A 2.2 Å resolution structure of the USP7 catalytic domain in a new space group elaborates upon structural rearrangements resulting from ubiquitin binding
about
The SARS-coronavirus papain-like protease: structure, function and inhibition by designed antiviral compounds.CDDO-Me reveals USP7 as a novel target in ovarian cancer cells.Structural basis of the specificity of USP18 toward ISG15.Molecular dynamics simulation reveals the possible druggable of USP7The structure of the deubiquitinase USP15 reveals a misaligned catalytic triad and an open ubiquitin-binding channel
P2860
A 2.2 Å resolution structure of the USP7 catalytic domain in a new space group elaborates upon structural rearrangements resulting from ubiquitin binding
description
2014 nî lūn-bûn
@nan
2014 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի մարտին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
A 2.2 Å resolution structure o ...... sulting from ubiquitin binding
@ast
A 2.2 Å resolution structure o ...... sulting from ubiquitin binding
@en
A 2.2 Å resolution structure o ...... sulting from ubiquitin binding
@nl
type
label
A 2.2 Å resolution structure o ...... sulting from ubiquitin binding
@ast
A 2.2 Å resolution structure o ...... sulting from ubiquitin binding
@en
A 2.2 Å resolution structure o ...... sulting from ubiquitin binding
@nl
prefLabel
A 2.2 Å resolution structure o ...... sulting from ubiquitin binding
@ast
A 2.2 Å resolution structure o ...... sulting from ubiquitin binding
@en
A 2.2 Å resolution structure o ...... sulting from ubiquitin binding
@nl
P2860
P1476
A 2.2 Å resolution structure o ...... sulting from ubiquitin binding
@en
P2093
Katrina Molland
P2860
P304
P356
10.1107/S2053230X14002519
P577
2014-02-19T00:00:00Z