PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15037661-0 2004 The CtBP2 co-repressor is regulated by NADH-dependent dimerization and possesses a novel N-terminal repression domain. NAD 39-43 C-terminal binding protein 2 Homo sapiens 4-9 15037661-5 2004 Here we extend the functional characterization of CtBP by demonstrating that amino acid substitutions at Gly189 in the conserved NAD+-binding fold both abrogate the ability of CtBP2 to homodimerize and are associated with a dramatic loss of co-repressor activity. NAD 129-133 C-terminal binding protein 2 Homo sapiens 176-181 15037661-8 2004 Our results suggest a model in which CtBP2 co-repressor function is regulated, at least in part, through the effect of NADH on CtBP2 homodimerization. NAD 119-123 C-terminal binding protein 2 Homo sapiens 37-42 15037661-8 2004 Our results suggest a model in which CtBP2 co-repressor function is regulated, at least in part, through the effect of NADH on CtBP2 homodimerization. NAD 119-123 C-terminal binding protein 2 Homo sapiens 127-132 33524397-2 2021 We have previously shown that NAD(H) promotes the assembly of similar tetramers from either human CtBP1 and CtBP2 and that CtBP2 tetramer destabilizing mutants are defective for oncogenic activity. NAD 30-36 C-terminal binding protein 2 Homo sapiens 108-113 33264605-4 2021 Here, we present the cryoelectron microscopic structures of two different constructs of CtBP2 corroborating that the native state of CtBP2 in the presence of NADH is tetrameric. NAD 158-162 C-terminal binding protein 2 Homo sapiens 88-93 33264605-4 2021 Here, we present the cryoelectron microscopic structures of two different constructs of CtBP2 corroborating that the native state of CtBP2 in the presence of NADH is tetrameric. NAD 158-162 C-terminal binding protein 2 Homo sapiens 133-138 11163272-5 2000 The A domain mediates assembly of RIBEYE into large structures, whereas the B domain binds NAD(+) with high affinity, similar to 2-hydroxyacid dehydrogenases. NAD 91-97 C-terminal binding protein 2 Homo sapiens 34-40 34728642-3 2021 The repressor activity of CtBP2 is reciprocally regulated by NADH and acyl-CoAs. NAD 61-65 C-terminal binding protein 2 Homo sapiens 26-31 34997967-0 2022 NADH/NAD+ binding and linked tetrameric assembly of the oncogenic transcription factors CtBP1 and CtBP2. NAD 0-4 C-terminal binding protein 2 Homo sapiens 98-103 34997967-0 2022 NADH/NAD+ binding and linked tetrameric assembly of the oncogenic transcription factors CtBP1 and CtBP2. NAD 5-9 C-terminal binding protein 2 Homo sapiens 98-103 24657618-3 2014 Crystal structures of human CtBP1 and CtBP2 in complex with MTOB and NAD(+) revealed two key features: a conserved tryptophan that likely contributes to substrate specificity and a hydrophilic cavity that links MTOB with an NAD(+) phosphate. NAD 69-75 C-terminal binding protein 2 Homo sapiens 38-43 25429601-3 2014 CtBP1 and CtBP2 are closely related and act as transcriptional corepressors when activated by nicotinamide adenine dinucleotide binding to their dehydrogenase domains. NAD 94-127 C-terminal binding protein 2 Homo sapiens 10-15 30585266-0 2018 The intracellular NADH level regulates atrophic nonunion pathogenesis through the CtBP2-p300-Runx2 transcriptional complex. NAD 18-22 C-terminal binding protein 2 Homo sapiens 82-87 30585266-5 2018 The lower NADH level in atrophic nonunion tissues disrupted CtBP2 dimerization and enhanced the blockage of the accessibility of the p300-Runx2 complex to the promoters of a series of bone-related target genes, such as OSC, ALPL, COL1A1, IBSP, SPP1 and MMP13. NAD 10-14 C-terminal binding protein 2 Homo sapiens 60-65 30585266-7 2018 In conclusion, our study revealed that NADH levels determine the expression of bone formation and development of related genes through affecting the dissociation or binding of CtBP2 to the p300-Runx2 complex. NAD 39-43 C-terminal binding protein 2 Homo sapiens 176-181 30585266-8 2018 These results represent a conserved mechanism, by which CtBP2 serves as a NADH-dependent repressor of the p300-Runx2 transcriptional complex and thus affects bone formation. NAD 74-78 C-terminal binding protein 2 Homo sapiens 56-61 29700119-4 2018 Here, multi-angle light scattering (MALS) data established the NAD+- and NADH-dependent assembly of CtBP1 and CtBP2 into tetramers. NAD 63-67 C-terminal binding protein 2 Homo sapiens 110-115 29700119-4 2018 Here, multi-angle light scattering (MALS) data established the NAD+- and NADH-dependent assembly of CtBP1 and CtBP2 into tetramers. NAD 73-77 C-terminal binding protein 2 Homo sapiens 110-115 29700119-5 2018 An examination of subunit interactions within CtBP1 and CtBP2 crystal lattices revealed that both share a very similar tetrameric arrangement resulting from assembly of two dimeric pairs, with specific interactions probably being sensitive to NAD(H) binding. NAD 243-249 C-terminal binding protein 2 Homo sapiens 56-61 28202712-0 2017 RIBEYE(B)-domain binds to lipid components of synaptic vesicles in an NAD(H)-dependent, redox-sensitive manner. NAD 70-76 C-terminal binding protein 2 Homo sapiens 0-6 28202712-3 2017 RIBEYE consists of a unique A-domain and a carboxyterminal B-domain, which binds NAD(H). NAD 81-87 C-terminal binding protein 2 Homo sapiens 0-6 28202712-8 2017 Interestingly, binding of liposomes to RIBEYE(B) depends on NAD(H) in a redox-sensitive manner. NAD 60-66 C-terminal binding protein 2 Homo sapiens 39-45 18664567-7 2008 A RIBEYE point mutant (RE(B)E844Q) that no longer interacted with Munc119 still bound NADH, arguing that binding of Munc119 and NADH to RIBEYE are independent from each other. NAD 128-132 C-terminal binding protein 2 Homo sapiens 136-142 25483087-5 2014 CSCs demonstrated significant upregulation of CtBP1 and CtBP2 levels (mRNA and protein) and activity partly due to increased NADH/NAD ratio, as well as increased TCF/LEF transcriptional activity, compared to respective controls. NAD 125-129 C-terminal binding protein 2 Homo sapiens 56-61 25483087-5 2014 CSCs demonstrated significant upregulation of CtBP1 and CtBP2 levels (mRNA and protein) and activity partly due to increased NADH/NAD ratio, as well as increased TCF/LEF transcriptional activity, compared to respective controls. NAD 125-128 C-terminal binding protein 2 Homo sapiens 56-61 20463219-5 2010 We show that the flexible hinge 2 linker region of RIBEYE(B) domain that connects the nicotinamide adenine dinucleotide (NADH)-binding subdomain with the substrate-binding subdomain (SBD) binds to the C terminus of GCAP2. NAD 86-119 C-terminal binding protein 2 Homo sapiens 51-57 20463219-5 2010 We show that the flexible hinge 2 linker region of RIBEYE(B) domain that connects the nicotinamide adenine dinucleotide (NADH)-binding subdomain with the substrate-binding subdomain (SBD) binds to the C terminus of GCAP2. NAD 121-125 C-terminal binding protein 2 Homo sapiens 51-57 20463219-6 2010 We demonstrate that the RIBEYE-GCAP2 interaction is induced by the binding of NADH to RIBEYE. NAD 78-82 C-terminal binding protein 2 Homo sapiens 24-30 20463219-6 2010 We demonstrate that the RIBEYE-GCAP2 interaction is induced by the binding of NADH to RIBEYE. NAD 78-82 C-terminal binding protein 2 Homo sapiens 86-92 18664567-5 2008 The PrBP/delta homology domain of Munc119 is essential for the interaction with the NADH binding region of RIBEYE(B) domain. NAD 84-88 C-terminal binding protein 2 Homo sapiens 107-113 18664567-7 2008 A RIBEYE point mutant (RE(B)E844Q) that no longer interacted with Munc119 still bound NADH, arguing that binding of Munc119 and NADH to RIBEYE are independent from each other. NAD 86-90 C-terminal binding protein 2 Homo sapiens 2-8 16762039-6 2006 Here, we show that HIC1 interacts with both CtBP1 and CtBP2 and that this interaction is stimulated by agents increasing NADH levels. NAD 121-125 C-terminal binding protein 2 Homo sapiens 54-59 18685021-7 2008 The docking site for RIBEYE(A) on RIBEYE(B) is topographically and functionally different from the RIBEYE(B) homodimerization interface and is negatively regulated by nicotinamide adenine dinucleotide. NAD 167-200 C-terminal binding protein 2 Homo sapiens 21-27 18685021-7 2008 The docking site for RIBEYE(A) on RIBEYE(B) is topographically and functionally different from the RIBEYE(B) homodimerization interface and is negatively regulated by nicotinamide adenine dinucleotide. NAD 167-200 C-terminal binding protein 2 Homo sapiens 34-40 18685021-7 2008 The docking site for RIBEYE(A) on RIBEYE(B) is topographically and functionally different from the RIBEYE(B) homodimerization interface and is negatively regulated by nicotinamide adenine dinucleotide. NAD 167-200 C-terminal binding protein 2 Homo sapiens 34-40 16356938-1 2006 CtBP family members, CtBP1 and CtBP2, are unique transcriptional regulators that adapt a metabolic enzyme fold, and their activities are regulated by NAD(H)-binding. NAD 150-156 C-terminal binding protein 2 Homo sapiens 31-36