Residues 240-250 in the C-terminus of the Pirh2 protein complement the function of the RING domain in self-ubiquitination of the Pirh2 protein.
about
Regulation of the DNA damage response by ubiquitin conjugation.Human Pirh2 is a novel inhibitor of prototype foamy virus replication.Molecular Analysis of the HOXA2-Dependent Degradation of RCHY1.p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1The physical interaction of p53 and plakoglobin is necessary for their synergistic inhibition of migration and invasion.Plakoglobin restores tumor suppressor activity of p53R175H mutant by sequestering the oncogenic potential of β-catenin.
P2860
Residues 240-250 in the C-terminus of the Pirh2 protein complement the function of the RING domain in self-ubiquitination of the Pirh2 protein.
description
2013 nî lūn-bûn
@nan
2013 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի դեկտեմբերին 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
Residues 240-250 in the C-term ...... tination of the Pirh2 protein.
@ast
Residues 240-250 in the C-term ...... tination of the Pirh2 protein.
@en
type
label
Residues 240-250 in the C-term ...... tination of the Pirh2 protein.
@ast
Residues 240-250 in the C-term ...... tination of the Pirh2 protein.
@en
prefLabel
Residues 240-250 in the C-term ...... tination of the Pirh2 protein.
@ast
Residues 240-250 in the C-term ...... tination of the Pirh2 protein.
@en
P2093
P2860
P1433
P1476
Residues 240-250 in the C-term ...... tination of the Pirh2 protein.
@en
P2093
Rami Abou Zeinab
Roger P Leng
P2860
P304
P356
10.1371/JOURNAL.PONE.0082803
P407
P577
2013-12-18T00:00:00Z