Identification of a SUMO-binding motif that recognizes SUMO-modified proteins. - Wikidata - wikimedia - TriplyDB

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.

http://www.wikidata.org/entity/Q37569061

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A functional SUMO-interacting motif in the transactivation domain of c-Myb regulates its myeloid transforming ability Poly-small ubiquitin-like modifier (PolySUMO)-binding proteins identified through a string search The mechanisms of PML-nuclear body formation MDA5 is SUMOylated by PIAS2β in the upregulation of type I interferon signaling Epstein-Barr virus latent membrane protein 1 (LMP1) C-terminal-activating region 3 contributes to LMP1-mediated cellular migration via its interaction with Ubc9 SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle SUMO conjugation to the matrix attachment region-binding protein, special AT-rich sequence-binding protein-1 (SATB1), targets SATB1 to promyelocytic nuclear bodies where it undergoes caspase cleavage Purification and identification of endogenous polySUMO conjugates SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression Isoform-specific monobody inhibitors of small ubiquitin-related modifiers engineered using structure-guided library design Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae SUSP1 antagonizes formation of highly SUMO2/3-conjugated species Analysis of human cytomegalovirus-encoded SUMO targets and temporal regulation of SUMOylation of the immediate-early proteins IE1 and IE2 during infection Infected cell protein 0 functional domains and their coordination in herpes simplex virus replication Identification of Posttranslational Modification-Dependent Protein Interactions Using Yeast Surface Displayed Human Proteome Libraries Structure and Analysis of a Complex between SUMO and Ubc9 Illustrates Features of a Conserved E2-Ubl Interaction Structure of a SUMO-binding-motif Mimic Bound to Smt3p–Ubc9p: Conservation of a Non-covalent Ubiquitin-like Protein–E2 Complex as a Platform for Selective Interactions within a SUMO Pathway The Intrinsic Affinity between E2 and the Cys Domain of E1 in Ubiquitin-like Modifications Mechanism of ubiquitylation by dimeric RING ligase RNF4 Insights into High Affinity Small Ubiquitin-like Modifier (SUMO) Recognition by SUMO-interacting Motifs (SIMs) Revealed by a Combination of NMR and Peptide Array Analysis Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2 Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO Adhiron: a stable and versatile peptide display scaffold for molecular recognition applications Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4 Structural analysis of poly-SUMO chain recognition by the RNF4-SIMs domain Mechanisms, regulation and consequences of protein SUMOylation The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition.Strategies to Identify Recognition Signals and Targets of SUMOylation.SUMOylation regulates the SNF1 protein kinase.Elg1, an alternative subunit of the RFC clamp loader, preferentially interacts with SUMOylated PCNA.Yeast axial-element protein, Red1, binds SUMO chains to promote meiotic interhomologue recombination and chromosome synapsis.Distinct SUMO ligases cooperate with Esc2 and Slx5 to suppress duplication-mediated genome rearrangements SUMO-mediated regulation of DNA damage repair and responses Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase A role for non-covalent SUMO interaction motifs in Pc2/CBX4 E3 activity.Allosteric Activation of Ubiquitin-Specific Proteases by β-Propeller Proteins UAF1 and WDR20 Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection Yeast PIAS-type Ull1/Siz1 is composed of SUMO ligase and regulatory domains

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P2860

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.

http://www.wikidata.org/entity/Q37569061

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 23 September 2004

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.

@en

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.

@nl

type

label

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.

@en

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.

@nl

prefLabel

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.

@en

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.

@nl

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PNAS.0403498101

P1433

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

P1476

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.

@en

P2093

Jing Song

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

Linda K Durrin

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

Theodore G Krontiris

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

Thomas A Wilkinson

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

Yuan Chen

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

P2860

Role of SUMO-1-modified PML in nuclear body formation

Daxx, a novel Fas-binding protein that activates JNK and apoptosis

A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2

Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis

SUMO modification of Huntingtin and Huntington's disease pathology

SUMO-1 modification activates the transcriptional response of p53

PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies

SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex

Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1

Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding

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14373-14378

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scholarly article

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10.1073/PNAS.0403498101

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40

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2004-09-23T00:00:00Z

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8326078

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15388847

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521952

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