Crystallographic analysis of human immunodeficiency virus 1 protease with an analog of the conserved CA-p2 substrate -- interactions with frequently occurring glutamic acid residue at P2' position of substrates

Crystallographic analysis of human immunodeficiency virus 1 protease with an analog of the conserved CA-p2 substrate -- interactions with frequently occurring glutamic acid residue at P2' position of substrates

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http://www.wikidata.org/entity/Q27747736

Q27747736

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Structural and kinetic analysis of drug resistant mutants of HIV-1 protease Structural implications of drug-resistant mutants of HIV-1 protease: high-resolution crystal structures of the mutant protease/substrate analogue complexes Combining mutations in HIV-1 protease to understand mechanisms of resistance Viability of a drug-resistant human immunodeficiency virus type 1 protease variant: structural insights for better antiviral therapy Computational design and experimental study of tighter binding peptides to an inactivated mutant of HIV-1 protease Caught in the Act: The 1.5 Å Resolution Crystal Structures of the HIV-1 Protease and the I54V Mutant Reveal a Tetrahedral Reaction Intermediate †Highly conserved glycine 86 and arginine 87 residues contribute differently to the structure and activity of the mature HIV-1 protease Structural, kinetic, and thermodynamic studies of specificity designed HIV-1 protease Effect of substrate residues on the P2' preference of retroviral proteinases Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packaging Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 angstroms resolution crystal structures of HIV-1 protease mutants with substrate analogs.Mechanism of substrate recognition by drug-resistant human immunodeficiency virus type 1 protease variants revealed by a novel structural intermediate Design, synthesis and evaluation of a potent substrate analog inhibitor identified by scanning Ala/Phe mutagenesis, mimicking substrate co-evolution, against multidrug-resistant HIV-1 protease.DOCK 6: Impact of new features and current docking performance.Structural basis for coevolution of a human immunodeficiency virus type 1 nucleocapsid-p1 cleavage site with a V82A drug-resistant mutation in viral protease.Narrow substrate specificity and sensitivity toward ligand-binding site mutations of human T-cell Leukemia virus type 1 protease.A substrate selected by phage display exhibits enhanced side-chain hydrogen bonding to HIV-1 protease Sub-picomolar Inhibition of HIV-1 Protease with a Boronic Acid

P2860

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P2860

Crystallographic analysis of human immunodeficiency virus 1 protease with an analog of the conserved CA-p2 substrate -- interactions with frequently occurring glutamic acid residue at P2' position of substrates

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http://www.wikidata.org/entity/Q27747736

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1997 nî lūn-bûn

@nan

1997 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1997年の論文

@ja

1997年学术文章

@wuu

1997年学术文章

@zh-cn

1997年学术文章

@zh-hans

1997年学术文章

@zh-my

1997年学术文章

@zh-sg

1997年學術文章

@yue