PARP-1, human recombinant
- Known as:
- PARP-1, H. sapiens Rec.
- Catalog number:
- BC-032
- Product Quantity:
- 20 ug
- Category:
- -
- Supplier:
- kamyia
- Gene target:
- PARP-1 human recombinant
Related genes to: PARP-1, human recombinant
- Gene:
- LINC01703 NIH gene
- Name:
- long intergenic non-protein coding RNA 1703
- Previous symbol:
- -
- Synonyms:
- lncPARP1
- Chromosome:
- 1q42.12
- Locus Type:
- RNA, long non-coding
- Date approved:
- 2016-11-08
- Date modifiied:
- 2018-06-13
- Gene:
- PARP1 NIH gene
- Name:
- poly(ADP-ribose) polymerase 1
- Previous symbol:
- PPOL, ADPRT
- Synonyms:
- PARP
- Chromosome:
- 1q42.12
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2016-10-05
- Gene:
- ZC3HAV1 NIH gene
- Name:
- zinc finger CCCH-type containing, antiviral 1
- Previous symbol:
- -
- Synonyms:
- ZAP, FLB6421, FLJ13288, MGC48898, ZC3HDC2, ZC3H2, PARP13
- Chromosome:
- 7q34
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-11
- Date modifiied:
- 2016-02-12
Related products to: PARP-1, human recombinant
Related articles to: PARP-1, human recombinant
- Viral manipulation of posttranslational modifications (PTMs) is critical to enable control over host defenses. Evidence suggests that one such PTM, adenosine 5'-diphosphate (ADP)-ribosylation, is important for viral replication, but the host and viral components involved are poorly understood. Here, we demonstrate that several human poly(ADP-ribose) polymerase (PARP) proteins, including the zinc-finger domain containing PARP7 (TiPARP) and PARP12, directly ADP-ribosylate the alphaviral nonstructural proteins (nsPs), nsP3 and nsP4. These same human PARP proteins inhibit alphavirus replication in a manner that can be antagonized by the ADP-ribosylhydrolase activity of the virally encoded macrodomain. Last, we find that knockdown of any of the three CCCH zinc-finger domain containing PARPs, PARP7, PARP12, or the enzymatically inactive PARP13 (ZAP/ZC3HAV1), attenuates the antiviral effects of interferon-γ on alphavirus replication. Combined with evolutionary analyses, these data suggest that zinc-finger PARPs share an ancestral antiviral function that can be antagonized by the activity of viral macrodomains, indicative of an ongoing evolutionary conflict between host ADP-ribosylation and viruses. - Source: PubMed
Publication date: 2025/01/31
Ryan Andrew PDelgado-Rodriguez Sofia EDaugherty Matthew D