PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ß1
about
Spermatid head elongation with normal nuclear shaping requires ADP-ribosyltransferase PARP11 (ARTD11) in miceA family of macrodomain proteins reverses cellular mono-ADP-ribosylationIntracellular Mono-ADP-Ribosylation in Signaling and DiseaseStructure and function of the ARH family of ADP-ribosyl-acceptor hydrolasesRab6a/a' are important Golgi regulators of pro-inflammatory TNF secretion in macrophages.Crystal Structure of Human ADP-ribose Transferase ARTD15/PARP16 Reveals a Novel Putative Regulatory DomainADP-ribosyltransferases and poly ADP-ribosylationThe intrinsic disorder alphabet. III. Dual personality of serine.Epigallocatechin-3-gallate enhances ER stress-induced cancer cell apoptosis by directly targeting PARP16 activity.Family-wide analysis of poly(ADP-ribose) polymerase activityA role of intracellular mono-ADP-ribosylation in cancer biology.Transition-state analysis of 2-O-acetyl-ADP-ribose hydrolysis by human macrodomain 1.New PARP targets for cancer therapyCrosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes.The Sound of Silence: RNAi in Poly (ADP-Ribose) ResearchExpanding functions of intracellular resident mono-ADP-ribosylation in cell physiology.ADP-ribosylation: activation, recognition, and removalBiological significance of the importin-β family-dependent nucleocytoplasmic transport pathways.Concepts and Molecular Aspects in the Polypharmacology of PARP-1 Inhibitors.In vivo vizualisation of mono-ADP-ribosylation by dPARP16 upon amino-acid starvation.A macrodomain-linked immunosorbent assay (MLISA) for mono-ADP-ribosyltransferases.Structural Basis for Potency and Promiscuity in Poly(ADP-ribose) Polymerase (PARP) and Tankyrase Inhibitors.PARPs transfer ADP-D-ribose to proteins (poly(ADP-ribosyl)ation)ARTC1-mediated ADP-ribosylation of GRP78/BiP: a new player in endoplasmic-reticulum stress responses.
P2860
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P248
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P2860
PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ß1
description
2012 nî lūn-bûn
@nan
2012 թուականին հրատարակուած գիտական յօդուած
@hyw
2012 թվականին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
PARP16/ARTD15 is a novel endop ...... h, and modifies karyopherin-ß1
@ast
PARP16/ARTD15 is a novel endop ...... h, and modifies karyopherin-ß1
@en
PARP16/ARTD15 is a novel endop ...... h, and modifies karyopherin-ß1
@en-gb
PARP16/ARTD15 is a novel endop ...... h, and modifies karyopherin-ß1
@nl
type
label
PARP16/ARTD15 is a novel endop ...... h, and modifies karyopherin-ß1
@ast
PARP16/ARTD15 is a novel endop ...... h, and modifies karyopherin-ß1
@en
PARP16/ARTD15 is a novel endop ...... h, and modifies karyopherin-ß1
@en-gb
PARP16/ARTD15 is a novel endop ...... h, and modifies karyopherin-ß1
@nl
prefLabel
PARP16/ARTD15 is a novel endop ...... h, and modifies karyopherin-ß1
@ast
PARP16/ARTD15 is a novel endop ...... h, and modifies karyopherin-ß1
@en
PARP16/ARTD15 is a novel endop ...... h, and modifies karyopherin-ß1
@en-gb
PARP16/ARTD15 is a novel endop ...... h, and modifies karyopherin-ß1
@nl
P2093
P2860
P921
P1433
P1476
PARP16/ARTD15 is a novel endop ...... h, and modifies karyopherin-ß1
@en
P2093
Giuseppe Di Tullio
Maria Di Girolamo
Massimo Micaroni
Simone Di Paola
P2860
P304
P356
10.1371/JOURNAL.PONE.0037352
P407
P577
2012-01-01T00:00:00Z