Four Amino Acid Changes in HIV-2 Protease Confer Class-Wide Sensitivity to Protease Inhibitors.

about

Analysis of the HIV-2 protease's adaptation to various ligands: characterization of backbone asymmetry using a structural alphabet.Exploration of the effect of sequence variations located inside the binding pocket of HIV-1 and HIV-2 proteases.

P2860

Q48240350-05A32A35-6389-4A43-963E-1313D6E6D614 Q52595330-4DF28DC3-2D02-4F07-8A84-784962070ACF

P2860

Four Amino Acid Changes in HIV-2 Protease Confer Class-Wide Sensitivity to Protease Inhibitors.

Item

http://www.wikidata.org/entity/Q38820118

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

Four Amino Acid Changes in HIV ...... tivity to Protease Inhibitors.

@en

type

Item

label

Four Amino Acid Changes in HIV ...... tivity to Protease Inhibitors.

@en

prefLabel

Four Amino Acid Changes in HIV ...... tivity to Protease Inhibitors.

@en

P1476

Four Amino Acid Changes in HIV ...... itivity to Protease Inhibitors

@en

P2093

Dana N Raugi

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

Robert A Smith

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

University of Washington-Dakar HIV-2 Study Group

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

P2860

Active human immunodeficiency virus protease is required for viral infectivity

Structural Evidence for Effectiveness of Darunavir and Two Related Antiviral Inhibitors against HIV-2 Protease

Amprenavir complexes with HIV-1 protease and its drug-resistant mutants altering hydrophobic clusters

Critical differences in HIV-1 and HIV-2 protease specificity for clinical inhibitors

Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease

Extreme Entropy–Enthalpy Compensation in a Drug-Resistant Variant of HIV-1 Protease

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

Crystal structure at 1.9-A resolution of human immunodeficiency virus (HIV) II protease complexed with L-735,524, an orally bioavailable inhibitor of the HIV proteases

Crystal structure of human immunodeficiency virus (HIV) type 2 protease in complex with a reduced amide inhibitor and comparison with HIV-1 protease structures

The crystallographic structure of the protease from human immunodeficiency virus type 2 with two synthetic peptidic transition state analog inhibitors

P304

1062-1069

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

P31

scholarly article

P356

10.1128/JVI.01772-15

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

P407

English

P433

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

P478

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

P50

Geoffrey S. Gottlieb

P577

2015-11-11T00:00:00Z

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

P698

26559830

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

P932

4702657

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

Four Amino Acid Changes in HIV-2 Protease Confer Class-Wide Sensitivity to Protease Inhibitors.

about

P2860

P2860

Four Amino Acid Changes in HIV-2 Protease Confer Class-Wide Sensitivity to Protease Inhibitors.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932