Ask about this productRelated genes to: MAD2L1BP Blocking Peptide
- Gene:
- MAD2L1BP NIH gene
- Name:
- MAD2L1 binding protein
- Previous symbol:
- -
- Synonyms:
- CMT2, KIAA0110, dJ261G23.1
- Chromosome:
- 6p21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-06-23
- Date modifiied:
- 2015-08-25
Related products to: MAD2L1BP Blocking Peptide
Related articles to: MAD2L1BP Blocking Peptide
- - Source: PubMed
Suto KeitoTakei NorioYokoyama KeitoChiba MasahiroIshio TakashiMaeda MichiyukiGoto HidekiEndo TomoyukiTeshima TakanoriYang YibinNakagawa Masao - Inflammation and genomic instability are among the hallmarks of human cancer. Proinflammatory cytokines induce DNA damage through the accumulation of reactive oxygen and nitrogen species (RONS), which often leads to base alternations. The link between proinflammatory cytokines and chromosomal instability remains largely elusive. - Source: PubMed
Publication date: 2025/06/03
Gao YifengYin QingGamallat YaserGrant Michael GSnell Aidan HShi XingxingUlstad Lara NSingh ArshitaChen TinganJohnson Joseph OAvram DorinaWan Lixin - - Source: PubMed
Publication date: 2024/10/21
Suto KeitoTakei NorioYokoyama KeitoChiba MasahiroIshio TakashiMaeda MichiyukiGoto HidekiEndo TomoyukiTeshima TakanoriYang YibinNakagawa Masao - Covalent chemistry is a versatile approach for expanding the ligandability of the human proteome. Activity-based protein profiling (ABPP) can infer the specific residues modified by electrophilic compounds through competition with broadly reactive probes. However, the extent to which such residue-directed platforms fully assess the protein targets of electrophilic compounds in cells remains unclear. Here we evaluate a complementary protein-directed ABPP method that identifies proteins showing stereoselective reactivity with alkynylated, chiral electrophilic compounds-termed stereoprobes. Integration of protein- and cysteine-directed data from cancer cells treated with tryptoline acrylamide stereoprobes revealed generally well-correlated ligandability maps and highlighted features, such as protein size and the proteotypicity of cysteine-containing peptides, that explain gaps in each ABPP platform. In total, we identified stereoprobe binding events for >300 structurally and functionally diverse proteins, including compounds that stereoselectively and site-specifically disrupt MAD2L1BP interactions with the spindle assembly checkpoint complex leading to delayed mitotic exit in cancer cells. - Source: PubMed
Publication date: 2024/08/13
Njomen EvertHayward Rachel EDeMeester Kristen EOgasawara DaisukeDix Melissa MNguyen TraceyAshby PaigeSimon Gabriel MSchreiber Stuart LMelillo BrunoCravatt Benjamin F - PAR3/INSC/LGN form an evolutionarily conserved complex required for asymmetric cell division in the developing brain, but its post-developmental function and disease relevance in the peripheral nervous system (PNS) remains unknown. We mapped a new locus for axonal Charcot-Marie-Tooth disease (CMT2) and identified a missense mutation c.209 T > G (p.Met70Arg) in the INSC gene. Modeling the INSC variant in Drosophila, we showed that it caused proprioceptive defects in adult flies, leading to gait defects resembling those in CMT2 patients. Cellularly, PAR3/INSC/LGN dysfunction caused tubulin aggregation and necrotic neurodegeneration, with microtubule-stabilizing agents rescuing both morphological and functional defects of the INSC mutation in the PNS. Our findings underscore the critical role of the PAR3/INSC/LGN machinery in the adult PNS and highlight a potential therapeutic target for INSC-associated CMT2. - Source: PubMed
Publication date: 2024/04/08
Yeh Jui-YuChao Hua-ChuanHong Cheng-LiHung Yu-ChienTzou Fei-YangHsiao Cheng-TsungLi Jeng-LinChen Wen-JieChou Cheng-TaTsai Yu-ShuenLiao Yi-ChuLin Yu-ChunLin SueweiHuang Shu-YiKennerson MarinaLee Yi-ChungChan Chih-Chiang