Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3
about
Poly(ADP-ribose) polymerase 3 (PARP3), a newcomer in cellular response to DNA damage and mitotic progressionPARPs and the DNA damage responseStructure of human tankyrase 1 in complex with small-molecule inhibitors PJ34 and XAV939Family-wide chemical profiling and structural analysis of PARP and tankyrase inhibitorsStructural basis and selectivity of tankyrase inhibition by a Wnt signaling inhibitor WIKI4Crystal Structure of Human ADP-ribose Transferase ARTD15/PARP16 Reveals a Novel Putative Regulatory DomainInhibition of poly(ADP-ribose) polymerase interferes with Trypanosoma cruzi infection and proliferation of the parasitePARP inhibition: PARP1 and beyondStructural basis for lack of ADP-ribosyltransferase activity in poly(ADP-ribose) polymerase-13/zinc finger antiviral protein.PARP3 affects the relative contribution of homologous recombination and nonhomologous end-joining pathways.Family-wide analysis of poly(ADP-ribose) polymerase activityInsights into the binding of PARP inhibitors to the catalytic domain of human tankyrase-2.PARP-1 dependent recruitment of the amyotrophic lateral sclerosis-associated protein FUS/TLS to sites of oxidative DNA damage.Identification and Functional Characterizations of N-Terminal α-N-Methylation and Phosphorylation of Serine 461 in Human Poly(ADP-ribose) Polymerase 3.Disrupted ADP-ribose metabolism with nuclear Poly (ADP-ribose) accumulation leads to different cell death pathways in presence of hydrogen peroxide in procyclic Trypanosoma brucei.Structural Implications for Selective Targeting of PARPs.Poly(ADP-ribose) polymerase inhibition in cancer therapy: are we close to maturity?Poly (ADP-ribose) polymerase 3 (PARP3), a potential repressor of telomerase activityPARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes.PARP3 controls TGFβ and ROS driven epithelial-to-mesenchymal transition and stemness by stimulating a TG2-Snail-E-cadherin axis.Poly(ADP-ribose) polymerase inhibitors as promising cancer therapeutics.The underlying mechanism for the PARP and BRCA synthetic lethality: clearing up the misunderstandings.PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis.PARP inhibitors in cancer therapy: an update.Structural biology of the writers, readers, and erasers in mono- and poly(ADP-ribose) mediated signaling.Beyond DNA repair, the immunological role of PARP-1 and its siblings.PARP inhibitors: polypharmacology versus selective inhibition.Latonduine Analogs Restore F508del-Cystic Fibrosis Transmembrane Conductance Regulator Trafficking through the Modulation of Poly-ADP Ribose Polymerase 3 and Poly-ADP Ribose Polymerase 16 Activity.PARP-3 is a mono-ADP-ribosylase that activates PARP-1 in the absence of DNAStructural basis for the inhibition of poly(ADP-ribose) polymerases 1 and 2 by BMN 673, a potent inhibitor derived from dihydropyridophthalazinone.Proteome-wide Profiling of Clinical PARP Inhibitors Reveals Compound-Specific Secondary Targets.Identifying Direct Protein Targets of Poly-ADP-Ribose Polymerases (PARPs) Using Engineered PARP Variants-Orthogonal Nicotinamide Adenine Dinucleotide (NAD+) Analog Pairs.Redundancy between nucleases required for homologous recombination promotes PARP inhibitor resistance in the eukaryotic model organism Dictyostelium.Structural Basis for Potency and Promiscuity in Poly(ADP-ribose) Polymerase (PARP) and Tankyrase Inhibitors.
P2860
Q24338495-F28ADCCE-53B7-434B-A5D8-407CED29FEF0Q26859010-6DD81390-23CC-49FC-82C7-E10191D51C58Q27676990-C802CDE9-AA86-48E6-A2EC-043945DBF4A9Q27677345-5FCB78A4-2DE2-4A5F-B3D6-3DC0A5DB38E3Q27678604-D6CC3904-EBD0-4A33-9791-B5D15D06B9E2Q27679467-AD7A0EA6-9CE2-4F70-9ED9-2E06B0C7638FQ28483989-E7BFD059-B784-4D1B-B447-E3A7A77513DFQ29619617-E0D98204-9300-4E3F-817A-6EF6D31C027AQ29977768-8624EFAB-F179-4CF6-B8B8-D2AC5018ADAAQ33635465-4E4CE213-30B0-432C-B7CE-1CCDFA019418Q34009850-5CE3722E-71F4-46E2-9E9A-A9013401088FQ34299288-9224AA3F-2924-4F2B-8482-A0C446D11DD6Q34992138-D2C5F0A7-18C3-4F2E-A107-047C4222E350Q36436390-492D039B-B565-409D-AA1B-1FCB824048C6Q36725115-F5A97E0E-5B51-4B1A-A201-E64489C460E0Q37405386-F8D7001E-73B9-4449-8586-A97D0AA539DBQ37594776-AAFEA4FE-19D2-41E2-81D9-F720610FC773Q37607431-C1B489CB-1BE8-4FEC-ACF0-B3A6A641F60EQ37661664-7CEC461E-99FB-4F53-9BC8-C28F3F8DF588Q37665592-B9F9D7A6-2119-49B0-ADDE-0EBFB0213DF6Q37727996-1AE22332-7530-49C5-BBC1-D1CE9489D5A6Q37912812-EDE99390-B744-4A6E-86A7-B09A73335A0DQ38075305-D3E46FA0-ABFF-4D29-BA49-4BAF1C1B3748Q38078993-E5A4BE37-2080-4585-8D57-53BB7F82079EQ38086332-A5EB1183-5CF8-4571-A0DA-DCCE64B1E98EQ38089268-95E76537-F1CC-49EE-B377-0AE3F573F986Q38100299-99BA535E-9CCE-4A0B-B0D3-C5C6AF0C5656Q38770149-6A663778-AAC5-4DC5-8647-330FB495B94DQ39430828-CAC0C132-2462-444B-B247-5CA34CC60C2DQ40220408-B4B163F2-FB7E-4DC4-8273-71145077E35CQ40465701-9702B3AA-727C-4ED5-9CA2-AA247645EF06Q41910306-B54122BE-8585-468A-AB68-731F3D565B98Q42368008-B7BDE4CB-190B-4091-9D8A-510712C7A5B6Q48129205-455FFD13-98A5-4728-9222-64DC889786BC
P2860
Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3
description
2009 nî lūn-bûn
@nan
2009 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3
@ast
Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3
@en
Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3
@nl
type
label
Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3
@ast
Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3
@en
Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3
@nl
prefLabel
Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3
@ast
Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3
@en
Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3
@nl
P2093
P50
P3181
P356
P1476
Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3
@en
P2093
Alex Flores
Andreas Johansson
Natalia Markova
Olga Loseva
P304
P3181
P356
10.1021/JM900052J
P407
P50
P577
2009-05-14T00:00:00Z