Role of glutamic acid 988 of human poly-ADP-ribose polymerase in polymer formation. Evidence for active site similarities to the ADP-ribosylating toxins.
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Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeresTIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complex2,3,7,8-Tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase (TiPARP, ARTD14) is a mono-ADP-ribosyltransferase and repressor of aryl hydrocarbon receptor transactivationDeficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative diseasePurification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteinsActivation of the abundant nuclear factor poly(ADP-ribose) polymerase-1 by Helicobacter pyloriNuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)Structural Basis for DNA Damage-Dependent Poly(ADP-ribosyl)ation by Human PARP-1Structure of the catalytic fragment of poly(AD-ribose) polymerase from chickenPoly(ADP-ribosyl)ation reactions in the regulation of nuclear functionsStructural basis for lack of ADP-ribosyltransferase activity in poly(ADP-ribose) polymerase-13/zinc finger antiviral protein.No Silver Bullet - Canonical Poly(ADP-Ribose) Polymerases (PARPs) Are No Universal Factors of Abiotic and Biotic Stress Resistance of Arabidopsis thaliana.Selective loss of poly(ADP-ribose) and the 85-kDa fragment of poly(ADP-ribose) polymerase in nucleoli during alkylation-induced apoptosis of HeLa cells.Analyzing structure-function relationships of artificial and cancer-associated PARP1 variants by reconstituting TALEN-generated HeLa PARP1 knock-out cells.Positive selection and increased antiviral activity associated with the PARP-containing isoform of human zinc-finger antiviral protein.Functional capacity of XRCC1 protein variants identified in DNA repair-deficient Chinese hamster ovary cell lines and the human populationGlobal analysis of transcriptional regulation by poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in MCF-7 human breast cancer cellsEvolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes.The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction.Family-wide analysis of poly(ADP-ribose) polymerase activityAvrRpm1 missense mutations weakly activate RPS2-mediated immune response in Arabidopsis thalianaThe Broad-Spectrum Antiviral Protein ZAP Restricts Human RetrotranspositionThe XRCC1 phosphate-binding pocket binds poly (ADP-ribose) and is required for XRCC1 function.New PARP targets for cancer therapyPARP1 Inhibitors: antitumor drug design.Dual roles of PARP-1 promote cancer growth and progression.Importin alpha binding and nuclear localization of PARP-2 is dependent on lysine 36, which is located within a predicted classical NLSTherapeutic applications of PARP inhibitors: anticancer therapy and beyondInteraction between PARP-1 and ATR in mouse fibroblasts is blocked by PARP inhibition.Conformational activation of poly(ADP-ribose) polymerase-1 upon DNA binding revealed by small-angle X-ray scattering.Functions of the poly(ADP-ribose) polymerase superfamily in plants.Tankyrases: structure, function and therapeutic implications in cancer.Photoaffinity labeling of mouse fibroblast enzymes by a base excision repair intermediate. Evidence for the role of poly(ADP-ribose) polymerase-1 in DNA repair.ADP ribosylation by PARP-1 suppresses HOXB7 transcriptional activity.Photoaffinity labelling of human poly(ADP-ribose) polymerase catalytic domain.Structural and functional analysis of Oceanobacillus iheyensis macrodomain reveals a network of waters involved in substrate binding and catalysis.Reversible mono-ADP-ribosylation of DNA breaks.MacroD1 Is a Promiscuous ADP-Ribosyl Hydrolase Localized to Mitochondria.
P2860
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P2860
Role of glutamic acid 988 of human poly-ADP-ribose polymerase in polymer formation. Evidence for active site similarities to the ADP-ribosylating toxins.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Role of glutamic acid 988 of h ...... o the ADP-ribosylating toxins.
@en
type
label
Role of glutamic acid 988 of h ...... o the ADP-ribosylating toxins.
@en
prefLabel
Role of glutamic acid 988 of h ...... o the ADP-ribosylating toxins.
@en
P2860
P356
P1476
Role of glutamic acid 988 of h ...... o the ADP-ribosylating toxins.
@en
P2093
Marsischky GT
P2860
P304
P356
10.1074/JBC.270.7.3247
P407
P577
1995-02-01T00:00:00Z