Role of N-terminal residues in the ubiquitin-independent degradation of human thymidylate synthase.
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Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability,Crystal Structure of Mouse Thymidylate Synthase in Tertiary Complex with dUMP and Raltitrexed Reveals N-Terminus Architecture and Two Different Active Site ConformationsA Regulated, Ubiquitin-Independent Degron in IκBαUbiquitin-independent proteasomal degradationThe intrinsically disordered N-terminal domain of thymidylate synthase targets the enzyme to the ubiquitin-independent proteasomal degradation pathwayDirect ubiquitin independent recognition and degradation of a folded protein by the eukaryotic proteasomes-origin of intrinsic degradation signals.Interaction between thymidylate synthase and its cognate mRNA in zebrafish embryosCooperation between an intrinsically disordered region and a helical segment is required for ubiquitin-independent degradation by the proteasomeCompetition between sumoylation and ubiquitination of serine hydroxymethyltransferase 1 determines its nuclear localization and its accumulation in the nucleus.Conformational diversity analysis reveals three functional mechanisms in proteins.Control of Pim2 kinase stability and expression in transformed human haematopoietic cellsCharacterization of the bipartite degron that regulates ubiquitin-independent degradation of thymidylate synthase.Alg13p, the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase, is a target for proteasomal degradation.APOBEC3G is degraded by the proteasomal pathway in a Vif-dependent manner without being polyubiquitylated.5-Fluorouracil: mechanisms of resistance and reversal strategies.Ubiquitin-independent degradation of p53 mediated by high-risk human papillomavirus protein E6.Two Degradation Pathways of the p35 Cdk5 (Cyclin-dependent Kinase) Activation Subunit, Dependent and Independent of UbiquitinationFunctional dissection of the N-terminal degron of human thymidylate synthase.Tau protein degradation is catalyzed by the ATP/ubiquitin-independent 20S proteasome under normal cell conditions.Structural analyses of human thymidylate synthase reveal a site that may control conformational switching between active and inactive states.
P2860
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P2860
Role of N-terminal residues in the ubiquitin-independent degradation of human thymidylate synthase.
description
2006 nî lūn-bûn
@nan
2006年の論文
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2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
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2006年论文
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name
Role of N-terminal residues in ...... of human thymidylate synthase.
@en
type
label
Role of N-terminal residues in ...... of human thymidylate synthase.
@en
prefLabel
Role of N-terminal residues in ...... of human thymidylate synthase.
@en
P2093
P2860
P356
P1433
P1476
Role of N-terminal residues in ...... of human thymidylate synthase.
@en
P2093
Franklin G Berger
Maria Marjorette O Peña
Sangita Koli
Yang Yang Xing
P2860
P304
P356
10.1042/BJ20051479
P407
P577
2006-02-01T00:00:00Z