Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation - Test2 - elhamkhani - TriplyDB

Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

http://www.wikidata.org/entity/Q27667262

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Threshold-controlled ubiquitination of the EGFR directs receptor fate USP15 is a deubiquitylating enzyme for receptor-activated SMADs RBR E3 ubiquitin ligases: new structures, new insights, new questions Regulation of ERBB3/HER3 signaling in cancer Structure and function of a HECT domain ubiquitin-binding site BIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer Structure of the HECT C-lobe of the UBR5 E3 ubiquitin ligase Structural Determinants of Ubiquitin Conjugation in Entamoeba histolytica Assembly, analysis and architecture of atypical ubiquitin chains Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3 Structure of a ubiquitin-loaded HECT ligase reveals the molecular basis for catalytic priming A HECT ubiquitin-protein ligase as a novel candidate gene for altered quinine and quinidine responses in Plasmodium falciparum A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis.A mechanism for protein monoubiquitination dependent on a trans-acting ubiquitin-binding domain.Ubiquitin E3 ligase FIEL1 regulates fibrotic lung injury through SUMO-E3 ligase PIAS4 Curcumin exerts its tumor suppressive function via inhibition of NEDD4 oncoprotein in glioma cancer cells.Structural and functional insights to ubiquitin-like protein conjugation.The ubiquitin-associated domain of cellular inhibitor of apoptosis proteins facilitates ubiquitylation Signaling-mediated control of ubiquitin ligases in endocytosis.Ubiquitin signaling: extreme conservation as a source of diversity.The E3 ubiquitin ligase NEDD4 negatively regulates HER3/ErbB3 level and signaling.Versatile roles of k63-linked ubiquitin chains in trafficking.Macromolecular juggling by ubiquitylation enzymes.Development of inhibitors in the ubiquitination cascade.System-Wide Modulation of HECT E3 Ligases with Selective Ubiquitin Variant Probes.Role of ubiquitin and the HPV E6 oncoprotein in E6AP-mediated ubiquitination A dual role for K63-linked ubiquitin chains in multivesicular body biogenesis and cargo sorting Covalent Tethering of Fragments For Covalent Probe Discovery A Small Molecule That Switches a Ubiquitin Ligase From a Processive to a Distributive Enzymatic Mechanism E6AP/UBE3A ubiquitin ligase harbors two E2~ubiquitin binding sites.Targeting ubiquitination for cancer therapies.The active form of E6-associated protein (E6AP)/UBE3A ubiquitin ligase is an oligomer.Endosomal transport via ubiquitination Abiotic stress tolerance mediated by protein ubiquitination.Policing Parkin with a UblD.HECT-type E3 ubiquitin ligases in nerve cell development and synapse physiology.Nedd4-induced monoubiquitination of IRS-2 enhances IGF signalling and mitogenic activity.Structural insights into the catalysis and regulation of E3 ubiquitin ligases.Ubiquitylation-dependent oligomerization regulates activity of Nedd4 ligases.Assembly and structure of Lys33-linked polyubiquitin reveals distinct conformations.

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Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

http://www.wikidata.org/entity/Q27667262

description

2011 nî lūn-bûn

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2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի ապրիլին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

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2011年论文

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name

Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

@ast

Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

@en

Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

@nl

type

label

Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

@ast

Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

@en

Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

@nl

prefLabel

Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

@ast

Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

@en

Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

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Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

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Alexander Fish

http://www.w3.org/2001/XMLSchema#string

Elena Maspero

http://www.w3.org/2001/XMLSchema#string

Eleonora Valentini

http://www.w3.org/2001/XMLSchema#string

Sara Mari

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Simona Polo

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P2860

Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase

Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Processing of X-ray diffraction data collected in oscillation mode

Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade

Insights into Ubiquitin Transfer Cascades from a Structure of a UbcH5B∼Ubiquitin-HECTNEDD4L Complex

Inference of macromolecular assemblies from crystalline state

Version 1.2 of the Crystallography and NMR system

Refinement of macromolecular structures by the maximum-likelihood method

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scholarly article

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10.1038/EMBOR.2011.21

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4

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12

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Andrea Musacchio

Sebastiano Pasqualato

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2011-04-01T00:00:00Z

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50377241

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21399620

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3077247

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