PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16533812-8 2006 Concurrent with its effect on cell growth, overexpression of HDAC3 and other Class I HDACs inhibited basal and butyrate-induced p21 transcription in a Sp1/Sp3-dependent manner, whereas silencing of HDAC3 stimulated p21 promoter activity and expression. Butyrates 111-119 Sp3 transcription factor Homo sapiens 155-158 17241874-0 2007 Butyrate induces intestinal sodium absorption via Sp3-mediated transcriptional up-regulation of epithelial sodium channels. Butyrates 0-8 Sp3 transcription factor Homo sapiens 50-53 16732318-0 2006 Upregulation of BAK by butyrate in the colon is associated with increased Sp3 binding. Butyrates 23-31 Sp3 transcription factor Homo sapiens 74-77 16732318-7 2006 We have shown that both Sp1 and Sp3 bind, but upon butyrate treatment Sp1 binding decreases in favour of Sp3 binding. Butyrates 51-59 Sp3 transcription factor Homo sapiens 32-35 16732318-7 2006 We have shown that both Sp1 and Sp3 bind, but upon butyrate treatment Sp1 binding decreases in favour of Sp3 binding. Butyrates 51-59 Sp3 transcription factor Homo sapiens 105-108 26159698-8 2015 Gel mobility shift assay identified an enhanced Sp3 protein binding on the human NHE8 basal promoter region upon butyrate stimulation. Butyrates 113-121 Sp3 transcription factor Homo sapiens 48-51 26159698-9 2015 Furthermore, Sp3 acetylation modification is involved in butyrate-mediated NHE8 activation in Caco-2 cells. Butyrates 57-65 Sp3 transcription factor Homo sapiens 13-16 26159698-10 2015 Our findings suggest that the mechanism of butyrate action on NHE8 expression involves enhanced Sp3 interaction at the basal promoter region of the human NHE8 gene promoter to activate NHE8 gene transcription. Butyrates 43-51 Sp3 transcription factor Homo sapiens 96-99 12626711-5 2003 The effect of butyrate and TSA maps to a single Sp1 site present in the proximal promoter of the gene, which is able to bind Sp1 and Sp3 proteins. Butyrates 14-22 Sp3 transcription factor Homo sapiens 133-136 16456404-11 2006 Analysis of the hIGFBP-3 promoter demonstrated a butyrate-response element that included the binding sites for p300 and Sp1/Sp3. Butyrates 49-57 Sp3 transcription factor Homo sapiens 124-127 16456404-13 2006 Because Sp3 represses the initiation of transcription, we studied whether butyrate induced Sp3 acetylation. Butyrates 74-82 Sp3 transcription factor Homo sapiens 91-94 16456404-14 2006 Electrophoretic mobility shift assays of nuclei extracted from Caco-2 cells treated with 5 mmol/L butyrate demonstrated an extra, heavier band in addition to the Sp3-DNA binding in untreated cells. Butyrates 98-106 Sp3 transcription factor Homo sapiens 162-165 16456404-15 2006 This corresponded to a protein, detected only in butyrate treated cells, that was identified both by an anti-Sp3 antibody and by an anti-acetyl lysine antibody. Butyrates 49-57 Sp3 transcription factor Homo sapiens 109-112 16456404-16 2006 CONCLUSIONS: This study demonstrates that butyrate increases the acetylation of a nonhistone protein, Sp3, catalyzed by p300 acetyltransferase activity. Butyrates 42-50 Sp3 transcription factor Homo sapiens 102-105 12840228-6 2003 Promoters of butyrate-responsive genes have butyrate response elements, and the action of butyrate is often mediated through Sp1/Sp3 binding sites (e.g., p21(Waf1/Cip1)). Butyrates 13-21 Sp3 transcription factor Homo sapiens 129-132 16081043-2 2005 We have characterized the role of the C-terminal D-domains of both Sp1 and Sp3 proteins in the activation of this promoter in response to butyrate treatment of Hep G2 cells. Butyrates 138-146 Sp3 transcription factor Homo sapiens 75-78 15650166-6 2005 Butyrate induced the formation of a group of novel complexes, including several Sp3-containing complexes, one Sp1-containing complex, and several other complexes that were not identified with antibodies to Sp1 or Sp3. Butyrates 0-8 Sp3 transcription factor Homo sapiens 80-83 15650166-6 2005 Butyrate induced the formation of a group of novel complexes, including several Sp3-containing complexes, one Sp1-containing complex, and several other complexes that were not identified with antibodies to Sp1 or Sp3. Butyrates 0-8 Sp3 transcription factor Homo sapiens 213-216 15650166-10 2005 The results suggest that induction of the KSHV lytic cycle by butyrate is mediated through interactions at the Sp1/Sp3 site located 103 to 112 nucleotides upstream of the translational initiation of ORF50 presumably by enhancing the binding of Sp1 to this site. Butyrates 62-70 Sp3 transcription factor Homo sapiens 115-118 11517158-0 2001 Butyrate, a histone deacetylase inhibitor, activates the human IGF binding protein-3 promoter in breast cancer cells: molecular mechanism involves an Sp1/Sp3 multiprotein complex. Butyrates 0-8 Sp3 transcription factor Homo sapiens 154-157