Details for: PARP1
Associated with
Significant Cells
Cell Significance Index (CSI) scores for the chosen context(s)
-
CSI 67.69rCSI 53.25%PRS 17.59
-
CSI 66.15rCSI 59.74%PRS 13.11
-
CSI 66.1rCSI 43.94%PRS 17.65
-
CSI 59.59rCSI 49.35%PRS 14.77
-
CSI 53.88rCSI 43.56%PRS 14.62
-
CSI 50.14rCSI 43.59%PRS 18.24
-
CSI 45.54rCSI 52.13%PRS 29.97
-
CSI 40.45rCSI 50.77%PRS 18.86
-
CSI 34.61rCSI 27.35%PRS 10.12
-
CSI 33.02rCSI 28.59%PRS 16.52
-
CSI 28.17rCSI 80.43%PRS 25.16
-
CSI 27.92rCSI 24.52%PRS 16.65
-
CSI 25.84rCSI 22.63%PRS 19.51
-
CSI 24.8rCSI 73.97%PRS 35.64
-
CSI 23.29rCSI 31.12%PRS 28.06
-
CSI 21.21rCSI 53.14%PRS 41.59
-
CSI 20.71rCSI 19.94%PRS 15.24
-
CSI 19.2rCSI 61.6%PRS 21.35
-
CSI 19.19rCSI 14.26%PRS 21.74
-
CSI 18.79rCSI 25.6%PRS 13.13
-
CSI 17.55rCSI 68.32%PRS 24.13
-
CSI 15.66rCSI 21.43%PRS 14.78
-
CSI 14.4rCSI 23.18%PRS 11.33
-
CSI 13.68rCSI 19.72%PRS 20.53
-
CSI 11.79rCSI 15.45%PRS 58.27
-
CSI 11.72rCSI 38.36%PRS 39.97
-
CSI 11.43rCSI 11.02%PRS 10.36
-
CSI 11.06rCSI 7.69%PRS 17.34
-
CSI 10.8rCSI 19.07%PRS 8.63
-
CSI 10.65rCSI 25.62%PRS 23.34
-
CSI 10.59rCSI 16.15%PRS 13.71
-
CSI 10.39rCSI 53.67%PRS 28.7
-
CSI 10.13rCSI 13.8%PRS 34.94
-
CSI 10rCSI 9.61%PRS 30.19
-
CSI 9.76rCSI 7.38%PRS 20.24
-
CSI 9.15rCSI 20.22%PRS 10.59
-
CSI 9.02rCSI 7.56%PRS 17.59
-
CSI 8.81rCSI 7.3%PRS 13.87
-
CSI 8.77rCSI 7.52%PRS 25.32
-
CSI 8.75rCSI 30.72%PRS 26.39
-
CSI 8.64rCSI 8.54%PRS 53.09
-
CSI 8.6rCSI 10.32%PRS 14.51
-
CSI 8.53rCSI 37.93%PRS 55.78
-
CSI 8.35rCSI 29.64%PRS 24.02
-
CSI 8.26rCSI 8.63%PRS 42.75
-
CSI 7.89rCSI 12.19%PRS 13.78
-
CSI 7.62rCSI 33.45%PRS 27.33
-
CSI 7.37rCSI 13.92%PRS 31.84
-
CSI 7.18rCSI 38.32%PRS 51.47
-
CSI 7.11rCSI 31.6%PRS 14.43
-
CSI 6.96rCSI 24.73%PRS 44.85
-
CSI 6.94rCSI 20.48%PRS 17.85
-
CSI 6.73rCSI 13.82%PRS 33.41
-
CSI 6.54rCSI 9.05%PRS 21.02
-
CSI 6.42rCSI 4.81%PRS 41.4
-
CSI 6.38rCSI 4.76%PRS 24.85
-
CSI 6.23rCSI 7.99%PRS 14.33
-
CSI 6.05rCSI 8.27%PRS 16.31
-
CSI 6.02rCSI 8.05%PRS 55.66
-
CSI 5.99rCSI 34.34%PRS 22.61
-
CSI 5.91rCSI 8.21%PRS 15.15
-
CSI 5.82rCSI 9.43%PRS 14.94
-
CSI 5.66rCSI 6.76%PRS 8.46
-
CSI 5.59rCSI 5.7%PRS 21
-
CSI 5.43rCSI 4.02%PRS 13.01
-
CSI 5.34rCSI 7.55%PRS 20.44
-
CSI 5.21rCSI 3.74%PRS 20.1
-
CSI 5.15rCSI 20.51%PRS 25.74
-
CSI 5.14rCSI 5.06%PRS 41.24
-
CSI 5.08rCSI 25.47%PRS 19.32
-
CSI 5.05rCSI 4.67%PRS 26.78
-
CSI 5.04rCSI 12.74%PRS 18.28
-
CSI 5.01rCSI 27.08%PRS 47.89
-
CSI 4.9rCSI 4.52%PRS 15.02
-
CSI 4.9rCSI 3.73%PRS 19.33
-
CSI 4.89rCSI 8.02%PRS 11.36
-
CSI 4.86rCSI 7.47%PRS 20.7
-
CSI 4.79rCSI 31.41%PRS 37.51
-
CSI 4.76rCSI 5.49%PRS 12.92
-
CSI 4.73rCSI 10.06%PRS 24.54
-
CSI 4.68rCSI 7.51%PRS 43.37
-
CSI 4.68rCSI 6.91%PRS 23.12
-
CSI 4.64rCSI 4.75%PRS 27.37
-
CSI 4.41rCSI 3.07%PRS 20.88
-
CSI 4.27rCSI 78.07%PRS 42.04
-
CSI 4.2rCSI 4.13%PRS 16
-
CSI 4.12rCSI 4.64%PRS 23.63
-
CSI 4.08rCSI 5.08%PRS 8.07
-
CSI 4.07rCSI 5.11%PRS 22.55
-
CSI 4.03rCSI 3.01%PRS 23.81
-
CSI 3.98rCSI 5.32%PRS 16.12
-
CSI 3.95rCSI 3.07%PRS 21.3
-
CSI 3.93rCSI 3.72%PRS 15.36
-
CSI 3.88rCSI 14.65%PRS 21.24
-
CSI 3.86rCSI 7.96%PRS 22.26
-
CSI 3.85rCSI 14.97%PRS 20.44
-
CSI 3.8rCSI 8.66%PRS 12.83
-
CSI 3.74rCSI 3.91%PRS 15.08
-
CSI 3.72rCSI 2.2%PRS 20.31
-
CSI 3.67rCSI 5.02%PRS 16.69
-
CSI -6.5rCSI -11.4%PRS 19.5%
-
CSI -2.6rCSI -16.1%PRS 11.6%
-
CSI -1.1rCSI -1.7%PRS 14.8%
-
CSI -0.1rCSI -0.3%PRS 10.0%
-
CSI 0.0rCSI 0.3%PRS 5.6%
-
CSI 0.2rCSI 0.6%PRS 9.3%
-
CSI 0.2rCSI 2.6%PRS 53.4%
-
CSI 0.2rCSI 5.5%PRS 26.9%
-
CSI 0.3rCSI 1.5%PRS 21.4%
-
CSI 0.3rCSI 0.4%PRS 17.0%
-
CSI 0.3rCSI 1.8%PRS 9.1%
-
CSI 0.3rCSI 3.6%PRS 35.9%
-
CSI 0.3rCSI 0.9%PRS 22.8%
-
CSI 0.3rCSI 1.0%PRS 20.7%
-
CSI 0.4rCSI 6.7%PRS 52.9%
-
CSI 0.4rCSI 6.5%PRS 63.4%
-
CSI 0.4rCSI 2.0%PRS 49.2%
-
CSI 0.5rCSI 7.2%PRS 35.9%
-
CSI 0.5rCSI 5.2%PRS 28.2%
-
CSI 0.5rCSI 3.6%PRS 43.6%
-
CSI 0.5rCSI 1.3%PRS 13.6%
-
CSI 0.5rCSI 1.9%PRS 8.1%
-
CSI 0.6rCSI 4.5%PRS 30.8%
-
CSI 0.6rCSI 3.2%PRS 45.4%
-
CSI 0.6rCSI 2.7%PRS 34.2%
-
CSI 0.6rCSI 0.7%PRS 25.6%
-
CSI 0.6rCSI 3.8%PRS 46.2%
-
CSI 0.6rCSI 1.8%PRS 11.4%
-
CSI 0.6rCSI 1.2%PRS 28.8%
-
CSI 0.6rCSI 0.6%PRS 17.3%
-
CSI 0.7rCSI 7.1%PRS 84.6%
-
CSI 0.7rCSI 1.9%PRS 24.3%
-
CSI 0.7rCSI 0.9%PRS 23.7%
-
CSI 0.7rCSI 1.5%PRS 13.7%
-
CSI 0.7rCSI 1.8%PRS 8.5%
-
CSI 0.7rCSI 3.7%PRS 20.0%
-
CSI 0.7rCSI 2.6%PRS 53.4%
-
CSI 0.8rCSI 3.5%PRS 30.5%
-
CSI 0.8rCSI 2.0%PRS 14.4%
-
CSI 0.8rCSI 1.6%PRS 29.8%
-
CSI 0.8rCSI 1.6%PRS 23.6%
-
CSI 0.8rCSI 0.6%PRS 13.4%
-
CSI 0.8rCSI 1.8%PRS 29.4%
-
CSI 0.8rCSI 0.6%PRS 15.4%
-
CSI 0.9rCSI 2.3%PRS 19.0%
-
CSI 0.9rCSI 1.4%PRS 16.1%
-
CSI 0.9rCSI 1.3%PRS 16.9%
-
CSI 0.9rCSI 1.3%PRS 16.9%
-
CSI 0.9rCSI 1.4%PRS 14.6%
-
CSI 0.9rCSI 1.7%PRS 10.6%
-
CSI 0.9rCSI 1.4%PRS 17.3%
-
CSI 0.9rCSI 1.2%PRS 20.7%
-
CSI 0.9rCSI 1.5%PRS 9.5%
-
CSI 1.0rCSI 0.9%PRS 17.0%
-
CSI 1.0rCSI 1.4%PRS 13.5%
-
CSI 1.0rCSI 1.5%PRS 25.8%
-
CSI 1.0rCSI 2.1%PRS 24.6%
-
CSI 1.1rCSI 1.4%PRS 9.1%
-
CSI 1.1rCSI 1.3%PRS 19.2%
-
CSI 1.1rCSI 1.6%PRS 23.5%
-
CSI 1.1rCSI 4.2%PRS 14.7%
-
CSI 1.1rCSI 2.1%PRS 33.5%
-
CSI 1.1rCSI 0.9%PRS 26.1%
-
CSI 1.1rCSI 1.5%PRS 19.5%
-
CSI 1.2rCSI 12.6%PRS 26.5%
-
CSI 1.2rCSI 2.8%PRS 22.1%
-
CSI 1.2rCSI 2.7%PRS 16.8%
-
CSI 1.2rCSI 2.3%PRS 18.4%
-
CSI 1.3rCSI 1.8%PRS 15.6%
-
CSI 1.3rCSI 2.3%PRS 38.1%
-
CSI 1.3rCSI 2.3%PRS 13.6%
-
CSI 1.3rCSI 1.7%PRS 30.1%
-
CSI 1.3rCSI 2.3%PRS 12.3%
-
CSI 1.3rCSI 30.8%PRS 7.8%
-
CSI 1.3rCSI 5.1%PRS 31.7%
-
CSI 1.3rCSI 2.3%PRS 22.5%
-
CSI 1.3rCSI 2.0%PRS 14.8%
-
CSI 1.3rCSI 3.4%PRS 11.2%
-
CSI 1.4rCSI 2.1%PRS 35.0%
-
CSI 1.4rCSI 1.2%PRS 14.7%
-
CSI 1.4rCSI 5.3%PRS 8.9%
-
CSI 1.4rCSI 1.5%PRS 25.9%
-
CSI 1.4rCSI 6.3%PRS 26.1%
-
CSI 1.5rCSI 5.3%PRS 25.3%
-
CSI 1.5rCSI 4.3%PRS 16.7%
-
CSI 1.5rCSI 1.4%PRS 22.3%
-
CSI 1.5rCSI 1.3%PRS 10.7%
-
CSI 1.5rCSI 36.0%PRS 6.9%
-
CSI 1.5rCSI 3.9%PRS 14.9%
-
CSI 1.5rCSI 8.3%PRS 35.7%
-
CSI 1.5rCSI 3.7%PRS 22.0%
-
CSI 1.6rCSI 39.9%PRS 62.2%
-
CSI 1.6rCSI 3.4%PRS 22.5%
-
CSI 1.6rCSI 2.7%PRS 14.6%
-
CSI 1.6rCSI 2.4%PRS 17.9%
-
CSI 1.6rCSI 2.3%PRS 16.6%
-
CSI 1.7rCSI 4.4%PRS 17.6%
-
CSI 1.7rCSI 3.8%PRS 15.3%
-
CSI 1.7rCSI 5.6%PRS 18.0%
-
CSI 1.7rCSI 3.9%PRS 20.4%
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Network Configuration
Explore relationships of the current gene. Select an Interaction Source: 'ONTOLOGY' for shared pathways (GO/Reactome) or 'STRING' for protein-protein interactions. Further refine by selecting context genes and comparing Cell Significance Index (CSI) scores between baseline and target cell types and their specific contexts.
Legend:
- Query Gene
-
Node Color (Target Cell CSI, relative to current network):
- Very High
- High
- Medium
- Low
- Very Low
- CSI N/A
- Node Size: Proportional to Target Cell CSI magnitude
- STRING PPI Edge
- Shared Pathway Edge (ONTOLOGY)
Other Information
This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.
Genular Protein ID: 1577874424
Symbol: PARP1_HUMAN
Name: Poly[ADP-ribose] synthase 1
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 3120710
Title: Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase.
PubMed ID: 3120710
PubMed ID: 2824474
Title: Primary structure of human poly(ADP-ribose) synthetase as deduced from cDNA sequence.
PubMed ID: 2824474
PubMed ID: 2891139
Title: cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase.
PubMed ID: 2891139
PubMed ID: 2513174
Title: Human nuclear NAD+ ADP-ribosyltransferase(polymerizing): organization of the gene.
PubMed ID: 2513174
PubMed ID: 16710414
Title: The DNA sequence and biological annotation of human chromosome 1.
PubMed ID: 16710414
DOI: 10.1038/nature04727
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 2125269
Title: Human poly(ADP-ribose) polymerase gene. Cloning of the promoter region.
PubMed ID: 2125269
PubMed ID: 2108670
Title: Characterization of a putative promoter region of the human poly(ADP-ribose) polymerase gene: structural similarity to that of the DNA polymerase beta gene.
PubMed ID: 2108670
PubMed ID: 17177976
Title: Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha and regulates interferon-gamma gene transcription in Th1 cells.
PubMed ID: 17177976
PubMed ID: 3121332
Title: Isolation of a cDNA clone for human NAD+: protein ADP-ribosyltransferase.
PubMed ID: 3121332
PubMed ID: 3113420
Title: Molecular cloning of cDNA for human poly(ADP-ribose) polymerase and expression of its gene during HL-60 cell differentiation.
PubMed ID: 3113420
PubMed ID: 2109322
Title: The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA.
PubMed ID: 2109322
PubMed ID: 2123876
Title: The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA.
PubMed ID: 2123876
PubMed ID: 2121735
Title: Expression and site-directed mutagenesis of the catalytic domain of human poly(ADP-ribose)polymerase in Escherichia coli. Lysine 893 is critical for activity.
PubMed ID: 2121735
PubMed ID: 1505517
Title: The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity.
PubMed ID: 1505517
PubMed ID: 7852410
Title: Role of glutamic acid 988 of human poly-ADP-ribose polymerase in polymer formation. Evidence for active site similarities to the ADP-ribosylating toxins.
PubMed ID: 7852410
PubMed ID: 7596430
Title: Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis.
PubMed ID: 7596430
DOI: 10.1038/376037a0
PubMed ID: 9315851
Title: Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching.
PubMed ID: 9315851
DOI: 10.1021/bi971055p
PubMed ID: 9721847
Title: Irreversible binding of poly(ADP)ribose polymerase cleavage product to DNA ends revealed by atomic force microscopy: possible role in apoptosis.
PubMed ID: 9721847
PubMed ID: 9518481
Title: Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication.
PubMed ID: 9518481
PubMed ID: 10497198
Title: Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7.
PubMed ID: 10497198
PubMed ID: 10467406
Title: Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro.
PubMed ID: 10467406
PubMed ID: 15607977
Title: NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1.
PubMed ID: 15607977
PubMed ID: 15044383
Title: Aprataxin, a novel protein that protects against genotoxic stress.
PubMed ID: 15044383
DOI: 10.1093/hmg/ddh122
PubMed ID: 16374543
Title: Nuclear caspase-3 and caspase-7 activation, and poly(ADP-ribose) polymerase cleavage are early events in camptothecin-induced apoptosis.
PubMed ID: 16374543
PubMed ID: 16904257
Title: The poly(ADP-ribose) polymerase 1 interacts with Sry and modulates its biological functions.
PubMed ID: 16904257
PubMed ID: 17396150
Title: A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses.
PubMed ID: 17396150
PubMed ID: 17525332
Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
PubMed ID: 17525332
PubMed ID: 18172500
Title: Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins.
PubMed ID: 18172500
DOI: 10.1038/nature06420
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19344625
Title: Poly(ADP-ribose) polymerase-1 (PARP-1) transcriptionally regulates angiotensin AT2 receptor (AT2R) and AT2R binding protein (ATBP) genes.
PubMed ID: 19344625
PubMed ID: 19779455
Title: PARP-1 transcriptional activity is regulated by sumoylation upon heat shock.
PubMed ID: 19779455
PubMed ID: 19764761
Title: Identification of the ADP-ribosylation sites in the PARP-1 automodification domain: analysis and implications.
PubMed ID: 19764761
DOI: 10.1021/ja906135d
PubMed ID: 19710015
Title: The metastasis efficiency modifier ribosomal RNA processing 1 homolog B (RRP1B) is a chromatin-associated factor.
PubMed ID: 19710015
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19661379
Title: Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1.
PubMed ID: 19661379
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20064938
Title: PARP-3 is a mono-ADP-ribosylase that activates PARP-1 in the absence of DNA.
PubMed ID: 20064938
PubMed ID: 20388712
Title: 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.
PubMed ID: 20388712
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 20106667
Title: Toward a unified nomenclature for mammalian ADP-ribosyltransferases.
PubMed ID: 20106667
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21266351
Title: hPuf-A/KIAA0020 modulates PARP-1 cleavage upon genotoxic stress.
PubMed ID: 21266351
PubMed ID: 21577210
Title: Poly(ADP-ribose)-dependent regulation of Snail1 protein stability.
PubMed ID: 21577210
DOI: 10.1038/onc.2011.153
PubMed ID: 21799911
Title: Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt signaling.
PubMed ID: 21799911
PubMed ID: 21680843
Title: SIRT6 promotes DNA repair under stress by activating PARP1.
PubMed ID: 21680843
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23213405
Title: Taperin (c9orf75), a mutated gene in nonsyndromic deafness, encodes a vertebrate specific, nuclear localized protein phosphatase one alpha (PP1alpha) docking protein.
PubMed ID: 23213405
DOI: 10.1242/bio.2011049
PubMed ID: 22863007
Title: Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling.
PubMed ID: 22863007
PubMed ID: 22300411
Title: Suppressive regulation of KSHV RTA with O-GlcNAcylation.
PubMed ID: 22300411
PubMed ID: 22464733
Title: Inflammasome-activated caspase 7 cleaves PARP1 to enhance the expression of a subset of NF-kappaB target genes.
PubMed ID: 22464733
PubMed ID: 22002106
Title: Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization.
PubMed ID: 22002106
PubMed ID: 22451931
Title: Caspase-7 uses an exosite to promote poly(ADP ribose) polymerase 1 proteolysis.
PubMed ID: 22451931
PubMed ID: 22753495
Title: Sirtuin 6 (SIRT6) rescues the decline of homologous recombination repair during replicative senescence.
PubMed ID: 22753495
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23966166
Title: ZNF365 promotes stalled replication forks recovery to maintain genome stability.
PubMed ID: 23966166
DOI: 10.4161/cc.25882
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 23230272
Title: BAL1 and its partner E3 ligase, BBAP, link Poly(ADP-ribose) activation, ubiquitylation, and double-strand DNA repair independent of ATM, MDC1, and RNF8.
PubMed ID: 23230272
DOI: 10.1128/mcb.00990-12
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25043379
Title: Family-wide analysis of poly(ADP-ribose) polymerase activity.
PubMed ID: 25043379
DOI: 10.1038/ncomms5426
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 24906880
Title: PARG is dispensable for recovery from transient replicative stress but required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress.
PubMed ID: 24906880
DOI: 10.1093/nar/gku505
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
PubMed ID: 25772364
Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.
PubMed ID: 25772364
PubMed ID: 25755297
Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.
PubMed ID: 25755297
PubMed ID: 25533949
Title: A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol.
PubMed ID: 25533949
DOI: 10.1038/nature14028
PubMed ID: 27067600
Title: HPF1/C4orf27 is a PARP-1-interacting protein that regulates PARP-1 ADP-ribosylation activity.
PubMed ID: 27067600
PubMed ID: 27471034
Title: Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro.
PubMed ID: 27471034
DOI: 10.1093/nar/gkw675
PubMed ID: 27257257
Title: ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for chromatin remodeling.
PubMed ID: 27257257
PubMed ID: 28190768
Title: Serine ADP-ribosylation depends on HPF1.
PubMed ID: 28190768
PubMed ID: 29220653
Title: A Poly-ADP-Ribose trigger releases the auto-inhibition of a chromatin remodeling oncogene.
PubMed ID: 29220653
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 30257210
Title: Interplay of histone marks with serine ADP-ribosylation.
PubMed ID: 30257210
PubMed ID: 29954836
Title: Comprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose acceptor site.
PubMed ID: 29954836
PubMed ID: 30356214
Title: Nuclear cGAS suppresses DNA repair and promotes tumorigenesis.
PubMed ID: 30356214
PubMed ID: 30104678
Title: PARP2 mediates branched poly ADP-ribosylation in response to DNA damage.
PubMed ID: 30104678
PubMed ID: 31609975
Title: KHDC3L mutation causes recurrent pregnancy loss by inducing genomic instability of human early embryonic cells.
PubMed ID: 31609975
PubMed ID: 33186521
Title: An HPF1/PARP1-based chemical biology strategy for exploring ADP-ribosylation.
PubMed ID: 33186521
PubMed ID: 27568560
Title: JNK phosphorylates SIRT6 to stimulate DNA double-strand break repair in response to oxidative stress by recruiting PARP1 to DNA Breaks.
PubMed ID: 27568560
PubMed ID: 27256882
Title: Chemical genetic discovery of PARP targets reveals a role for PARP-1 in transcription elongation.
PubMed ID: 27256882
PubMed ID: 30675909
Title: Increased PARP1-DNA binding due to autoPARylation inhibition of PARP1 on DNA rather than PARP1-DNA trapping is correlated with PARP1 inhibitor's cytotoxicity.
PubMed ID: 30675909
DOI: 10.1002/ijc.32131
PubMed ID: 31848352
Title: PARP1 exhibits enhanced association and catalytic efficiency with gammaH2A.X-nucleosome.
PubMed ID: 31848352
PubMed ID: 31796734
Title: Barrier-to-autointegration factor 1 (Banf1) regulates poly [ADP-ribose] polymerase 1 (PARP1) activity following oxidative DNA damage.
PubMed ID: 31796734
PubMed ID: 32844745
Title: PARP1 inhibitors trigger innate immunity via PARP1 trapping-induced DNA damage response.
PubMed ID: 32844745
DOI: 10.7554/elife.60637
PubMed ID: 32028527
Title: HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation.
PubMed ID: 32028527
PubMed ID: 32358582
Title: Real-time monitoring of PARP1-dependent PARylation by ATR-FTIR spectroscopy.
PubMed ID: 32358582
PubMed ID: 32315358
Title: PARP1-cGAS-NF-kappaB pathway of proinflammatory macrophage activation by extracellular vesicles released during Trypanosoma cruzi infection and Chagas disease.
PubMed ID: 32315358
PubMed ID: 34732825
Title: Dual function of HPF1 in the modulation of PARP1 and PARP2 activities.
PubMed ID: 34732825
PubMed ID: 34049076
Title: PARP1-mediated PARylation of TonEBP prevents R-loop-associated DNA damage.
PubMed ID: 34049076
PubMed ID: 33683197
Title: HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase.
PubMed ID: 33683197
DOI: 10.7554/elife.65773
PubMed ID: 34874266
Title: Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin remodeling.
PubMed ID: 34874266
DOI: 10.7554/elife.71502
PubMed ID: 33168626
Title: The 89-kDa PARP1 cleavage fragment serves as a cytoplasmic PAR carrier to induce AIF-mediated apoptosis.
PubMed ID: 33168626
PubMed ID: 33412112
Title: CARM1 regulates replication fork speed and stress response by stimulating PARP1.
PubMed ID: 33412112
PubMed ID: 34102106
Title: XRCC1 prevents toxic PARP1 trapping during DNA base excision repair.
PubMed ID: 34102106
PubMed ID: 34811483
Title: XRCC1 protects transcription from toxic PARP1 activity during DNA base excision repair.
PubMed ID: 34811483
PubMed ID: 34210965
Title: Serine-linked PARP1 auto-modification controls PARP inhibitor response.
PubMed ID: 34210965
PubMed ID: 34625544
Title: The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome.
PubMed ID: 34625544
PubMed ID: 34737271
Title: SPINDOC binds PARP1 to facilitate PARylation.
PubMed ID: 34737271
PubMed ID: 34795260
Title: HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications.
PubMed ID: 34795260
PubMed ID: 34465625
Title: Multiple roles for PARP1 in ALC1-dependent nucleosome remodeling.
PubMed ID: 34465625
PubMed ID: 35124853
Title: PARP1 is activated by membrane damage and is involved in membrane repair through poly(ADP-ribosyl)ation.
PubMed ID: 35124853
DOI: 10.1111/gtc.12926
PubMed ID: 35025765
Title: RECON syndrome is a genome instability disorder caused by mutations in the DNA helicase RECQL1.
PubMed ID: 35025765
DOI: 10.1172/jci147301
PubMed ID: 35104452
Title: SPARCLE, a p53-induced lncRNA, controls apoptosis after genotoxic stress by promoting PARP-1 cleavage.
PubMed ID: 35104452
PubMed ID: 35219381
Title: Micropeptide PACMP inhibition elicits synthetic lethal effects by decreasing CtIP and poly(ADP-ribosyl)ation.
PubMed ID: 35219381
PubMed ID: 35460603
Title: Cytoplasmic PARP1 links the genome instability to the inhibition of antiviral immunity through PARylating cGAS.
PubMed ID: 35460603
PubMed ID: 35013556
Title: The ubiquitin-dependent ATPase p97 removes cytotoxic trapped PARP1 from chromatin.
PubMed ID: 35013556
PubMed ID: 35393539
Title: Poly(ADP-ribosylation) of P-TEFb by PARP1 disrupts phase separation to inhibit global transcription after DNA damage.
PubMed ID: 35393539
PubMed ID: 37823600
Title: ZNF432 stimulates PARylation and inhibits DNA resection to balance PARPi sensitivity and resistance.
PubMed ID: 37823600
DOI: 10.1093/nar/gkad791
PubMed ID: 18055453
Title: A third zinc-binding domain of human poly(ADP-ribose) polymerase-1 coordinates DNA-dependent enzyme activation.
PubMed ID: 18055453
PubMed ID: 21233213
Title: Crystal structures of poly(ADP-ribose) polymerase-1 (PARP-1) zinc fingers bound to DNA: structural and functional insights into DNA-dependent PARP-1 activity.
PubMed ID: 21233213
PubMed ID: 22683995
Title: The zinc-finger domains of PARP1 cooperate to recognize DNA strand breaks.
PubMed ID: 22683995
DOI: 10.1038/nsmb.2335
PubMed ID: 22582261
Title: Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1.
PubMed ID: 22582261
PubMed ID: 26344098
Title: Timeless interacts with PARP-1 to promote homologous recombination repair.
PubMed ID: 26344098
PubMed ID: 26626479
Title: Structural basis of detection and signaling of DNA single-strand breaks by human PARP-1.
PubMed ID: 26626479
PubMed ID: 26626480
Title: PARP-1 activation requires local unfolding of an autoinhibitory domain.
PubMed ID: 26626480
PubMed ID: 29487285
Title: NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains.
PubMed ID: 29487285
PubMed ID: 32241924
Title: Structural basis for allosteric PARP-1 retention on DNA breaks.
PubMed ID: 32241924
PubMed ID: 33361107
Title: Dissecting the molecular determinants of clinical PARP1 inhibitor selectivity for tankyrase1.
PubMed ID: 33361107
PubMed ID: 34919819
Title: The BRCT domain of PARP1 binds intact DNA and mediates intrastrand transfer.
PubMed ID: 34919819
PubMed ID: 33589610
Title: HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones.
PubMed ID: 33589610
PubMed ID: 16959974
Title: The consensus coding sequences of human breast and colorectal cancers.
PubMed ID: 16959974
Sequence Information:
- Length: 1014
- Mass: 113084
- Checksum: 6A5FC01EB91C046B
- Sequence:
MAESSDKLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV GHSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVTGKGQD GIGSKAEKTL GDFAAEYAKS NRSTCKGCME KIEKGQVRLS KKMVDPEKPQ LGMIDRWYHP GCFVKNREEL GFRPEYSASQ LKGFSLLATE DKEALKKQLP GVKSEGKRKG DEVDGVDEVA KKKSKKEKDK DSKLEKALKA QNDLIWNIKD ELKKVCSTND LKELLIFNKQ QVPSGESAIL DRVADGMVFG ALLPCEECSG QLVFKSDAYY CTGDVTAWTK CMVKTQTPNR KEWVTPKEFR EISYLKKLKV KKQDRIFPPE TSASVAATPP PSTASAPAAV NSSASADKPL SNMKILTLGK LSRNKDEVKA MIEKLGGKLT GTANKASLCI STKKEVEKMN KKMEEVKEAN IRVVSEDFLQ DVSASTKSLQ ELFLAHILSP WGAEVKAEPV EVVAPRGKSG AALSKKSKGQ VKEEGINKSE KRMKLTLKGG AAVDPDSGLE HSAHVLEKGG KVFSATLGLV DIVKGTNSYY KLQLLEDDKE NRYWIFRSWG RVGTVIGSNK LEQMPSKEDA IEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE AVKKLTVNPG TKSKLPKPVQ DLIKMIFDVE SMKKAMVEYE IDLQKMPLGK LSKRQIQAAY SILSEVQQAV SQGSSDSQIL DLSNRFYTLI PHDFGMKKPP LLNNADSVQA KVEMLDNLLD IEVAYSLLRG GSDDSSKDPI DVNYEKLKTD IKVVDRDSEE AEIIRKYVKN THATTHNAYD LEVIDIFKIE REGECQRYKP FKQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG LGKTTPDPSA NISLDGVDVP LGTGISSGVN DTSLLYNEYI VYDIAQVNLK YLLKLKFNFK TSLW