Covalent modification of PML by the sentrin family of ubiquitin-like proteins - Wikidata - awgldk - TriplyDB

Covalent modification of PML by the sentrin family of ubiquitin-like proteins

Covalent modification of PML by the sentrin family of ubiquitin-like proteins

http://www.wikidata.org/entity/Q28260723

about

A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway Differential regulation of sentrinized proteins by a novel sentrin-specific protease The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections Differential role of Sp100 isoforms in interferon-mediated repression of herpes simplex virus type 1 immediate-early protein expression PMLRARα binds to Fas and suppresses Fas-mediated apoptosis through recruiting c-FLIP in vivo Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase SUMO modification of human XRCC4 regulates its localization and function in DNA double-strand break repair.Distinct in vivo dynamics of vertebrate SUMO paralogues Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1 PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1 Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling Role of desumoylation in the development of prostate cancer The Cullin3 ubiquitin ligase functions as a Nedd8-bound heterodimer Resistance to Rhabdoviridae Infection and Subversion of Antiviral Responses The potential link between PML NBs and ICP0 in regulating lytic and latent infection of HSV-1 Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1.Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3.The SUMO-specific protease SENP5 is required for cell division.Mechanisms, regulation and consequences of protein SUMOylation Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins.Regulation of heat shock transcription factor 1 by stress-induced SUMO-1 modification A dominant-negative UBC12 mutant sequesters NEDD8 and inhibits NEDD8 conjugation in vivo Modification of CCAAT/enhancer-binding protein-beta by the small ubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3 Regulation of Pax3 transcriptional activity by SUMO-1-modified PML PML protein isoforms and the RBCC/TRIM motif Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes Transcriptional activity of CCAAT/enhancer-binding proteins is controlled by a conserved inhibitory domain that is a target for sumoylation Identification of three major sentrinization sites in PML PIC-1/SUMO-1-modified PML-retinoic acid receptor alpha mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation SUMO-specific protease 2 is essential for suppression of polycomb group protein-mediated gene silencing during embryonic development.The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers Downregulation of active IKK beta by Ro52-mediated autophagy.Identification and characterization of a SUMO-1 conjugation system that modifies neuronal calcium/calmodulin-dependent protein kinase II in Drosophila melanogaster.Regulation of the NEDD8 conjugation system by a splicing variant, NUB1L.Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting protein

P2860

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P2860

Covalent modification of PML by the sentrin family of ubiquitin-like proteins

http://www.wikidata.org/entity/Q28260723

description

1998 nî lūn-bûn

@nan

1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

name

Covalent modification of PML by the sentrin family of ubiquitin-like proteins

@ast

Covalent modification of PML by the sentrin family of ubiquitin-like proteins

@en

Covalent modification of PML by the sentrin family of ubiquitin-like proteins

@nl

type

label

Covalent modification of PML by the sentrin family of ubiquitin-like proteins

@ast

Covalent modification of PML by the sentrin family of ubiquitin-like proteins

@en

Covalent modification of PML by the sentrin family of ubiquitin-like proteins

@nl

prefLabel

Covalent modification of PML by the sentrin family of ubiquitin-like proteins

@ast

Covalent modification of PML by the sentrin family of ubiquitin-like proteins

@en

Covalent modification of PML by the sentrin family of ubiquitin-like proteins

@nl

P1433

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P1476

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P2860

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P356

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P407

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P433

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P478

Q28260723-4E3BF91A-6E76-49E1-8F7B-79FC42AF8F7B

P577

Q28260723-6DAB7E79-FA5F-45BE-BCF5-A840C63F73AE

P5875

Q28260723-B2707023-9DB1-456E-838F-713AB1ED0634

P698

Q28260723-598AD82D-BF7C-4AAC-8992-91439F6620E3

P356

P1433

Journal of Biological Chemistry

P1476

Covalent modification of PML by the sentrin family of ubiquitin-like proteins

@en

P2093

E T Yeh

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

H P Nguyen

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

K Kito

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

T Fukuda-Kamitani

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

T Kamitani

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

P2860

A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex

SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family

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

Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein

PML, a growth suppressor disrupted in acute promyelocytic leukemia

Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML

Preferential modification of nuclear proteins by a novel ubiquitin-like molecule

The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR

The ubiquitin system for protein degradation

Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells

P304

3117-20

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

P31

scholarly article

P356

10.1074/JBC.273.6.3117

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P407

P433

6

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P478

273

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P577

1998-02-06T00:00:00Z

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P5875

13779147

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P698

9452416

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