The rise and fall of poly(ADP-ribose): An enzymatic perspective.
about
Structure of the sirtuin-linked macrodomain SAV0325 from Staphylococcus aureusHPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation ActivityAnalyzing structure-function relationships of artificial and cancer-associated PARP1 variants by reconstituting TALEN-generated HeLa PARP1 knock-out cells.Characterization of the interactions of PARP-1 with UV-damaged DNA in vivo and in vitroPARP-2 domain requirements for DNA damage-dependent activation and localization to sites of DNA damageSister chromatid telomere fusions, but not NHEJ-mediated inter-chromosomal telomere fusions, occur independently of DNA ligases 3 and 4.ADPriboDB: The database of ADP-ribosylated proteins.Opportunities for the repurposing of PARP inhibitors for the therapy of non-oncological diseases.LncRNA-SLC6A9-5:2: A potent sensitizer in 131I-resistant papillary thyroid carcinoma with PARP-1 induction.Poly(ADP-ribose) polymerase 1 escorts XPC to UV-induced DNA lesions during nucleotide excision repair.Reversible mono-ADP-ribosylation of DNA breaks.Specificity of reversible ADP-ribosylation and regulation of cellular processes.Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: new insights into DNA ADP-ribosylation.MacroD1 Is a Promiscuous ADP-Ribosyl Hydrolase Localized to Mitochondria.NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains.PARP-1 protects against colorectal tumor induction, but promotes inflammation-driven colorectal tumor progression.Interplay of Histone Marks with Serine ADP-RibosylationMicroRNA-7-5p Promotes Cisplatin Resistance of Cervical Cancer Cells and Modulation of Cellular Energy Homeostasis by Regulating the Expression of the PARP-1 and BCL2 Genes
P2860
Q27713797-88620AAE-A9D5-476D-B44F-0BDEFD54B7A9Q28118267-20BDE504-8684-4924-BEFA-2497CF78057AQ30830820-0B06EB83-B104-4172-946E-316A1571F7B7Q36453246-09817B42-E7CB-4795-9A21-E82C16279CC6Q36627921-EB00452C-9C2D-463A-A836-910C5CC6E982Q36893804-259F7807-E0F4-4FC4-B4A9-EBF66F73B6C6Q37556937-4EEFEF97-B4E3-49D8-A47B-7FFC5D50D8E5Q38954348-52BC801E-0039-4AFF-B371-A8EABD2F9CA9Q39021756-43244B38-00FC-4970-873F-8BE7ACEBBC05Q41477151-45DAC556-D68C-4EDB-ADAD-02C90BE89871Q47118010-D3135285-5A0D-4C8E-8827-D88BB4CBB052Q47446139-C9A1ED44-15B2-435D-8159-1679A138738AQ47800832-9F93CB28-7614-4027-9141-1CDA494726E2Q50112075-F9C66520-5FC6-47A9-9903-8B8AA5DF227DQ50333817-10AE2B07-D0B0-4528-83D5-B9DDB6DD17B4Q52597868-88F0AF44-CF85-4867-AEB8-01EDB8228690Q58697556-B0A016A1-A824-488A-8594-63C7E4EFE853Q58735914-ACC40E80-E259-4B74-A709-0C2079909066
P2860
The rise and fall of poly(ADP-ribose): An enzymatic perspective.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
The rise and fall of poly(ADP-ribose): An enzymatic perspective.
@en
type
label
The rise and fall of poly(ADP-ribose): An enzymatic perspective.
@en
prefLabel
The rise and fall of poly(ADP-ribose): An enzymatic perspective.
@en
P2860
P1433
P1476
The rise and fall of poly(ADP-ribose): An enzymatic perspective.
@en
P2093
John M Pascal
Tom Ellenberger
P2860
P356
10.1016/J.DNAREP.2015.04.008
P577
2015-05-01T00:00:00Z