Transition states of native and drug-resistant HIV-1 protease are the same. - Wikidata - awgldk - TriplyDB

Transition states of native and drug-resistant HIV-1 protease are the same.

Transition states of native and drug-resistant HIV-1 protease are the same.

http://www.wikidata.org/entity/Q34031459

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Transition-state inhibitors of purine salvage and other prospective enzyme targets in malaria Capturing the Reaction Pathway in Near-Atomic-Resolution Crystal Structures of HIV-1 Protease Correlation of chemical shifts predicted by molecular dynamics simulations for partially disordered proteins Transition States, analogues, and drug development.Dynamic and Electrostatic Effects on the Reaction Catalyzed by HIV-1 Protease.Elucidating a relationship between conformational sampling and drug resistance in HIV-1 protease.QM/MM Analysis of Transition States and Transition State Analogues in Metalloenzymes.Protein motions and dynamic effects in enzyme catalysis.

P2860

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P2860

Transition states of native and drug-resistant HIV-1 protease are the same.

http://www.wikidata.org/entity/Q34031459

description

2012 nî lūn-bûn

@nan

2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի ապրիլին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Transition states of native and drug-resistant HIV-1 protease are the same.

@ast

Transition states of native and drug-resistant HIV-1 protease are the same.

@en

Transition states of native and drug-resistant HIV-1 protease are the same.

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type

label

Transition states of native and drug-resistant HIV-1 protease are the same.

@ast

Transition states of native and drug-resistant HIV-1 protease are the same.

@en

Transition states of native and drug-resistant HIV-1 protease are the same.

@nl

prefLabel

Transition states of native and drug-resistant HIV-1 protease are the same.

@ast

Transition states of native and drug-resistant HIV-1 protease are the same.

@en

Transition states of native and drug-resistant HIV-1 protease are the same.

@nl

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PNAS.1202808109

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Transition states of native and drug-resistant HIV-1 protease are the same.

@en

P2093

Aya Wakata

http://www.w3.org/2001/XMLSchema#string

D Randal Kipp

http://www.w3.org/2001/XMLSchema#string

Harris Goldstein

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Jennifer S Hirschi

http://www.w3.org/2001/XMLSchema#string

Vern L Schramm

http://www.w3.org/2001/XMLSchema#string

P2860

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 †

The Catalytic Mechanism of an Aspartic Proteinase Explored with Neutron and X-ray Diffraction

X-ray snapshot of HIV-1 protease in action: observation of tetrahedral intermediate and short ionic hydrogen bond SIHB with catalytic aspartate

Autocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV-1 protease: Relevance to drug resistance

Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease

Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1

HIV-1 protease: mechanism and drug discovery

Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes

Kinetic, stability, and structural changes in high-resolution crystal structures of HIV-1 protease with drug-resistant mutations L24I, I50V, and G73S.

Probing the S1/S1' substrate binding pocket geometry of HIV-1 protease with modified aspartic acid analogues.

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6543-6548

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scholarly article

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10.1073/PNAS.1202808109

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17

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109

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22493227

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3340095

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