Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5. - Wikidata - awgldk - TriplyDB

Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5.

Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5.

http://www.wikidata.org/entity/Q35052128

about

Structure of the ubiquitin-binding zinc finger domain of human DNA Y-polymerase eta Structural basis for Rab GTPase activation by VPS9 domain exchange factors Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin Identification of a novel ubiquitin binding site of STAM1 VHS domain by NMR spectroscopy Autoubiquitination of BCA2 RING E3 ligase regulates its own stability and affects cell migration NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain RNF168, a new RING finger, MIU-containing protein that modifies chromatin by ubiquitination of histones H2A and H2AX Molecular insights into the function of RING finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation Roles of RabGEF1/Rabex-5 domains in regulating Fc epsilon RI surface expression and Fc epsilon RI-dependent responses in mast cells Protein homeostasis at the plasma membrane The ubiquitin/proteasome system mediates entry and endosomal trafficking of Kaposi's sarcoma-associated herpesvirus in endothelial cells Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis Molecular Architecture and Functional Model of the Complete Yeast ESCRT-I Heterotetramer Structural Basis for Ubiquitin Recognition by the Otu1 Ovarian Tumor Domain Protein Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction Structural Basis for Ubiquitin Recognition by a Novel Domain from Human Phospholipase A2-activating Protein Insights into Ubiquitin Transfer Cascades from a Structure of a UbcH5B∼Ubiquitin-HECTNEDD4L Complex Unconventional Ubiquitin Recognition by the Ubiquitin-Binding Motif within the Y Family DNA Polymerases ι and Rev1 Structural Analysis of the Conserved Ubiquitin-binding Motifs (UBMs) of the Translesion Polymerase iota in Complex with Ubiquitin Structural Basis of Ubiquitin Recognition by Translesion Synthesis DNA Polymerase ι The yeast regulator of transcription protein Rtr1 lacks an active site and phosphatase activity Mechanism of ubiquitylation by dimeric RING ligase RNF4 Structural Insights into the Conformation and Oligomerization of E2∼Ubiquitin Conjugates Crystal structure of the ubiquitin-like domain of human TBK1 Molecular mechanism for Rabex-5 GEF activation by Rabaptin-5 MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes.The ubiquitin system: a critical regulator of innate immunity and pathogen-host interactions Functional diversification of the RING finger and other binuclear treble clef domains in prokaryotes and the early evolution of the ubiquitin system Suppression of the ligand-mediated down-regulation of epidermal growth factor receptor by Ymer, a novel tyrosine-phosphorylated and ubiquitinated protein The ubiquitin-editing enzyme A20 restricts nucleotide-binding oligomerization domain containing 2-triggered signals A single MIU motif of MINDY-1 recognizes K48-linked polyubiquitin chains Ubiquitin-binding domains Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics.Rabx-5 regulates RAB-5 early endosomal compartments and synaptic vesicles in C. elegans.The ubiquitination code: a signalling problem.The hydrophobic patch of ubiquitin is required to protect transactivator-promoter complexes from destabilization by the proteasomal ATPases Rabex-5 ubiquitin ligase activity restricts Ras signaling to establish pathway homeostasis in Drosophila.The unusual UBZ domain of Saccharomyces cerevisiae polymerase η Ubiquitin signaling: extreme conservation as a source of diversity.When ubiquitination meets phosphorylation: a systems biology perspective of EGFR/MAPK signalling.

P2860

2a2e7b8f99adf51deda366ee0d8b039f21e1e8a3 59fdc2ff127a13eb2ba6e7e5a3e8e5a3ab43edb9

P248

Q24297425-1E84885A-F528-4467-A4B6-427854E2A6E4 Q24303645-51A78F40-6116-4D2D-9F26-80D2DBE6453A Q24306397-A1E70513-0889-4E77-9B4E-D627196F0ECC Q24311300-38B5A034-F8C9-4AA6-A7E0-3F33D15B0964 Q24316451-FC1EEF66-6D3E-48BD-980B-1036F0CB6A75 Q24317367-685475B5-5811-4D89-80C3-E096026BE0E0 Q24317544-5CB592C6-8A28-418E-80C7-2AEFCEF91FA5 Q24633548-D5A01057-E29F-4BF5-9CDD-40324D522072 Q24674977-2E5E0DF0-1C16-46DF-A3B8-837AE077D10D Q27009009-0B754D58-90DC-4080-A863-A09CBD1713F1 Q27345534-2C6F9CA1-998F-4B96-A08B-1268051A6589 Q27641237-576C9289-1F29-41B1-9DA6-7BBC34C544B7 Q27644496-1FCE4F70-4647-403D-89B6-DEEA777722F0 Q27649839-C1AB094F-5A3E-4C8E-96C3-AA7B9025E162 Q27650666-D7DAD4E6-560B-4A6D-BE8B-76B846DD5259 Q27655413-2CE33A60-C491-4A10-A73B-2AFF4C8D3B5A Q27658921-F797D49B-DDFC-4C50-B138-694ECCCB10C0 Q27659881-BDF27BFC-8339-4F23-B95B-734AD31155AB Q27664947-F5CD61D6-AE9B-4901-AF11-92E49A06EEAF Q27665594-7D66414C-ECB3-4BC4-BADE-20A40D5693CF Q27670698-9C1B6738-D858-4BAA-B2F0-13FF761C397D Q27671855-E4504CCF-48CF-4F53-8EB1-98937AAD2406 Q27678872-EDF8E803-7253-4B62-A5EA-9478FD5B2765 Q27679207-3A622FE0-6281-486B-A495-E4A0E0D51223 Q27684443-A0BDA87A-D85D-4803-AE6E-28B686A40B7B Q27934744-E806F952-C792-4D2F-859C-EA9D6402C774 Q28067104-B4A76EE5-751B-4C17-A4DC-D2D7523DF874 Q28236887-651347ED-732F-4F85-A3A3-90C880318D5C Q28248770-84D2B686-8A2A-4BFF-91EC-36407495C06C Q28506474-29E2814F-6610-46DD-A81A-82DFF33E8045 Q28910344-B4B35ABB-E6FB-4305-8313-F43C10BDF8B5 Q29616461-233FE83D-84C7-4B99-8B70-4CABDBD95065 Q30369740-28F8F815-1FB4-4571-AEBD-700A1DF08A24 Q31063785-585ECD98-D086-4116-AFBA-2003E7CBCE19 Q33343831-FF16DA07-08B4-459D-997E-DC5EF72FAA34 Q33633763-DA2278FC-0C8F-45BA-91F1-80FC98B09F43 Q34122495-A31A9A27-1EF6-4BA1-8E78-B4772A4BE12F Q34268165-B9AD9A71-F629-4FC9-A80D-E256CA0135ED Q34341547-46606BE0-6436-4410-BB96-CB9BA4776752 Q34360923-2BD31733-E846-49A0-80BB-9664D6C1CA4F

P2860

Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5.

http://www.wikidata.org/entity/Q35052128

description

2006 nî lūn-bûn

@nan

2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

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

name

Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5.

@ast

Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5.

@en

type

label

Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5.

@ast

Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5.

@en

prefLabel

Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5.

@ast

Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5.

@en

P1433

Q35052128-3348DAAC-4E37-490F-B9AD-BEC75F47F668

P1476

Q35052128-D29CD858-491B-4511-84A0-C44BFAC60F26

P2093

Q35052128-5F4E3C5B-AB05-419C-8B19-C1F33B67CA58

Q35052128-6F8671C8-B335-4183-AB9A-0C0B9347E775

Q35052128-88409433-E6ED-4237-A4D8-A479E43D93A7

Q35052128-AA337F57-233D-49A6-81D0-DB25B28D8579

Q35052128-E21A0075-F0C1-4D76-A0C7-8945CC81FB1F

P2860

Q35052128-01A46CA0-2412-4215-8CF4-52E975ADF672

Q35052128-038C24AC-DC86-460C-AA0C-842028058389

Q35052128-09235146-06FC-471A-823C-FC8CC12FD99F

Q35052128-0A55FDA9-DA1A-4C72-9147-09EAADB34291

Q35052128-0E0D126C-28DA-4898-8BED-5F82D5DE56A1

Q35052128-19F05266-0D44-4B2B-AB49-BA6FA20628FB

Q35052128-1C7014B5-7B92-406A-A226-A47C096A8988

Q35052128-22DC0A7A-E0FA-40B3-B061-CAA90D9A86A3

Q35052128-25C784F5-F75A-405A-A99D-CC16BBA583DC

Q35052128-2CEC58B3-BC9A-4155-B284-EC832550DBFD

P2888

Q35052128-766933B7-850C-459C-806D-A05438A875BD

P304

Q35052128-57CA0147-1E44-4564-9188-D927B63BE1C5

P31

Q35052128-C63429C9-A68A-4C5B-AC9A-6272DC6379F7

P356

Q35052128-916780D5-DF60-477E-AA98-7934002D7D06

P433

Q35052128-2359DCCE-E2D2-429E-AA6E-B0A5A92A5C71

P478

Q35052128-2C6F33FB-26BA-4DBD-B75F-D688E2D78634

P50

Q35052128-225DDEF6-07F5-4457-957D-6FC972BFA8A1

Q35052128-5582CAD5-C245-4B0D-9B50-66A21FBDF745

Q35052128-96CD4342-2518-4E2A-ACD9-26634D3A7E3D

P577

Q35052128-0B8F9496-C2F3-413B-A178-DFE8208A8084

P5875

Q35052128-DAC416EF-92F7-4FFB-B84C-92FC04023DBC

P698

Q35052128-D4D78E97-0A65-4D07-B68F-E4EB512B0BF8

P921

Q35052128-6358C434-9721-4FBC-A395-95CDB73670E7

P932

Q35052128-5D2C122A-0BB7-4D33-AED7-99EFF1BF1185

P356

P1433

Nature Structural & Molecular Biology

P1476

Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5

@en

P2093

Allan M Weissman

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

James H Hurley

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

Michael S Kostelansky

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

Rafael Mattera

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

William J Smith

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

P2860

RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination

The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum

De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling

Identification of a family of closely related human ubiquitin conjugating enzymes

The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site

Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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

Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases

P2888

P304

264-271

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

P31

scholarly article

P356

10.1038/NSMB1064

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

P433

3

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

P478

13

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

P50

Juan S. Bonifacino

P577

2006-02-05T00:00:00Z

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

P5875

7311107

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

P698

16462746

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

P921

Ubiquitin-conjugating enzyme E2G 2

P932

1578505

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