DNA cleavage activity of the V(D)J recombination protein RAG1 is autoregulated.
about
Thermal dependency of RAG1 self-association properties.Karyopherin alpha 1 is a putative substrate of the RAG1 ubiquitin ligase.An amphioxus RAG1-like DNA fragment encodes a functional central domain of vertebrate core RAG1.Riches in RAGs: Revealing the V(D)J Recombinase through High-Resolution Structures.An interdomain boundary in RAG1 facilitates cooperative binding to RAG2 in formation of the V(D)J recombinase complex.Biochemical Characterization of Nonamer Binding Domain of RAG1 Reveals its Thymine Preference with Respect to Length and Position.Structure-specific nuclease activity of RAGs is modulated by sequence, length and phase position of flanking double-stranded DNA.
P2860
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P2860
DNA cleavage activity of the V(D)J recombination protein RAG1 is autoregulated.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
DNA cleavage activity of the V(D)J recombination protein RAG1 is autoregulated.
@ast
DNA cleavage activity of the V(D)J recombination protein RAG1 is autoregulated.
@en
type
label
DNA cleavage activity of the V(D)J recombination protein RAG1 is autoregulated.
@ast
DNA cleavage activity of the V(D)J recombination protein RAG1 is autoregulated.
@en
prefLabel
DNA cleavage activity of the V(D)J recombination protein RAG1 is autoregulated.
@ast
DNA cleavage activity of the V(D)J recombination protein RAG1 is autoregulated.
@en
P2860
P1476
DNA cleavage activity of the V(D)J recombination protein RAG1 is autoregulated
@en
P2093
Mandy M Peak
Pallabi De
P2860
P304
P356
10.1128/MCB.24.15.6850-6860.2004
P407
P577
2004-08-01T00:00:00Z