(Q81041303)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17786489%20AND%20SRC:MED&resulttype=core&format=json

5 January 2020

title

Molecular dynamics studies on HIV-1 protease: a comparison of the flap motions between wild type protease and the M46I/G51D double mutant (English)

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5 January 2020

1

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5 January 2020

Anna Maria Almerico

series ordinal

3

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5 January 2020

author name string

Mario Ippolito

series ordinal

2

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5 January 2020

publication date

6 September 2007

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Journal of Molecular Modeling

5 January 2020

published in

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5 January 2020

volume

13

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5 January 2020

issue

11

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5 January 2020

page(s)

1151-1156

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Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A

5 January 2020

cites work

1 reference

12 December 2020

Curling of flap tips in HIV-1 protease as a mechanism for substrate entry and tolerance of drug resistance

1 reference

12 December 2020

Mutation patterns and structural correlates in human immunodeficiency virus type 1 protease following different protease inhibitor treatments

1 reference

12 December 2020

Flap opening dynamics in HIV-1 protease explored with a coarse-grained model

1 reference

12 December 2020

A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6

1 reference

12 December 2020

Insights into amprenavir resistance in E35D HIV-1 protease mutation from molecular dynamics and binding free-energy calculations.

1 reference

12 December 2020

Multidrug Resistance to HIV-1 Protease Inhibition Requires Cooperative Coupling between Distal Mutations

1 reference

12 December 2020

HIV protease: a novel chemotherapeutic target for AIDS.

1 reference

12 December 2020

Kinetics of the dimerization of retroviral proteases: the "fireman's grip" and dimerization.

1 reference

12 December 2020

Human immunodeficiency virus. Mutations in the viral protease that confer resistance to saquinavir increase the dissociation rate constant of the protease-saquinavir complex

1 reference

12 December 2020

Flap opening mechanism of HIV-1 protease.

1 reference

12 December 2020

VEGA: a versatile program to convert, handle and visualize molecular structure on Windows-based PCs.

1 reference

12 December 2020

HIV-1 protease flaps spontaneously open and reclose in molecular dynamics simulations

1 reference

12 December 2020

VMD: visual molecular dynamics

1 reference

12 December 2020

The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU

1 reference

12 December 2020

Drug resistance in HIV-1 protease: Flexibility-assisted mechanism of compensatory mutations

1 reference

12 December 2020

HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: possible contributions to drug resistance and a potential new target site for drugs

1 reference

12 December 2020

Inhibition and catalytic mechanism of HIV-1 aspartic protease

1 reference

12 December 2020

10.1007/S00894-007-0242-3

Identifiers

DOI

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5 January 2020

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