About: Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum

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About: Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum Goto Sponge NotDistinct Permalink

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rdf:type	Item
description	artículu científicu espublizáu en 1993 (ast) vědecký článek publikovaný v roce 1993 (cs) 1993 թվականի հունիսին հրատարակված գիտական հոդված (hy) 1993 թուականի Յունիսին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в червні 1993 (uk) vedecký článok (publikovaný 1993/06/15) (sk) مقالة علمية (نشرت في 15-6-1993) (ar) article scientifique publié en 1993 (fr) scientific journal article (en) im Juni 1993 veröffentlichter wissenschaftlicher Artikel (de) wetenschappelijk artikel (gepubliceerd op 1993/06/15) (nl)
publication date	wds:Q28117412-B8D547DB-7154-414A-A5C6-53253412327B
publication date	1993-06-15 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28117412-71A4EDA3-B3C8-487F-9A52-B54BA42AFD54
language of work or name	English
cites work	wds:Q28117412-03F5D6C0-801D-40BB-8654-0D6E0F4B28BF wds:Q28117412-7299E63C-09DC-4CA1-AEEA-A2D024573879 wds:Q28117412-A0C4D83B-8E7B-4F8D-8310-898C3D43792F wds:Q28117412-C43F0FE6-BFB0-41D7-8DDE-7C236BA934FA wds:Q28117412-E2F20811-C6CB-4F46-9368-F0259AD7BE48 wds:Q28117412-EE19A200-79A8-46EC-B605-BB1604326577 wds:Q28117412-F61F2E36-1A58-4622-9935-39D13728961A
cites work	Are diprotin A (Ile-Pro-Ile) and diprotin B (Val-Pro-Leu) inhibitors or substrates of dipeptidyl peptidase IV? Proline residues in the maturation and degradation of peptide hormones and neuropeptides Extended investigation of the substrate specificity of dipeptidyl peptidase IV from pig kidney Liver dipeptidyl aminopeptidase IV hydrolyzes substance P Studies on dipeptidyl(amino)peptidase IV (glycyl-proline naphthylamidase) Peptidases II. Localization of dipeptidylpeptidase IV (DPP IV). Histochemical and biochemical study Catabolism of rat growth hormone-releasing factor(1-29) amide in rat serum and liver
author name string	wds:Q28117412-387C0F7E-3683-4683-8924-D4232FA570A4 wds:Q28117412-749BC4D1-FF13-409F-801C-5160CCBB5A6B wds:Q28117412-DE6B45A9-E636-435B-9FEF-43AD7218FAD7
OpenCitations bibliographic resource ID	wds:Q28117412-38CCBF69-8DDB-40DE-8C08-D860DC2EEB33
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/2582842
author name string	B. Gallwitz R. Mentlein W. E. Schmidt
OpenCitations bibliographic resource ID	2582842
rdfs:label	Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum (en) Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum (nl) Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum (ast)
skos:prefLabel	Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum (en) Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum (nl) Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum (ast)
name	Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum (en) Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum (nl) Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum (ast)
title	wds:Q28117412-EF6E611E-3119-435C-968E-3F34F1B555FF
title	Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum (en)
page(s)	wds:Q28117412-1BCA3C81-8D4F-4E42-B516-897C94D5907A
page(s)	829–835
instance of	wds:Q28117412-87EE4D7B-A8DD-4688-B524-60D33D8BE628
instance of	scholarly article
main subject	wds:Q28117412-991C35F6-3028-424D-AC4D-BEB4D2FA1ECD wds:Q28117412-C931722E-8473-44C6-A0E7-A18C5E5DF199
main subject	wd:Q412214 serine-type endopeptidase activity
PubMed ID	wds:Q28117412-DBFDE0FC-EFDF-47BF-B52A-9450D958A563
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8100523
PubMed ID	8100523
published in	wds:Q28117412-48331D4F-EA74-40C1-A492-290F9B3990A4
published in	FEBS Journal
issue	wds:Q28117412-57188610-9C99-43AC-8B30-C40EAE674EB6
volume	wds:Q28117412-8E9ABCB7-D3EA-4F0A-8B8D-617DB6E7644C
issue	3
volume	214
DOI	wds:Q28117412-4B56E1D6-FC77-40BB-AD89-2619B9F93A33
DOI	http://dx.doi.org/10.1111/J.1432-1033.1993.TB17986.X
DOI	10.1111/J.1432-1033.1993.TB17986.X
ResearchGate publication ID	wds:Q28117412-0FE16992-A014-4F54-B94A-7A8B7EE40A1D
ResearchGate publication ID	15097775
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28117412
is cites work of	Neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY are novel substrates of fibroblast activation protein-α Encapsulated, genetically engineered cells, secreting glucagon-like peptide-1 for the treatment of non-insulin-dependent diabetes mellitus Genetically modified rice seeds accumulating GLP-1 analogue stimulate insulin secretion from a mouse pancreatic beta-cell line. Restoration of the insulinotropic effect of glucose-dependent insulinotropic polypeptide contributes to the antidiabetic effect of dipeptidyl peptidase-4 inhibitors. Exendin-4 increases blood glucose levels acutely in rats by activation of the sympathetic nervous system GLP-1 receptor agonists for individualized treatment of type 2 diabetes mellitus The gut-renal axis: do incretin-based agents confer renoprotection in diabetes? Investigating G protein signalling bias at the glucagon-like peptide-1 receptor in yeast Pharmacokinetic, insulinotropic, and glucagonostatic properties of GLP-1 [7-36 amide] after subcutaneous injection in healthy volunteers. Dose-response-relationships. Incretin mimetics as emerging treatments for type 2 diabetes Partial D-amino acid substitution: Improved enzymatic stability and preserved Ab recognition of a MUC2 epitope peptide Dipeptidyl-peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV. Regulation of pancreatic PC1 and PC2 associated with increased glucagon-like peptide 1 in diabetic rats What mediates the benefits associated with dipeptidyl peptidase-IV inhibition? Improved glucose tolerance and insulin secretion by inhibition of dipeptidyl peptidase IV in mice. Cardiovascular biology of the incretin system Treatment of diabetes with glucagon-like peptide-1 gene therapy Dipeptidyl peptidase IV (DPIV/CD26) degradation of glucagon. Characterization of glucagon degradation products and DPIV-resistant analogs Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion. Identification of a bioactive domain in the amino-terminus of glucose-dependent insulinotropic polypeptide (GIP). A locked, dimeric CXCL12 variant effectively inhibits pulmonary metastasis of CXCR4-expressing melanoma cells due to enhanced serum stability Current and emerging concepts on the role of peripheral signals in the control of food intake and development of obesity Therapeutic potential of dipeptidyl peptidase IV inhibitors for the treatment of type 2 diabetes The 3D structure of rat DPPIV/CD26 as obtained by cryo-TEM and single particle analysis Dipeptidyl-peptidase IV (CD26)--role in the inactivation of regulatory peptides Investigation of the dimer interface and substrate specificity of prolyl dipeptidase DPP8. Emerging DPP-4 inhibitors: focus on linagliptin for type 2 diabetes

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