sxtv.txt	./txt/cord-336394-1xf2sxtv.txt