SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
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Crystal Structure of Get4-Get5 Complex and Its Interactions with Sgt2, Get3, and Ydj1Structural characterization of the Get4/Get5 complex and its interaction with Get3A Structural Model of the Sgt2 Protein and Its Interactions with Chaperones and the Get4/Get5 ComplexStructures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic InterfaceStructure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteinsTail-anchor targeting by a Get3 tetramer: the structure of an archaeal homologueStructure of the Sgt2 dimerization domain complexed with the Get5 UBL domain involved in the targeting of tail-anchored membrane proteins to the endoplasmic reticulumStructural and functional characterization of ybr137wp implicates its involvement in the targeting of tail-anchored proteins to membranes.A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum.Nuclear import of UBL-domain protein Mdy2 is required for heat-induced stress response in Saccharomyces cerevisiae.The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion.The cochaperone SGTA (small glutamine-rich tetratricopeptide repeat-containing protein alpha) demonstrates regulatory specificity for the androgen, glucocorticoid, and progesterone receptors.Overexpression of human virus surface glycoprotein precursors induces cytosolic unfolded protein response in Saccharomyces cerevisiae.Interaction surface and topology of Get3-Get4-Get5 protein complex, involved in targeting tail-anchored proteins to endoplasmic reticulum.Ubiquitin-like domains can target to the proteasome but proteolysis requires a disordered region.Small Glutamine-Rich Tetratricopeptide Repeat-Containing Protein Alpha (SGTA) Ablation Limits Offspring Viability and Growth in Mice.Biogenesis of tail-anchored proteins: the beginning for the end?Prions, Chaperones, and Proteostasis in Yeast.Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like protein 4a) complex reveals a novel binding interface that functions in tail-anchored protein biogenesis.The mechanism of tail-anchored protein insertion into the ER membrane.The special delivery of a tail-anchored protein: why it pays to use a dedicated courierRegulation of chaperone effects on a yeast prion by cochaperone Sgt2.New phenotypes generated by the G57R mutation of BUD23 in Saccharomyces cerevisiae.
P2860
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P2860
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
description
2007 nî lūn-bûn
@nan
2007 թուականին հրատարակուած գիտական յօդուած
@hyw
2007 թվականին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
@ast
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
@en
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae.
@nl
type
label
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
@ast
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
@en
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae.
@nl
prefLabel
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
@ast
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
@en
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae.
@nl
P2093
P2860
P921
P3181
P356
P1476
SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae
@en
P2093
Chung Wang
Ming-Yuan Cheng
Shen-Ting Liou
P2860
P2888
P3181
P356
10.1379/CSC-220R.1
P407
P577
2007-01-01T00:00:00Z
P6179
1002440724