title: Thermodynamics and proton uptake for pepstatin binding to retroviral and eukaryotic aspartic proteases.
authors.affiliation: Structural Biochemistry Program, SAIC Frederick, National Cancer Institute, Frederick Cancer Research and Development Center, Maryland 21702-1201, USA.
authors.forename: D
authors.initials: D
authors.lastname: Xie
authors.forename: S
authors.initials: S
authors.lastname: Gulnik
authors.forename: L
authors.initials: L
authors.lastname: Collins
authors.forename: E
authors.initials: E
authors.lastname: Gustchina
authors.forename: T N
authors.initials: TN
authors.lastname: Bhat
authors.forename: J W
authors.initials: JW
authors.lastname: Erickson
mesh_terms: D016282:Aspartic Acid Endopeptidases / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000201:enzymology; D016333:HIV Protease / Q000378:metabolism*; D017320:HIV Protease Inhibitors / Q000378:metabolism*; D006801:Humans; D010436:Pepstatins / Q000378:metabolism*; D011480:Protease Inhibitors / Q000378:metabolism*; D011522:Protons; D013816:Thermodynamics
chemical_list: D017320:HIV Protease Inhibitors; D010436:Pepstatins; D011480:Protease Inhibitors; D011522:Protons; C014195:Streptomyces pepsin inhibitor; D016282:Aspartic Acid Endopeptidases; D016333:HIV Protease; C031375:pepstatin