Multiple routes and milestones in the folding of HIV-1 protease monomer
about
The Parkinson disease-linked LRRK2 protein mutation I2020T stabilizes an active state conformation leading to increased kinase activityNatural polymorphisms and unusual mutations in HIV-1 protease with potential antiretroviral resistance: a bioinformatic analysis.HIV-1 Protease Dimerization Dynamics Reveals a Transient Druggable Binding Pocket at the Interface.Type II kinase inhibitors show an unexpected inhibition mode against Parkinson's disease-linked LRRK2 mutant G2019S.The maturation of HIV-1 protease precursor studied by discrete molecular dynamics.Pressure induced structural changes and dimer destabilization of HIV-1 protease studied by molecular dynamics simulations.
P2860
Multiple routes and milestones in the folding of HIV-1 protease monomer
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Multiple routes and milestones in the folding of HIV-1 protease monomer
@ast
Multiple routes and milestones in the folding of HIV-1 protease monomer
@en
Multiple routes and milestones in the folding of HIV-1 protease monomer
@nl
type
label
Multiple routes and milestones in the folding of HIV-1 protease monomer
@ast
Multiple routes and milestones in the folding of HIV-1 protease monomer
@en
Multiple routes and milestones in the folding of HIV-1 protease monomer
@nl
prefLabel
Multiple routes and milestones in the folding of HIV-1 protease monomer
@ast
Multiple routes and milestones in the folding of HIV-1 protease monomer
@en
Multiple routes and milestones in the folding of HIV-1 protease monomer
@nl
P2860
P1433
P1476
Multiple routes and milestones in the folding of HIV-1 protease monomer
@en
P2093
Massimiliano Bonomi
Michele Parrinello
P2860
P304
P356
10.1371/JOURNAL.PONE.0013208
P407
P577
2010-10-13T00:00:00Z