A triad of lys12, lys41, arg78 spatial domain, a novel identified heparin binding site on tat protein, facilitates tat-driven cell adhesion.
about
Molecular interaction studies of HIV-1 matrix protein p17 and heparin: identification of the heparin-binding motif of p17 as a target for the development of multitarget antagonistsSulfated polymannuroguluronate inhibits Tat-induced SLK cell adhesion via a novel binding site, a KKR spatial triad.Heparosan-derived heparan sulfate/heparin-like compounds: one kind of potential therapeutic agents.Theoretical insight into the structural mechanism for the binding of vinblastine with tubulin.
P2860
A triad of lys12, lys41, arg78 spatial domain, a novel identified heparin binding site on tat protein, facilitates tat-driven cell adhesion.
description
2008 nî lūn-bûn
@nan
2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
A triad of lys12, lys41, arg78 ...... ates tat-driven cell adhesion.
@ast
A triad of lys12, lys41, arg78 ...... ates tat-driven cell adhesion.
@en
A triad of lys12, lys41, arg78 ...... ates tat-driven cell adhesion.
@nl
type
label
A triad of lys12, lys41, arg78 ...... ates tat-driven cell adhesion.
@ast
A triad of lys12, lys41, arg78 ...... ates tat-driven cell adhesion.
@en
A triad of lys12, lys41, arg78 ...... ates tat-driven cell adhesion.
@nl
prefLabel
A triad of lys12, lys41, arg78 ...... ates tat-driven cell adhesion.
@ast
A triad of lys12, lys41, arg78 ...... ates tat-driven cell adhesion.
@en
A triad of lys12, lys41, arg78 ...... ates tat-driven cell adhesion.
@nl
P2093
P2860
P1433
P1476
A triad of lys12, lys41, arg78 ...... ates tat-driven cell adhesion.
@en
P2093
Hualiang Jiang
Limei Wang
Meiyu Geng
Shuai Wang
Shuying Peng
Xianliang Xin
P2860
P356
10.1371/JOURNAL.PONE.0002662
P407
P577
2008-07-16T00:00:00Z