PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34702509-3 2021 For these purposes, a group of Gly-Pro amides deriving from several near-infrared fluorophores were designed on the basis of the unique prolyl-cleaving dipeptidease activity of CD26, while molecular docking simulations were applied to assess the possibility of the designed amides as CD26 specific substrates. Amides 274-280 dipeptidyl peptidase 4 Homo sapiens 284-288 8100523-7 1993 When human serum was incubated with GIP or GLP-1(7-36)amide the same fragments as with the purified dipeptidyl-peptidase IV, namely the des-Xaa-Ala peptides and Tyr-Ala in the case of GIP or His-Ala in the case of GLP-1(7-36)amide, were identified as the main degradation products of these peptide hormones. Amides 225-230 dipeptidyl peptidase 4 Homo sapiens 100-123 8100523-9 1993 It is concluded that dipeptidyl-peptidase IV initiates the metabolism of GIP and GLP-1(7-36)amide in human serum. Amides 92-97 dipeptidyl peptidase 4 Homo sapiens 21-44 7883856-7 1995 Inhibitors of dipeptidyl peptidase-IV or low temperature (4 C) completely prevented formation of the metabolite, which was confirmed to be GLP-1-(9-36)amide by mass spectrometry and sequence analysis. Amides 151-156 dipeptidyl peptidase 4 Homo sapiens 14-37 8100523-0 1993 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. Amides 96-101 dipeptidyl peptidase 4 Homo sapiens 0-23 28194113-3 2017 Native GLP-1 (7-36) amide is rapidly degraded by diaminopeptidyl peptidase-4 (DPP4) to GLP-1 (9-36) amide, making 9-36a the major circulating form. Amides 20-25 dipeptidyl peptidase 4 Homo sapiens 78-82 31640932-3 2020 Exploring SAR by introduction of a variety of amide and halogen on benzene ring led to identification of several compounds, exerting moderated to excellent DPP-4 activities, in which 4"-chlorine substituted methyl amide 17g showed most potent DPP-4 activity with the IC50 value of 1.6 nM. Amides 46-51 dipeptidyl peptidase 4 Homo sapiens 156-161 31640932-3 2020 Exploring SAR by introduction of a variety of amide and halogen on benzene ring led to identification of several compounds, exerting moderated to excellent DPP-4 activities, in which 4"-chlorine substituted methyl amide 17g showed most potent DPP-4 activity with the IC50 value of 1.6 nM. Amides 46-51 dipeptidyl peptidase 4 Homo sapiens 243-248 31640932-3 2020 Exploring SAR by introduction of a variety of amide and halogen on benzene ring led to identification of several compounds, exerting moderated to excellent DPP-4 activities, in which 4"-chlorine substituted methyl amide 17g showed most potent DPP-4 activity with the IC50 value of 1.6 nM. Amides 207-219 dipeptidyl peptidase 4 Homo sapiens 156-161 31640932-3 2020 Exploring SAR by introduction of a variety of amide and halogen on benzene ring led to identification of several compounds, exerting moderated to excellent DPP-4 activities, in which 4"-chlorine substituted methyl amide 17g showed most potent DPP-4 activity with the IC50 value of 1.6 nM. Amides 207-219 dipeptidyl peptidase 4 Homo sapiens 243-248 28040864-2 2017 The insulinotropic activity of the native incretin hormone GLP-1(7-36)amide, which is mainly exerted through a unique G protein-coupled receptor (GLP-1R), is terminated via enzymatic cleavage by dipeptidyl peptidase-IV that generates a C-terminal GLP-1 metabolite GLP-1(9-36)amide, the major circulating form in plasma. Amides 70-75 dipeptidyl peptidase 4 Homo sapiens 195-218 28040864-2 2017 The insulinotropic activity of the native incretin hormone GLP-1(7-36)amide, which is mainly exerted through a unique G protein-coupled receptor (GLP-1R), is terminated via enzymatic cleavage by dipeptidyl peptidase-IV that generates a C-terminal GLP-1 metabolite GLP-1(9-36)amide, the major circulating form in plasma. Amides 275-280 dipeptidyl peptidase 4 Homo sapiens 195-218 28194113-3 2017 Native GLP-1 (7-36) amide is rapidly degraded by diaminopeptidyl peptidase-4 (DPP4) to GLP-1 (9-36) amide, making 9-36a the major circulating form. Amides 100-105 dipeptidyl peptidase 4 Homo sapiens 78-82 25482888-1 2015 INTRODUCTION: Dipeptidyl peptidase 4 (DPP-4) is a serine protease, which catalyzes the hydrolytic process of the amide bond X-Ala or X-Pro at the N-terminus of peptides. Amides 113-118 dipeptidyl peptidase 4 Homo sapiens 14-36 25482888-1 2015 INTRODUCTION: Dipeptidyl peptidase 4 (DPP-4) is a serine protease, which catalyzes the hydrolytic process of the amide bond X-Ala or X-Pro at the N-terminus of peptides. Amides 113-118 dipeptidyl peptidase 4 Homo sapiens 38-43 25620096-3 2015 The proof-of-concept of this prodrug technology is provided for amine-containing agents by directly linking appropriate di- (or oligo)peptide moieties to a free amino group of a non-peptidic drug through an amide bond which is specifically hydrolized by DPP IV/CD26. Amides 207-212 dipeptidyl peptidase 4 Homo sapiens 254-260 25620096-3 2015 The proof-of-concept of this prodrug technology is provided for amine-containing agents by directly linking appropriate di- (or oligo)peptide moieties to a free amino group of a non-peptidic drug through an amide bond which is specifically hydrolized by DPP IV/CD26. Amides 207-212 dipeptidyl peptidase 4 Homo sapiens 261-265 24056839-1 2013 Previous studies have revealed that the glucoincretin hormone glucagon-like peptide-1 (GLP-1)(7-36)amide is metabolized by dipeptidyl peptidase-IV (DPP-IV) and neutral endopeptidase 24.11 (NEP) to yield GLP-1(9-36)amide and GLP-1(28-36)amide, respectively, as the principal metabolites. Amides 99-104 dipeptidyl peptidase 4 Homo sapiens 123-146 24056839-1 2013 Previous studies have revealed that the glucoincretin hormone glucagon-like peptide-1 (GLP-1)(7-36)amide is metabolized by dipeptidyl peptidase-IV (DPP-IV) and neutral endopeptidase 24.11 (NEP) to yield GLP-1(9-36)amide and GLP-1(28-36)amide, respectively, as the principal metabolites. Amides 99-104 dipeptidyl peptidase 4 Homo sapiens 148-154 24056839-1 2013 Previous studies have revealed that the glucoincretin hormone glucagon-like peptide-1 (GLP-1)(7-36)amide is metabolized by dipeptidyl peptidase-IV (DPP-IV) and neutral endopeptidase 24.11 (NEP) to yield GLP-1(9-36)amide and GLP-1(28-36)amide, respectively, as the principal metabolites. Amides 214-219 dipeptidyl peptidase 4 Homo sapiens 123-146 24056839-1 2013 Previous studies have revealed that the glucoincretin hormone glucagon-like peptide-1 (GLP-1)(7-36)amide is metabolized by dipeptidyl peptidase-IV (DPP-IV) and neutral endopeptidase 24.11 (NEP) to yield GLP-1(9-36)amide and GLP-1(28-36)amide, respectively, as the principal metabolites. Amides 214-219 dipeptidyl peptidase 4 Homo sapiens 148-154 24056839-1 2013 Previous studies have revealed that the glucoincretin hormone glucagon-like peptide-1 (GLP-1)(7-36)amide is metabolized by dipeptidyl peptidase-IV (DPP-IV) and neutral endopeptidase 24.11 (NEP) to yield GLP-1(9-36)amide and GLP-1(28-36)amide, respectively, as the principal metabolites. Amides 214-219 dipeptidyl peptidase 4 Homo sapiens 123-146 24056839-1 2013 Previous studies have revealed that the glucoincretin hormone glucagon-like peptide-1 (GLP-1)(7-36)amide is metabolized by dipeptidyl peptidase-IV (DPP-IV) and neutral endopeptidase 24.11 (NEP) to yield GLP-1(9-36)amide and GLP-1(28-36)amide, respectively, as the principal metabolites. Amides 214-219 dipeptidyl peptidase 4 Homo sapiens 148-154 21361038-1 2010 To research the structure-activity relationship (SAR) of glycinamide-bearing compounds that used as inhibitors of dipeptidyl peptidase IV (DPP-IV), P32/98 and compound A were chosen as the leading compounds, heterocycles containing nitrogen atom were introduced to form amide, and different residues on a-position of carbonyl were designed. Amides 63-68 dipeptidyl peptidase 4 Homo sapiens 114-137 22307932-1 2012 We previously described a novel prodrug approach in which a di- or tetrapeptide moiety is linked to a wide variety of amine-containing drugs through an amide bond, which is specifically cleaved by dipeptidyl peptidase IV (DPPIV/CD26) activity. Amides 152-157 dipeptidyl peptidase 4 Homo sapiens 197-220 22307932-1 2012 We previously described a novel prodrug approach in which a di- or tetrapeptide moiety is linked to a wide variety of amine-containing drugs through an amide bond, which is specifically cleaved by dipeptidyl peptidase IV (DPPIV/CD26) activity. Amides 152-157 dipeptidyl peptidase 4 Homo sapiens 222-227 22307932-1 2012 We previously described a novel prodrug approach in which a di- or tetrapeptide moiety is linked to a wide variety of amine-containing drugs through an amide bond, which is specifically cleaved by dipeptidyl peptidase IV (DPPIV/CD26) activity. Amides 152-157 dipeptidyl peptidase 4 Homo sapiens 228-232 22650224-3 2012 GLP-1 is cleaved by the dipeptidyl peptidase-4 enzyme to its metabolite GLP-1 (9-36)-amide within 1-2 min of its release into the circulation. Amides 85-90 dipeptidyl peptidase 4 Homo sapiens 24-46 23094100-2 2012 GLP-1 7-36 amide, the predominant circulating active form of GLP-1, is rapidly truncated by dipeptidyl peptidase-4 to GLP-1 9-36 amide, which is generally considered inactive. Amides 11-16 dipeptidyl peptidase 4 Homo sapiens 92-114 21361038-1 2010 To research the structure-activity relationship (SAR) of glycinamide-bearing compounds that used as inhibitors of dipeptidyl peptidase IV (DPP-IV), P32/98 and compound A were chosen as the leading compounds, heterocycles containing nitrogen atom were introduced to form amide, and different residues on a-position of carbonyl were designed. Amides 63-68 dipeptidyl peptidase 4 Homo sapiens 139-145 20684603-2 2010 Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities. Amides 123-128 dipeptidyl peptidase 4 Homo sapiens 175-179 19833514-0 2009 The design of potent and selective inhibitors of DPP-4: optimization of ADME properties by amide replacements. Amides 91-96 dipeptidyl peptidase 4 Homo sapiens 49-54 20075143-2 2010 The active amide GLP-1 (7-36) is degraded by the enzyme DPP-4, and drugs that inhibit this enzyme (such as sitagliptin) have been introduced to treat type 2 diabetes. Amides 11-16 dipeptidyl peptidase 4 Homo sapiens 56-61 20018525-1 2010 GLP-1 (9-36)amide is the cleavage product of GLP-1(7-36) amide, formed by the action of diaminopeptidyl peptidase-4 (Dpp4), and is the major circulating form in plasma. Amides 12-17 dipeptidyl peptidase 4 Homo sapiens 117-121 20018525-1 2010 GLP-1 (9-36)amide is the cleavage product of GLP-1(7-36) amide, formed by the action of diaminopeptidyl peptidase-4 (Dpp4), and is the major circulating form in plasma. Amides 57-62 dipeptidyl peptidase 4 Homo sapiens 117-121 17675255-2 2007 When a variety of tetrapeptidyl amide prodrugs of NAP-TSAO were synthesized and exposed to purified dipeptidyl-peptidase IV (DPPIV/CD26) as well as human and bovine sera, they are converted to the parent NAP-TSAO drug in two successive steps by both purified CD26 and human and bovine serum. Amides 32-37 dipeptidyl peptidase 4 Homo sapiens 100-123 18600568-2 2008 The two incretins glucagon-like peptide-1 (7-36) (GLP-1(7-36)) amide and glucose-dependent insulinotropic peptide (GIP) are released from the small intestine in response to the ingestion of nutrients and regulate glucose homeostasis in a glucose-dependent fashion; however, the action of both incretins is terminated by the rapid N-terminal cleavage of two amino acid residues of GLP-1 and GIP by dipeptidyl peptidase-IV (DPP-IV). Amides 63-68 dipeptidyl peptidase 4 Homo sapiens 397-420 18600568-2 2008 The two incretins glucagon-like peptide-1 (7-36) (GLP-1(7-36)) amide and glucose-dependent insulinotropic peptide (GIP) are released from the small intestine in response to the ingestion of nutrients and regulate glucose homeostasis in a glucose-dependent fashion; however, the action of both incretins is terminated by the rapid N-terminal cleavage of two amino acid residues of GLP-1 and GIP by dipeptidyl peptidase-IV (DPP-IV). Amides 63-68 dipeptidyl peptidase 4 Homo sapiens 422-428 17904681-1 2008 Dipeptidyl peptidase (DPP-IV) rapidly metabolizes hormones such as glucagon-like peptide-1(7-36)amide. Amides 96-101 dipeptidyl peptidase 4 Homo sapiens 22-28 15908206-1 2005 anti-Substituted biaryl beta-methylphenylalanine derived amides have been shown to be potent DPP-IV inhibitors that suffer from suboptimal selectivity and pharmacokinetics. Amides 57-63 dipeptidyl peptidase 4 Homo sapiens 93-99 16332437-1 2006 anti-Substituted beta-methylphenylalanine derived amides have been shown to be potent DPP-IV inhibitors exhibiting excellent selectivity over both DPP8 and DPP9. Amides 50-56 dipeptidyl peptidase 4 Homo sapiens 86-92 16919457-1 2006 A novel series of oxadiazole based amides have been shown to be potent DPP-4 inhibitors. Amides 35-41 dipeptidyl peptidase 4 Homo sapiens 71-76 16913724-1 2006 Here we describe a novel type of enzyme-based prodrug approach in which a dipeptide moiety is linked to a nonpeptidic therapeutic drug through an amide bond which is specifically cleaved by the dipeptidyl-peptidase IV (DPP IV/CD26) enzyme activity present in plasma and on the surface of certain cells. Amides 146-151 dipeptidyl peptidase 4 Homo sapiens 194-217 16913724-1 2006 Here we describe a novel type of enzyme-based prodrug approach in which a dipeptide moiety is linked to a nonpeptidic therapeutic drug through an amide bond which is specifically cleaved by the dipeptidyl-peptidase IV (DPP IV/CD26) enzyme activity present in plasma and on the surface of certain cells. Amides 146-151 dipeptidyl peptidase 4 Homo sapiens 219-225 16913724-1 2006 Here we describe a novel type of enzyme-based prodrug approach in which a dipeptide moiety is linked to a nonpeptidic therapeutic drug through an amide bond which is specifically cleaved by the dipeptidyl-peptidase IV (DPP IV/CD26) enzyme activity present in plasma and on the surface of certain cells. Amides 146-151 dipeptidyl peptidase 4 Homo sapiens 226-230 15728907-3 2005 The results show that when the tripeptide amide came into contact with the apical enterocyte membrane, it was degraded by CD26 (dipeptidyl peptidase IV) to glycylproline and the antiretrovirally active metabolite glycinamide. Amides 42-47 dipeptidyl peptidase 4 Homo sapiens 122-126 15863311-1 2005 anti-Substituted beta-methylphenylalanine derived amides have been shown to be potent DPP-IV inhibitors exhibiting excellent selectivity over both DPP8 and DPP9. Amides 50-56 dipeptidyl peptidase 4 Homo sapiens 86-92 15728907-3 2005 The results show that when the tripeptide amide came into contact with the apical enterocyte membrane, it was degraded by CD26 (dipeptidyl peptidase IV) to glycylproline and the antiretrovirally active metabolite glycinamide. Amides 42-47 dipeptidyl peptidase 4 Homo sapiens 128-151 14664713-0 2003 Novel dipeptidyl peptidase IV resistant analogues of glucagon-like peptide-1(7-36)amide have preserved biological activities in vitro conferring improved glucose-lowering action in vivo. Amides 82-87 dipeptidyl peptidase 4 Homo sapiens 6-29 14767880-0 2004 Lys9 for Glu9 substitution in glucagon-like peptide-1(7-36)amide confers dipeptidylpeptidase IV resistance with cellular and metabolic actions similar to those of established antagonists glucagon-like peptide-1(9-36)amide and exendin (9-39). Amides 59-64 dipeptidyl peptidase 4 Homo sapiens 73-95 15655705-4 2004 DPP IV cleavage generates N-terminally truncated metabolites (GLP-1 (9-36) amide / (9-37) and GIP (3-42)), which are the major circulating forms. Amides 75-80 dipeptidyl peptidase 4 Homo sapiens 0-6 15012592-0 2004 N-terminal His(7)-modification of glucagon-like peptide-1(7-36) amide generates dipeptidyl peptidase IV-stable analogues with potent antihyperglycaemic activity. Amides 64-69 dipeptidyl peptidase 4 Homo sapiens 80-103 15012592-4 2004 Incubation of GLP-1 with either DPP IV or human plasma resulted in rapid degradation of native GLP-1 to GLP-1(9-36)amide, while N-acetyl-GLP-1 and N-pyroglutamyl-GLP-1 were completely resistant to degradation. Amides 115-120 dipeptidyl peptidase 4 Homo sapiens 32-38 12675225-0 2003 Different inhibition mechanisms of dipeptidyl peptidase IV by tryptophan containing peptides and amides. Amides 97-103 dipeptidyl peptidase 4 Homo sapiens 35-58 10512614-6 1999 Through kinetic evaluation of DPP-IV inhibition by the D-antipode, des-cyano, and amide analogues of NVP-DPP728, it was determined that the nitrile functionality at the 2-pyrrolidine position is required, in the L-configuration, for maximal activity (K(i) of 11 nM vs K(i) values of 5.6 to >300 microM for the other analogues tested). Amides 82-87 dipeptidyl peptidase 4 Homo sapiens 30-36 8798518-2 1996 The incretins glucose-dependent insulinotropic polypeptide (GIP1-42) and glucagon-like peptide-1-(7-36)-amide (GLP-17-36), hormones that potentiate glucose-induced insulin secretion from the endocrine pancreas, are substrates of the circulating exopeptidase dipeptidyl peptidase IV and are rendered biologically inactive upon cleavage of their N-terminal dipeptides. Amides 104-109 dipeptidyl peptidase 4 Homo sapiens 258-281