Ask about this productRelated genes to: TRIP13 antibody
- Gene:
- TRIP13 NIH gene
- Name:
- thyroid hormone receptor interactor 13
- Previous symbol:
- -
- Synonyms:
- 16E1BP
- Chromosome:
- 5p15.33
- Locus Type:
- gene with protein product
- Date approved:
- 2000-01-04
- Date modifiied:
- 2016-10-05
Related products to: TRIP13 antibody
Related articles to: TRIP13 antibody
- Thyroid hormone receptor-interacting protein 13 (TRIP13), an enzyme from the AAA-ATPase family, facilitates the assembly or disassembly of protein complexes and participates in various biological processes. However, its impact on cancer immune infiltration and pan-cancer prognosis remains largely unexplored. - Source: PubMed
Publication date: 2026/04/22
Zhao YuanqiaoZhao YongqiLiu RuilinLi JingWang Yinhuai - The synaptonemal complex (SC) is a highly ordered proteinaceous structure that assembles between homologous chromosomes during the prophase I of meiosis. Conserved as a tripartite architecture across species, the SC plays a central role in chromosome synapsis, meiotic recombination, and faithful chromosome segregation. This review marks the 70th anniversary of the discovery of the synaptonemal complex by Montrose Moses in 1956. In mammals, the SC is composed of eight core (canonical) structural proteins: SYCP1, SYCP2, SYCP3, SYCE1, SYCE2, SYCE3, SIX6OS1, and TEX12. The archetypal SC consists of two lateral elements (SYCP2 and SYCP3), a central element (SYCE1/2/3, SIX6OS1, and TEX12), and numerous transverse filaments (SYCP1). A shared structural feature of SC components is the presence of coiled-coil domains. Although the tripartite organization of the SC is evolutionarily conserved, its constituent proteins exhibit little to no sequence homology across species. In addition to these core components, a number of proteins, including HORMAD1, HORMAD2, TRIP13, SKP1, CDCA5 (Sororin), UBE2I (UBC9), SYCP2L, HSPA2, PSMA8, and FKBP6, associate with the SC. Beyond serving as a structural scaffold essential for homolog synapsis, SC proteins interact with key recombination factors such as DMC1, RAD51, and TEX11, thereby regulating recombination progression and crossover formation. Genetic, biochemical, and structural analyses of SC components have provided important mechanistic insights into SC assembly and function, as well as their clinical relevance to non-obstructive azoospermia (NOA) and premature ovarian insufficiency (POI) in humans. - Source: PubMed
Publication date: 2026/04/30
Yang FangWang P Jeremy - Juvenile European seabass (Dicentrarchus labrax) were exposed to environmentally relevant 6PPD-quinone (2.85 µg/L) for five days to evaluate transcriptional, oxidative, and antioxidant responses and histopathology. The liver showed the strongest gene induction: cdc28 (∼75×), bax (48×), spc25 (45×), and hsp70 (42.5×). Kidney responses were moderate, with bax up ∼5.5× and hsp70 and casp9 ∼2×, while pcna, cenpi, cenpf, and cdc28 were downregulated (0.32-0.66×). Spleen and intestine exhibited marked upregulation of spc25, cenpf, cenpi, and bcl2 (up to ∼34.6× and 16×, respectively), whereas trip13, bax, and bcl2 were unchanged in spleen. Gills displayed strong trip13 (∼32.5×) and spc25 (∼13.7×) induction but downregulation of bax and bcl2. Oxidative DNA damage (8-OHdG) increased in all organs except skin, peaking in spleen; N-myc protein rose in spleen. Catalase activity decreased in liver, kidney, and skin but increased in spleen; MDA decreased in most tissues except skin. Histopathology revealed multifocal hepatic necrosis and vacuolation, splenic fibrosis with hemorrhage and lymphoid depletion, intestinal villous sloughing with submucosal inflammation, severe myositis, epidermal desquamation, and gill lamellar damage. In conclusion, short-term exposure to environmentally relevant 6PPD-quinone elicits organ-specific molecular, oxidative, and pathological alterations in juvenile seabass, indicating significant multisystemic toxicity and potential population-level risks and warrants further ecological investigation. - Source: PubMed
Publication date: 2026/04/19
Abo-Al-Ela Haitham GAl Wakeel Rasha AZaki Abeer GamalElkatatny Nasema MahmoudAbdelatty AlaaAssas MonaZaid Attia A AbouElnaggar Mahmoud MAbdo Safaa E - Cancers driven by a loss of tumor suppressor function lack actionable druggable targets. We investigated the cell cycle-specific mechanisms underlying the efficacy of co-targeting TRIP13 and Aurora A by defining their key functions in Rb-deficient cancers to develop effective treatment strategies. - Source: PubMed
Publication date: 2026/04/21
Yapindi LacinGhosh SomaShen LiDiao LixiaWang JingJohnson Faye M - Prostate cancer (PCa), a common malignancy, is a leading cause of cancer-related deaths among men. Advances in high-throughput technologies have led to the identification of various genetic alterations, including amplifications, deletions, mutations, gene fusions, and aberrant gene expressions, associated with PCa initiation and progression. Identifying key drivers of tumor progression and their underlying signaling pathways contributes to early diagnosis and therapeutic targeting. Here, we showed that thyroid hormone receptor-interacting protein 13 (TRIP13), a member of the AAA-ATPase family is overexpressed in PCa. Additionally, we observed amplification of the TRIP13 locus in a small subset of PCa samples. Functional studies demonstrated that TRIP13 knockdown in PCa cells reduced their proliferation and invasion. Furthermore, ectopic overexpression of TRIP13 in prostate epithelial cells (RWPE-1) resulted in enhanced cell invasion. Additionally, pharmacologic inhibition of TRIP13 by the small molecule inhibitor DCZ0415 suppressed PCa cell proliferation, induced apoptosis, modulated markers of the epithelial-mesenchymal transition (EMT), and inhibited tumor growth. Overall, these findings highlight a functional role for TRIP13 in PCa progression and demonstrate its potential as a therapeutic target in TRIP13-overexpressing PCa. - Source: PubMed
Publication date: 2026/04/17
Afaq FarrukhPathi Satya SChakravarthi Balabhadrapatruni V S KChandrashekar Darshan ShimogaCarskadon ShannonDiffalha Sameer AlKunju Lakshmi PPalanisamy NallasivamManne UpenderSingh RajeshVarambally Sooryanarayana