Molecular dynamics simulations reveal the HIV-1 Vpu transmembrane protein to form stable pentamers.
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Atomistic detailed mechanism and weak cation-conducting activity of HIV-1 Vpu revealed by free energy calculationsPrediction of the structures of helical membrane proteins based on a minimum unfavorable contacts approach.Conserved residues within the HIV-1 Vpu transmembrane-proximal hinge region modulate BST2 binding and antagonism.
P2860
Molecular dynamics simulations reveal the HIV-1 Vpu transmembrane protein to form stable pentamers.
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2013 nî lūn-bûn
@nan
2013 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Molecular dynamics simulations ...... tein to form stable pentamers.
@ast
Molecular dynamics simulations ...... tein to form stable pentamers.
@en
type
label
Molecular dynamics simulations ...... tein to form stable pentamers.
@ast
Molecular dynamics simulations ...... tein to form stable pentamers.
@en
prefLabel
Molecular dynamics simulations ...... tein to form stable pentamers.
@ast
Molecular dynamics simulations ...... tein to form stable pentamers.
@en
P2093
P2860
P1433
P1476
Molecular dynamics simulations ...... tein to form stable pentamers.
@en
P2093
Nabab Khan
Shahid Jameel
U Deva Priyakumar
P2860
P304
P356
10.1371/JOURNAL.PONE.0079779
P407
P577
2013-11-06T00:00:00Z