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Werner's syndrome is a rare autosomal recessive disorder characterized by accelerated aging that is caused by defects in the Werner syndrome ATP-dependent helicase gene (WRN). Additionally we are shipping WRNIP1 Antibodies (82) and WRNIP1 Kits (6) and many more products for this protein.
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findings define the WHIP-TRIM14-PPP6C mitochondrial signalosome required for RIG-I-mediated innate antiviral immunity.
WRNIP1 connects PCNA monoubiquitination with ATMIN/ATM to activate ATM signalling in response to replication stress and contribute to the maintenance of genomic stability.
The authors show that WRNIP1 is directly involved in preventing uncontrolled MRE11-mediated degradation of stalled replication forks by promoting RAD51 stabilization on ssDNA.
We propose that UBZ domains can be divided into at least two different types in terms of the ubiquitin-binding surfaces: the pol type and the WRNIP1 type
results suggest that WRNIP1 functions upstream of Poleta in the response to UV irradiation
Mutated WRNIP1 with a deleted ATPase domain or with mutations in lysine residues accumulated in laser light irradiated sites, suggesting that the ATPase domain of WRNIP1 and ubiquitination of WRNIP1 are dispensable for the accumulation.
WHIP was identified as a partner/component of the nuclear envelope/nuclear pore complex (NPC) and set forth to investigate a role for the protein positioned at the NPC.
These results indicate that WRNIP1 functions as a modulator for initiation or restart events during pol delta-mediated DNA synthesis and that its ATPase activity is utilized to sense DNA ends and to regulate the extent of stimulation.
Werner helicase-interacting protein 1 binds polyubiquitin via its zinc finger domain
analysis of the composite and regulated topography of Wrnip1 in the human nucleus highlights its potential role in replication and other nuclear transactions
Data show that that WRNIP1 interacts physically with RAD18 and interferes with the binding of RAD18 to forked DNA and to template/primer DNA.
Mutations in the Walker A motifs of the two proteins revealed that WRNIP1, but not WRN, must bind ATP before an efficient interaction can occur.
Werner's syndrome is a rare autosomal recessive disorder characterized by accelerated aging that is caused by defects in the Werner syndrome ATP-dependent helicase gene (WRN). The protein encoded by this gene interacts with the exonuclease-containing N-terminal portion of the Werner protein. This protein has a ubiquitin-binding zinc-finger domain in the N-terminus, an ATPase domain, and two leucine zipper motifs in the C-terminus. It has sequence similarity to replication factor C family proteins and is conserved from E. coli to human. This protein likely accumulates at sites of DNA damage by interacting with polyubiquinated proteins and also binds to DNA polymerase delta and increases the initiation frequency of DNA polymerase delta-mediated DNA synthesis. This protein also interacts with nucleoporins at nuclear pore complexes. Two transcript variants encoding different isoforms have been isolated for this gene.
, Werner helicase interacting protein 1
, Werner helicase-interacting protein 1
, putative helicase RUVBL
, Werner helicasae interacting protein 1
, Werner syndrome homolog interacting protein
, werner helicase-interacting protein 1