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TopBP1 transcriptional activity is regulated by AKT, and treatment with AKT inhibitors suppresses expression of E2F1 and p73 without interfering with ATR signaling.
The cells expressing an ATR-activation domain mutant of TopBP1 show increased initiation of DNA replication in the S phase by losing local dormant origin suppression.
these data uncover two distinct mechanisms by which mutp53 enhances DNA replication: (i) Both contact and conformational mutp53s can bind TopBP1 and attenuate the checkpoint response to replication stress, and (ii) during normal growth, contact (but not conformational) mutp53s can override the Cdk2 requirement to promote replication by facilitating the TopBP1/Treslin interaction.
The rs115160714 TopBP1 may be a genetic marker of etiology and progression in laryngeal cancer.
The innate immune regulator STAT-5 is shown to regulate transcription of the ATR binding factor TopBP1, and this is critical for the induction of the ATR pathway in human papillomavirus-infected keratinocytes.
TOPBP1 physically binds PLK1 and promotes PLK1 kinase-mediated phosphorylation of RAD51 at serine 14, a modification required for RAD51 recruitment to chromatin.
Functional analyses indicat that the expression TopBP1 and Claspin positively affects the survival of brain cancer cells after exposure to radiation.
TopBP1 interacts with BLM to maintain genome stability but is dispensable for preventing BLM degradation.Crucial residues mediating TopBP1-MDC1 interactions identified.
TopBP1 maintains genome integrity in mitosis by controlling chromatin recruitment of SLX4 and by facilitating unscheduled DNA synthesis.
Findings demonstrate that TopBP1 and ATR are able to inhibit the synthesis of rRNA and to activate nucleolar stress pathway.
TOPBP1 has a role in recruiting TOP2A to ultra-fine anaphase bridges to aid in their resolution
The results suggest that interactions between TopBP1 and E2 and between Brd4 and E2 are required to correctly initiate human papillomavirus 16 DNA replication but are not required for continuing DNA replication.
Phosphorylation of BRIT1 protein coordinates TopBP1 protein recruitment and amplifies ATR signaling in cell DNA damage.
High TopBP1 mRNA and protein expression is associated with endometrial cancer.
Studies identify the SIRT1-TopBP1 axis as a key signaling mode in the regulation of the metabolic checkpoint and the DNA damage checkpoint.
TopBP1 deficiency may increase susceptibility to small vessel loss in IPAH.
BLM was ubiquitinated by E3 ligase MIB1 and degraded in G1 cells but was stabilized by TopBP1 in S phase cells.
Different modes of phosphopeptide binding by TOPBP1 BRCT domains in the DNA damage response.
Akt can switch the TopBP1 function from checkpoint activation to transcriptional regulation by regulating its quaternary structure.
Polymorphism in TOPBP1 gene is associated with pancreatic cancer.
DNA damage response protein TOPBP1 regulates X chromosome silencing in the mammalian germ line.
Consistent with prior reports, TopBP1 co-localized in discrete nuclear foci and was in complex with papillomavirus E2 protein.
The deacetylated form of TopBP1 in SIRT1 mutant cells repressed replication origin firing, while the acetylated form of TopBP1 lost this function.
TopBP1 is a crucial factor in V(D)J rearrangement during the development of B, T and iNKT cells.
Our data suggest that, unlike the yeast models, the TopBP1-AAD is the major activator of ATR, sustaining cell proliferation and embryonic development
TopBP1 is crucial for maintaining genome integrity in the early progenitors that drive neurogenesis.
Tethering DNA damage checkpoint mediator proteins topoisomerase IIbeta-binding protein 1 (TopBP1) and Claspin to DNA activates ataxia-telangiectasia mutated and RAD3-related (ATR) phosphorylation of checkpoint kinase 1 (Chk1).
TopBP1 deficiency in untransformed mouse and human primary cells induces cellular senescence rather than apoptosis. These results indicate that TopBP1 is essential for cell proliferation and maintenance of chromosomal integrity.
ATR and TopBP1 monitor meiotic recombination and are required for activation of the meiotic recombination checkpoint
TopBP1 is a c-Abl-interacting protein and a repressor for c-Abl expression
Data show that TopBP1 and Nbs1 associate with the N-terminal region of Mdc1 in egg extracts.
The critical ATR activator, TopBP1, senses DNA damage and stalled replication forks to initiate assembly of checkpoint signaling complexes.
TopBP1's C-terminal motif containing a putative nuclear localization signal was required for Importin beta interaction and that CT100 of Importin beta was required for TopBP1 interaction.
these findings indicate that WDR18 is a bona fide checkpoint protein and that WDR18 works together with TopBP1 to promote DNA damage checkpoint signaling.
MRN (MRE11-RAD50-NBS1) complex has role in ATR activation via TOPBP1 recruitment.
Cut5 plays an integral role in the recruitment and assembly of the Chk1 signaling cascade components following DNA damage
Data show that Rad17 mediates the interaction of the Rad9-Hus1-Rad1 (9-1-1) complex with the ATR-activating protein TopBP1 in Xenopus egg extracts.
Data show that recombinant TopBP1 induces a large increase in the kinase activity of both Xenopus and human ATR-ATRIP.
GEMC1 promotes initiation of chromosomal DNA replication in multicellular organisms by mediating TopBP1- and Cdk2-dependent recruitment of Cdc45 onto replication origins.
Cut5 plays a crucial role in the initial amplification step of the ATR-Chk1 signaling pathway at the stalled replication fork.
This gene encodes a binding protein which interacts with the C-terminal region of topoisomerase II beta. This interaction suggests a supportive role for this protein in the catalytic reactions of topoisomerase II beta through transient breakages of DNA strands.
DNA topoisomerase 2-binding protein 1
, topoisomerase (DNA) II beta binding protein
, topoisomerase (DNA) II binding protein 1
, dna topoisomerase ii binding protein 1 (IC)
, DNA topoisomerase 2-binding protein 1-like
, DNA topoisomerase II-beta-binding protein 1
, DNA topoisomerase II-binding protein 1
, Cut5-related protein
, DNA topoisomerase 2-binding protein 1-A
, DNA topoisomerase 2-binding protein 1-B
, DNA topoisomerase II-binding protein 1-A
, DNA topoisomerase II-binding protein 1-B