One site mutation disrupts dimer formation in human DPP-IV proteins
about
Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1Dipeptidyl peptidase-4 and kidney fibrosis in diabetesDPP4 in DiabetesKv4.2 and accessory dipeptidyl peptidase-like protein 10 (DPP10) subunit preferentially form a 4:2 (Kv4.2:DPP10) channel complexInvolvement of DPP-IV catalytic residues in enzyme-saxagliptin complex formationRegulation of somatostatin receptor 4-mediated cytostatic effects by CD26 in malignant pleural mesotheliomaThe dimeric transmembrane domain of prolyl dipeptidase DPP-IV contributes to its quaternary structure and enzymatic activities.Investigation of the dimer interface and substrate specificity of prolyl dipeptidase DPP8.Structure-activity relationships of wheat flavone O-methyltransferase: a homodimer of convenience.Identification and partial characterization of the enzyme of omega: one of five putative DPP IV genes in Drosophila melanogasterHeparin oligosaccharides inhibit chemokine (CXC motif) ligand 12 (CXCL12) cardioprotection by binding orthogonal to the dimerization interface, promoting oligomerization, and competing with the chemokine (CXC motif) receptor 4 (CXCR4) N terminusDownregulation of Signaling-active IGF-1 by Dipeptidyl Peptidase IV (DPP-IV)Structure of human dipeptidyl peptidase 10 (DPPY): a modulator of neuronal Kv4 channels.A Porphyromonas gingivalis Periplasmic Novel Exopeptidase, Acylpeptidyl Oligopeptidase, Releases N-Acylated Di- and Tripeptides from Oligopeptides.Computational Analysis of Gynura bicolor Bioactive Compounds as Dipeptidyl Peptidase-IV Inhibitor.Hydrophilic residues surrounding the S1 and S2 pockets contribute to dimerisation and catalysis in human dipeptidyl peptidase 8 (DP8).The amino terminus extension in the long dipeptidyl peptidase 9 isoform contains a nuclear localization signal targeting the active peptidase to the nucleus.Concentration-dependent plasma protein binding of the novel dipeptidyl peptidase 4 inhibitor BI 1356 due to saturable binding to its target in plasma of mice, rats and humans.The role of renal dipeptidyl peptidase-4 in kidney disease: renal effects of dipeptidyl peptidase-4 inhibitors with a focus on linagliptin.
P2860
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P2860
One site mutation disrupts dimer formation in human DPP-IV proteins
description
2004 nî lūn-bûn
@nan
2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
One site mutation disrupts dimer formation in human DPP-IV proteins
@ast
One site mutation disrupts dimer formation in human DPP-IV proteins
@en
One site mutation disrupts dimer formation in human DPP-IV proteins
@en-gb
One site mutation disrupts dimer formation in human DPP-IV proteins
@nl
type
label
One site mutation disrupts dimer formation in human DPP-IV proteins
@ast
One site mutation disrupts dimer formation in human DPP-IV proteins
@en
One site mutation disrupts dimer formation in human DPP-IV proteins
@en-gb
One site mutation disrupts dimer formation in human DPP-IV proteins
@nl
prefLabel
One site mutation disrupts dimer formation in human DPP-IV proteins
@ast
One site mutation disrupts dimer formation in human DPP-IV proteins
@en
One site mutation disrupts dimer formation in human DPP-IV proteins
@en-gb
One site mutation disrupts dimer formation in human DPP-IV proteins
@nl
P2093
P2860
P356
P1476
One site mutation disrupts dimer formation in human DPP-IV proteins
@en
P2093
Chia-Hui Chien
Gu-Gang Chang
Li-Hao Huang
Po-Huang Liang
Yuan-Shou Chen
P2860
P304
52338-52345
P356
10.1074/JBC.M406185200
P407
P577
2004-09-24T00:00:00Z