Structure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteins - Wikidata - awgldk - TriplyDB

Structure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteins

Structure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteins

http://www.wikidata.org/entity/Q27675806

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Structural and Functional Insights into Small, Glutamine-Rich, Tetratricopeptide Repeat Protein Alpha Structure of the Sgt2 dimerization domain complexed with the Get5 UBL domain involved in the targeting of tail-anchored membrane proteins to the endoplasmic reticulum Solution structure of the SGTA dimerisation domain and investigation of its interactions with the ubiquitin-like domains of BAG6 and UBL4A The association of BAG6 with SGTA and tail-anchored proteins Extension of a protein docking algorithm to membranes and applications to amyloid precursor protein dimerization.Ubiquitin-like domains can target to the proteasome but proteolysis requires a disordered region.All roads lead to Rome (but some may be harder to travel): SRP-independent translocation into the endoplasmic reticulum.Structural and functional insights into the E3 ligase, RNF126.SGTA regulates the cytosolic quality control of hydrophobic substrates.SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism.Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.

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Structure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteins

http://www.wikidata.org/entity/Q27675806

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2013 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2013 թվականի հունվարին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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Structure of the Sgt2/Get5 com ...... ail-anchored membrane proteins

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Structure of the Sgt2/Get5 com ...... ail-anchored membrane proteins

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Structure of the Sgt2/Get5 com ...... ail-anchored membrane proteins

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Structure of the Sgt2/Get5 com ...... ail-anchored membrane proteins

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Structure of the Sgt2/Get5 com ...... ail-anchored membrane proteins

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Structure of the Sgt2/Get5 com ...... ail-anchored membrane proteins

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Structure of the Sgt2/Get5 com ...... ail-anchored membrane proteins

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Structure of the Sgt2/Get5 com ...... ail-anchored membrane proteins

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Structure of the Sgt2/Get5 com ...... ail-anchored membrane proteins

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Proceedings of the National Academy of Sciences of the United States of America

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Structure of the Sgt2/Get5 com ...... ail-anchored membrane proteins

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Aline C Simon

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Ewelina M Krysztofinska

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James W Murray

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Peter J Simpson

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Rachael M Goldstone

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Rivka L Isaacson

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Stephen High

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P2860

A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation

Small glutamine-rich tetratricopeptide repeat-containing protein (SGT) interacts with the ubiquitin-dependent endocytosis (UbE) motif of the growth hormone receptor

Structural and functional characterization of human SGT and its interaction with Vpu of the human immunodeficiency virus type 1

Crystal Structure of Get4-Get5 Complex and Its Interactions with Sgt2, Get3, and Ydj1

The structure of Get4 reveals an alpha-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesis

The Yeast E4 Ubiquitin Ligase Ufd2 Interacts with the Ubiquitin-like Domains of Rad23 and Dsk2 via a Novel and Distinct Ubiquitin-like Binding Domain

Structural characterization of the Get4/Get5 complex and its interaction with Get3

Structural Basis for Tail-Anchored Membrane Protein Biogenesis by the Get3-Receptor Complex

A Structural Model of the Sgt2 Protein and Its Interactions with Chaperones and the Get4/Get5 Complex

The mechanism of membrane-associated steps in tail-anchored protein insertion

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