cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase.
about
Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferasePARP-1 binds E2F-1 independently of its DNA binding and catalytic domains, and acts as a novel coactivator of E2F-1-mediated transcription during re-entry of quiescent cells into S phaseCloning of ELL, a gene that fuses to MLL in a t(11;19)(q23;p13.1) in acute myeloid leukemiaPoly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life spanCrystal Structure of Human ADP-ribose Transferase ARTD15/PARP16 Reveals a Novel Putative Regulatory DomainThe large subunit of the DNA replication complex C (DSEB/RF-C140) cleaved and inactivated by caspase-3 (CPP32/YAMA) during Fas-induced apoptosisA B-cell-specific DNA recombination complexPoly(ADP-ribosyl)ation reactions in the regulation of nuclear functionsEthidium bromide provides a simple tool for identifying genuine DNA-independent protein associationsPARP-1 expression and activity in primary human lung cells.An in vivo assay for the identification of target proteases which cleave membrane-associated substrates.Identification of novel components of NAD-utilizing metabolic pathways and prediction of their biochemical functions.Structural analysis of the putative regulatory region of the rat gene encoding poly(ADP-ribose) polymerase.Structure/function analysis of PARP-1 in oxidative and nitrosative stress-induced monomeric ADPR formation.Deletion of transfected oncogenes from NIH 3T3 transformants by inhibitors of poly(ADP-ribose) polymerase.Human nuclear NAD+ ADP-ribosyltransferase: localization of the gene on chromosome 1q41-q42 and expression of an active human enzyme in Escherichia coliPoly(ADP-ribose) polymerase in DNA damage-response pathway: implications for radiation oncology.Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase.Human autoantibodies to poly(adenosine diphosphate-ribose) polymerase recognize cross-reactive epitopes associated with the catalytic site of the enzyme.Detection of DNA breaks in apoptotic cells utilizing the DNA binding domain of poly(ADP-ribose) polymerase with fluorescence microscopy.Poly(ADP-ribosyl)ation of p53 in vitro and in vivo modulates binding to its DNA consensus sequence.A duplicated region is responsible for the poly(ADP-ribose) polymerase polymorphism, on chromosome 13, associated with a predisposition to cancer.Sequence and organization of the mouse poly (ADP-ribose) polymerase gene.Regulation of chromatin structure by poly(ADP-ribosyl)ation.Cloning of cDNA encoding Drosophila poly(ADP-ribose) polymerase: leucine zipper in the auto-modification domain.Apopain/CPP32 cleaves proteins that are essential for cellular repair: a fundamental principle of apoptotic death.trans-dominant inhibition of poly(ADP-ribosyl)ation sensitizes cells against gamma-irradiation and N-methyl-N'-nitro-N-nitrosoguanidine but does not limit DNA replication of a polyomavirus replicon.Chromosomal aberrations in PARP(-/-) mice: genome stabilization in immortalized cells by reintroduction of poly(ADP-ribose) polymerase cDNA.Cloning of the large subunit of activator 1 (replication factor C) reveals homology with bacterial DNA ligasesStructural recognition of DNA by poly(ADP-ribose)polymerase-like zinc finger families.Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sitesPotential biological role of poly (ADP-ribose) polymerase (PARP) in male gametes.The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA.A decade of the human genome sequence--how does the medicinal chemist benefit?Germ cell DNA-repair systems-possible tools in cancer research?Protease activity of in vitro transcribed and translated Caenorhabditis elegans cell death gene (ced-3) product.Coordination of DNA single strand break repair.Failure of poly(ADP-ribose) polymerase cleavage by caspases leads to induction of necrosis and enhanced apoptosis.PolyADP-ribose polymerase is a coactivator for AP-2-mediated transcriptional activation.The genes pme-1 and pme-2 encode two poly(ADP-ribose) polymerases in Caenorhabditis elegans.
P2860
Q24290390-AD02DF4F-1282-4D85-B645-A031998CE93EQ24300180-665B0BCB-A3C4-4B8F-8DE3-F5D0A22C47D7Q24310726-00C3D4EC-F916-4617-8E10-7ECCA49AB13CQ24563052-39FDC1CB-8A09-4540-B346-89921DB61B31Q27679467-6BF2FAC9-3A39-4486-ABCA-94092CD8436EQ28244608-BF2266F8-CCDD-4297-A17F-1121799F40ABQ28274822-BA0B5B45-9ACB-41A7-B99E-217C416FF63BQ29617672-5B1B5717-073E-40EA-81BC-BDDBBF9A2703Q29620211-1C84FE1A-0146-4782-B8E5-CFCF4C8E97EBQ30318555-A47F8A6E-A5A2-4DF5-9A38-726E5629E0FBQ30828412-6C60533E-B989-45D2-BBC7-3EF7863FF1D1Q31049613-A9F8A460-5A75-4F4C-971E-B67B50FE77DAQ33218764-084EDD45-2B14-45CE-A720-8CE108761B51Q33488547-5506BDC1-2826-4281-916E-E4EFFC9BE4AEQ33679478-B2DD4BD2-D716-4454-9566-57ABB6ABFFB4Q33856024-201281B3-D0F9-4203-8081-A0B551D59A0BQ33920728-A9509ABF-F788-4795-A456-98A975DC5393Q34064483-79C8B80F-E6E3-43C8-91B6-7E8EF4B844DAQ34564205-38D22233-5A95-4D49-BA80-5E78DE58710CQ34627150-A5548558-3FF3-4333-A026-3BF7AFA3D85CQ34779828-4E0F24C1-08C5-4A01-920B-3FB8FBC1F141Q35194323-5635909B-ECF5-460A-AB70-7337059FCA3FQ35225699-5332A032-8615-41D8-AB9C-92CC5B78B38FQ36204365-DFD1BA1D-C09D-45DF-ADC1-51368108BD3EQ36246658-9B041ADA-B736-4E43-A243-4615ADFB304BQ36366579-44488180-A384-405D-98BF-620449AE097AQ36551405-45C4C20B-65AB-4129-B796-2FFDFBAA8E54Q36668248-1CE19BB3-3951-440E-9507-A152A912786CQ36712721-FA726CBF-D622-43A7-89F9-2EDF560B9D5CQ37063627-58FF7703-65D1-4C97-B497-76EFA7393F71Q37235363-F1D05E4A-3EA2-4BC6-AD6F-A2B1BBE6C4B5Q37644563-F653BCCA-45BC-4010-986E-EE46C37A3439Q37738852-B1AF609F-630D-404B-AE65-31A25CAAF5D7Q37968558-694E0293-C900-4B6B-B751-71CF5C70DC9BQ37983009-B99A0432-2FE8-47BA-83A3-4A40AFE2C923Q38361510-CC330C95-C09E-4827-A268-BF1091D2C678Q39021578-9D5DB0BE-8298-468B-9D94-BCDF69FABF86Q39446494-C28815A3-F308-44CF-91D0-34E4FE9E94ECQ39727130-614FDE8A-9289-461E-9A68-EA2D26D5EC1FQ42022034-CCAC31A0-6CFB-4CE3-AC3E-C7C00A7CF2DA
P2860
cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase.
description
1987 nî lūn-bûn
@nan
1987 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
cDNA sequence, protein structu ...... r poly(ADP-ribose) polymerase.
@ast
cDNA sequence, protein structu ...... r poly(ADP-ribose) polymerase.
@en
type
label
cDNA sequence, protein structu ...... r poly(ADP-ribose) polymerase.
@ast
cDNA sequence, protein structu ...... r poly(ADP-ribose) polymerase.
@en
prefLabel
cDNA sequence, protein structu ...... r poly(ADP-ribose) polymerase.
@ast
cDNA sequence, protein structu ...... r poly(ADP-ribose) polymerase.
@en
P2093
P2860
P356
P1476
cDNA sequence, protein structu ...... r poly(ADP-ribose) polymerase.
@en
P2093
B W Cherney
H Alkhatib
M E Smulson
O W McBride
P2860
P304
P356
10.1073/PNAS.84.23.8370
P407
P577
1987-12-01T00:00:00Z