Over 300 Bi-binding peptides from 166 proteins in H. pylori were identified by Bi-IMAC. Bi(3+) exhibits high selectivity towards peptide enriched by cysteines and histidines with dominated motif patterns of CXnC, CXnH and HXnH. Structural rationalization and functional categorization on the identified Bi-binding peptides and proteins provide an insight into the inhibitory action of bismuth drugs.
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Bio-coordination of bismuth in Helicobacter pylori revealed by immobilized metal affinity chromatography.
Chem Commun (Camb)
November 2015
Department of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, P. R. China.
Over 300 Bi-binding peptides from 166 proteins in H. pylori were identified by Bi-IMAC. Bi(3+) exhibits high selectivity towards peptide enriched by cysteines and histidines with dominated motif patterns of CXnC, CXnH and HXnH.
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Biochim Biophys Acta
May 2015
Department of Internal Medicine I, Regensburg University Hospital, Regensburg, Germany. Electronic address:
The syntrophins alpha (SNTA) and beta 2 (SNTB2) are molecular adaptor proteins shown to stabilize ABCA1, an essential regulator of HDL cholesterol. Furthermore, SNTB2 is involved in glucose stimulated insulin release. Hyperglycemia and dyslipidemia are characteristic features of the metabolic syndrome, a serious public health problem with rising prevalence.
View Article and Find Full Text PDFOverexpression of the PDZ1 domain of PDZK1 blocks the activity of hepatic scavenger receptor, class B, type I by altering its abundance and cellular localization.
J Biol Chem
August 2008
Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
PDZK1 is a four-PDZ domain-containing scaffold protein that, via its first PDZ domain (PDZ1), binds to the C terminus of the high density lipoprotein (HDL) receptor scavenger receptor, class B, type I (SR-BI). Abolishing PDZK1 expression in PDZK1 knock-out (KO) mice leads to a post-transcriptional, tissue-specific decrease in SR-BI protein level and an increase in total plasma cholesterol carried in abnormally large HDL particles. Here we show that, although hepatic overexpression of PDZK1 restored normal SR-BI protein abundance and function in PDZK1 KO mice, hepatic overexpression of only the PDZ1 domain was not sufficient to restore normal SR-BI function.
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