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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Thyroid hormone receptor interactor 13

TRIP13, 16E1-BP
This gene encodes a protein that interacts with thyroid hormone receptors, also known as hormone-dependent transcription factors. The gene product interacts specifically with the ligand binding domain. This gene is one of several that may play a role in early-stage non-small cell lung cancer. [provided by RefSeq, Oct 2009] (from NCBI)
Top mentioned proteins: ATPase, p31, CAN, Mad2, Ubiquitin
Papers using TRIP13 antibodies
MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment
Lichten Michael, In PLoS Genetics, 1989
... Trip13 was amplified from samples of Clontech's Mouse Multiple Tissue cDNA Panel I (
Papers on TRIP13
Translating Proteomic Into Functional Data: An High Mobility Group A1 (HMGA1) Proteomic Signature Has Prognostic Value in Breast Cancer.
Sgarra et al., Trieste, Italy. In Mol Cell Proteomics, Jan 2016
qRT-PCR, Western blot, and immunohistochemistry analyses validated the link of three members of this signature (KIFC1, LRRC59, and TRIP13) with HMGA1 expression levels both in vitro and in vivo and wound healing assays demonstrated that these three proteins are involved in modulating tumor cell motility.
TRIP13PCH-2 promotes Mad2 localization to unattached kinetochores in the spindle checkpoint response.
Bhalla et al., Santa Cruz, United States. In J Cell Biol, Dec 2015
Here, we report that the conserved AAA+ ATPase TRIP13(PCH-2) localizes to unattached kinetochores and is required for spindle checkpoint activation in Caenorhabditis elegans.
Mode of interaction of TRIP13 AAA-ATPase with the Mad2-binding protein p31comet and with mitotic checkpoint complexes.
Hershko et al., Haifa, Israel. In Proc Natl Acad Sci U S A, Oct 2015
The AAA-ATPase thyroid hormone receptor interacting protein 13 (TRIP13), jointly with the Mad2-binding protein p31(comet), promotes the inactivation of the mitotic (spindle assembly) checkpoint by disassembling the mitotic checkpoint complex (MCC).
Pch2(TRIP13): controlling cell division through regulation of HORMA domains.
Vader, Dortmund, Germany. In Chromosoma, Sep 2015
Pch2(TRIP13), a generally conserved member of the AAA(+) ATPase (AAA(+)--ATPases associated with diverse cellular activities) family of ATPases, is rapidly emerging as a key regulator of specific chromosomal events.
Gradual implementation of the meiotic recombination program via checkpoint pathways controlled by global DSB levels.
Börner et al., Cleveland, United States. In Mol Cell, Apr 2015
Their resection and interhomolog processing are controlled by the conserved checkpoint proteins Tel1(ATM) kinase and Pch2(TRIP13) ATPase.
The ATM signaling cascade promotes recombination-dependent pachytene arrest in mouse spermatocytes.
Roig et al., Barcelona, Spain. In Plos Genet, Mar 2015
Mechanisms underlying the recombination-dependent arrest response are not well understood, so we sought to identify factors involved by examining mutants deficient for TRIP13, a conserved AAA+ ATPase required for the completion of meiotic DSB repair.
PCH-2 regulates Caenorhabditis elegans lifespan.
Niklason et al., New Haven, United States. In Aging (albany Ny), 2015
The C. elegans gene pch-2 and its homologs, including TRIP13 in humans, have been studied for their functions in cell mitosis and meiosis, but have never been implicated in lifespan regulation.
TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching.
Corbett et al., San Diego, United States. In Elife, 2014
The AAA+ family ATPase TRIP13 is a key regulator of meiotic recombination and the spindle assembly checkpoint, acting on signaling proteins of the conserved HORMA domain family.
MicroRNA-215 Regulates Fibroblast Function: Insights from a Human Fibrotic Disease.
Tong et al., Singapore, Singapore. In Cell Cycle, 2014
A few cell cycle related transcripts were downregulated (2.2-4.5-fold) on addition of miR-215: Mcm3, Dicer1, Cdc25A, Ick, Trip13 and Mcm10.
Thyroid hormone receptor interacting protein 13 (TRIP13) AAA-ATPase is a novel mitotic checkpoint-silencing protein.
Liu et al., Edmonton, Canada. In J Biol Chem, 2014
Previously, we and others have reported that TRIP13 AAA-ATPase binds to the mitotic checkpoint-silencing protein p31(comet).
Disassembly of mitotic checkpoint complexes by the joint action of the AAA-ATPase TRIP13 and p31(comet).
Hershko et al., Haifa, Israel. In Proc Natl Acad Sci U S A, 2014
We now show that HeLa cell extracts contain a factor that promotes ATP- and p31(comet)-dependent disassembly of a Cdc20-Mad2 subcomplex and identify it as Thyroid Receptor Interacting Protein 13 (TRIP13), an AAA-ATPase known to interact with p31(comet).
TRIP13 promotes error-prone nonhomologous end joining and induces chemoresistance in head and neck cancer.
D'Silva et al., Ann Arbor, United States. In Nat Commun, 2013
Here we describe a mechanism where the AAA-ATPase TRIP13 promotes treatment resistance.
Central region component1, a novel synaptonemal complex component, is essential for meiotic recombination initiation in rice.
Cheng et al., Beijing, China. In Plant Cell, 2013
CRC1 is orthologous to Saccharomyces cerevisiae pachytene checkpoint2 (Pch2) and Mus musculus THYROID receptor-interacting protein13 (TRIP13) and may be a conserved SC component.
A meta-analysis of gene expression data identifies a molecular signature characteristic for tumor-stage mycosis fungoides.
Tensen et al., Leiden, Netherlands. In J Invest Dermatol, 2012
We uncovered details of the immunophenotype, suggesting that MF originates from IL-32-producing cells and identified previously unreported therapeutic targets and/or diagnostic markers, for example, GTSF1 and TRIP13.
Identification of novel mitosis regulators through data mining with human centromere/kinetochore proteins as group queries.
Liu et al., Toledo, United States. In Bmc Cell Biol, 2011
Experimental validation found that KIAA1377 is a novel centrosomal protein that also associates with microtubules and midbody; while TRIP13 is a novel kinetochore protein and directly interacts with mitotic checkpoint silencing protein p31(comet).
Mouse TRIP13/PCH2 is required for recombination and normal higher-order chromosome structure during meiosis.
Keeney et al., New York City, United States. In Plos Genet, 2010
TRIP13 is required for recombination and normal higher-order chromosome structure during meiosis.
Mouse HORMAD1 and HORMAD2, two conserved meiotic chromosomal proteins, are depleted from synapsed chromosome axes with the help of TRIP13 AAA-ATPase.
Toth et al., Dresden, Germany. In Plos Genet, 2009
HORMAD1 and HORMAD2 are depleted from synapsed chromosome axes with the help of TRIP13.
Mouse pachytene checkpoint 2 (trip13) is required for completing meiotic recombination but not synapsis.
Schimenti et al., Ithaca, United States. In Plos Genet, 2007
results demonstrate that in mice, the primary meiotic function of TRIP13 is in recombination itself
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