The human selenoprotein VCP-interacting membrane protein (VIMP) is non-globular and harbors a reductase function in an intrinsically disordered region.
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The N-terminal Region of the Ubiquitin Regulatory X (UBX) Domain-containing Protein 1 (UBXD1) Modulates Interdomain Communication within the Valosin-containing Protein p97.Pro178 and Pro183 of selenoprotein S are essential residues for interaction with p97(VCP) during endoplasmic reticulum-associated degradation.Selenoproteins: molecular pathways and physiological roles.Alternative transcripts and 3'UTR elements govern the incorporation of selenocysteine into selenoprotein SSelenoprotein S Is Highly Expressed in the Blood Vessels and Prevents Vascular Smooth Muscle Cells From Apoptosis.Expression and purification of the membrane enzyme selenoprotein KSelenoprotein S-dependent Selenoprotein K Binding to p97(VCP) Protein Is Essential for Endoplasmic Reticulum-associated DegradationThe intrinsically disordered membrane protein selenoprotein S is a reductase in vitro.Contribution of selenocysteine to the peroxidase activity of selenoprotein S.Selenium biochemistry and its role for human health.Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER.Biochemical characterization of the selenoproteome in Gallus gallus via bioinformatics analysis: structure-function relationships and interactions of binding molecules.Endoplasmic reticulum-resident selenoproteins as regulators of calcium signaling and homeostasis.Selenoprotein S: a therapeutic target for diabetes and macroangiopathy?Selenoprotein S is involved in maintenance and transport of multiprotein complexes.Structural basis for nucleotide-modulated p97 association with the ER membrane.Conserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex formation for ER-associated degradation (ERAD).Comparison of growth-related traits and gene expression profiles between the offspring of neomale (XX) and normal male (XY) rainbow trout.Dissection of the Role of VIMP in Endoplasmic Reticulum-Associated Degradation of CFTRΔF508.
P2860
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P2860
The human selenoprotein VCP-interacting membrane protein (VIMP) is non-globular and harbors a reductase function in an intrinsically disordered region.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
The human selenoprotein VCP-in ...... trinsically disordered region.
@en
The human selenoprotein VCP-interacting membrane protein
@nl
type
label
The human selenoprotein VCP-in ...... trinsically disordered region.
@en
The human selenoprotein VCP-interacting membrane protein
@nl
prefLabel
The human selenoprotein VCP-in ...... trinsically disordered region.
@en
The human selenoprotein VCP-interacting membrane protein
@nl
P2093
P2860
P356
P1476
The human selenoprotein VCP-in ...... trinsically disordered region.
@en
P2093
Andrea Vala
Jakob Rahr Winther
Jurate Kamarauskaite
Kay Hofmann
Lea Cecilie Christensen
Linda Johansson
Njal Winther Jensen
P2860
P304
26388-26399
P356
10.1074/JBC.M112.346775
P407
P577
2012-06-14T00:00:00Z