Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog
about
DPP10 modulates Kv4-mediated A-type potassium channelsRole 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 CARMA1One site mutation disrupts dimer formation in human DPP-IV proteinsModulation of Kv4.2 channel expression and gating by dipeptidyl peptidase 10 (DPP10)Stromal cell-derived factors 1alpha and 1beta, inflammatory protein-10 and interferon-inducible T cell chemo-attractant are novel substrates of dipeptidyl peptidase 8Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IVRegulation of glucose homeostasis by GLP-1The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanismCrystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formationInvolvement of DPP-IV catalytic residues in enzyme-saxagliptin complex formationThe first structure of dipeptidyl-peptidase III provides insight into the catalytic mechanism and mode of substrate bindingDipeptidyl Aminopeptidase IV from Stenotrophomonas maltophilia Exhibits Activity against a Substrate Containing a 4-Hydroxyproline ResidueInduced-fit mechanism for prolyl endopeptidase.Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidaseStructure and Catalysis of Acylaminoacyl Peptidase: CLOSED AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASEStructures of Human DPP7 Reveal the Molecular Basis of Specific Inhibition and the Architectural Diversity of Proline-Specific PeptidasesStructural evidence that puromycin hydrolase is a new type of aminopeptidase with a prolyl oligopeptidase family foldCrystal structures of Trypanosoma brucei oligopeptidase B broaden the paradigm of catalytic regulation in prolyl oligopeptidase family enzymesS46 Peptidases are the First Exopeptidases to be Members of Clan PACatalytically distinct states captured in a crystal lattice: the substrate-bound and scavenger states of acylaminoacyl peptidase and their implications for functionalityAnagliptin, a potent dipeptidyl peptidase IV inhibitor: its single-crystal structure and enzyme interactionsEffects of Glycosylation on the Enzymatic Activity and Mechanisms of ProteasesRegulation of Chemokine Activity - A Focus on the Role of Dipeptidyl Peptidase IV/CD26Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity.Selective inhibition of fibroblast activation protein protease based on dipeptide substrate specificity.Molecular cloning of the precursor polypeptide of mastoparan B and its putative processing enzyme, dipeptidyl peptidase IV, from the black-bellied hornet, Vespa basalis.Structure, Function, and Evolution of Coronavirus Spike Proteins.C-peptide microheterogeneity in type 2 diabetes populations.Building multidimensional biomarker views of type 2 diabetes on the basis of protein microheterogeneityIsolation of dipeptidyl peptidase IV (DP 4) isoforms from porcine kidney by preparative isoelectric focusing to improve crystallization.The 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.Nuclear localization of CD26 induced by a humanized monoclonal antibody inhibits tumor cell growth by modulating of POLR2A transcriptionThe dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.Receptor recognition mechanisms of coronaviruses: a decade of structural studies.The metabolic serine hydrolases and their functions in mammalian physiology and disease.Ligand deconstruction: Why some fragment binding positions are conserved and others are notHot spot analysis for driving the development of hits into leads in fragment-based drug discovery.Inhibitors of dipeptidyl peptidase IV: a novel approach for the prevention and treatment of Type 2 diabetes?
P2860
Q24292726-4A047A56-E9C0-4123-B694-BEDB215AD4A0Q24293344-79B6C09D-0BD1-4526-ADAD-C837BA5A9E63Q24296240-69704960-9F3D-4531-AFCC-DF1D94EAEEB6Q24305361-4457E2E3-AF8E-4B17-A08C-C0D247F406DBQ24305686-4D1F7EDA-1640-49A4-83B2-989E93AFEBCAQ24313619-366B23A8-000C-4074-8670-642686E66AABQ24543939-FC54BBFE-B4FC-4609-933A-2715F678DA1AQ24563430-15EF1F1A-3A42-48E6-BAB4-2CC4C678DB0BQ27640960-F979F677-A046-43DC-B39E-71DA03558FA1Q27642932-7539D019-C470-4FBA-B6B9-6AE2F3408888Q27649728-0DB9C8A7-9178-4B9D-A0EE-5A46C8640EE6Q27650815-D78446B0-795E-48D5-AF97-342076113BA2Q27652311-3DFD06D2-5AD1-4930-B841-F5DAD06E85DBQ27661330-617E5FEF-3866-4930-8F60-19C143F90175Q27662174-AE14AFC9-EE0C-4338-AAD6-678D5E24658DQ27665946-AFC102E0-8B52-406D-A94D-9196CE7920A1Q27672453-6415305A-A07A-4C22-8251-AF9FC027A10DQ27673668-4A3E2464-159A-4DD2-BC92-E51E7F5C26EFQ27680672-34485E44-0521-40C8-AF59-E03EBDDF3C38Q27683781-6F12D6CE-9136-4AE7-A6EC-D83B49110D04Q27698250-71B3CEF4-21AE-4C9F-855E-7747E80F416FQ27701492-C6D2CAA7-96FF-4588-8FD2-6266618F976DQ28069869-3E11A80E-A2CB-41E3-873C-85F4FAFB27FAQ28072580-03719527-A170-4FF8-9B3A-4A5DA03020D5Q30152912-25A6B6D9-F14D-4ED9-8ED3-9A9D08F4BB4EQ33231553-D8EB3D4E-3219-49B9-B884-3B9028687F76Q33273703-B90030A0-AE4E-4BB3-AD8E-B74A6FADF8C1Q33760875-AEC4A65A-6843-4EC9-8C0D-CDF88B2679BBQ33764455-D1913D10-40CA-47A7-A93E-CA4775AB74B3Q33845667-E3987B90-C333-4F91-975B-7B07E5415493Q33927989-2596BF50-ECF9-4F98-9D8C-989FFCB48E3AQ34284911-9C06FA2B-54E7-4FDE-A570-F7E24C32F314Q34573849-E95EAE47-035F-46D5-B428-6A7562CF77A5Q34701204-6B58E8FB-3F92-4DB4-A082-05957B53C591Q35022184-919BCDCC-3021-4C63-9721-A536B4A7C800Q35115572-FEE72EFC-44E7-4315-8587-F13AC48B9937Q35333042-ECEB4014-72D1-4BE9-AE65-21397D78C851Q35616254-893DF18D-E84B-49F7-AB1E-FC88ABB5C5ACQ35690787-4B058F40-974F-45BA-AD36-FC56F8134CA9Q35871904-9065332E-A8EB-4DA5-904A-B091F5C89BB4
P2860
Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Crystal structure of human dip ...... omplex with a substrate analog
@ast
Crystal structure of human dip ...... omplex with a substrate analog
@en
Crystal structure of human dip ...... omplex with a substrate analog
@nl
type
label
Crystal structure of human dip ...... omplex with a substrate analog
@ast
Crystal structure of human dip ...... omplex with a substrate analog
@en
Crystal structure of human dip ...... omplex with a substrate analog
@nl
prefLabel
Crystal structure of human dip ...... omplex with a substrate analog
@ast
Crystal structure of human dip ...... omplex with a substrate analog
@en
Crystal structure of human dip ...... omplex with a substrate analog
@nl
P2093
P3181
P356
P1476
Crystal structure of human dip ...... omplex with a substrate analog
@en
P2093
Finn C Wiberg
Hanne B Rasmussen
Nicolai Wagtmann
Sven Branner
P3181
P356
10.1038/NSB882
P577
2003-01-01T00:00:00Z