PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24793774-7 2014 DPP-IV inhibitory peptides generally had a hydrophobic or aromatic amino acid at the N-terminus, preferentially a Trp for non-competitive inhibitors and a broader range of residues for competitive inhibitors (Ile, Leu, Val, Phe, Trp or Tyr). Tyrosine 236-239 dipeptidyl peptidase 4 Homo sapiens 0-6 30862104-4 2019 In this work, initially, molecular docking simulations revealed that a natural compound, Galangin, possess a binding energy of -24 KJ/mol and interaction residues SER 630 and TYR 547, that are responsible for potent DPP-4 inhibition. Tyrosine 175-178 dipeptidyl peptidase 4 Homo sapiens 216-221 17040910-4 2006 Four conserved residues in the C-terminal loop of DPP8 (Phe(822), Val(833), Tyr(844), and His(859)), corresponding to those located at the dimer interface of DPP-IV, were individually mutated to Ala. Tyrosine 76-79 dipeptidyl peptidase 4 Homo sapiens 158-164 20942971-8 2010 Furthermore, tyrosine phosphorylation of DPPIV protein was up-regulated in Tat/DPPIV-co-expressing cells after 72 h culturing and also in DPPIV-expressing Sf9 cells after application of purified recombinant Tat protein. Tyrosine 13-21 dipeptidyl peptidase 4 Homo sapiens 41-46 20942971-8 2010 Furthermore, tyrosine phosphorylation of DPPIV protein was up-regulated in Tat/DPPIV-co-expressing cells after 72 h culturing and also in DPPIV-expressing Sf9 cells after application of purified recombinant Tat protein. Tyrosine 13-21 dipeptidyl peptidase 4 Homo sapiens 79-84 20942971-8 2010 Furthermore, tyrosine phosphorylation of DPPIV protein was up-regulated in Tat/DPPIV-co-expressing cells after 72 h culturing and also in DPPIV-expressing Sf9 cells after application of purified recombinant Tat protein. Tyrosine 13-21 dipeptidyl peptidase 4 Homo sapiens 79-84 15175333-0 2004 Tyrosine 547 constitutes an essential part of the catalytic mechanism of dipeptidyl peptidase IV. Tyrosine 0-8 dipeptidyl peptidase 4 Homo sapiens 73-96 16611738-6 2006 The increase in protein tyrosine phosphatase activity leads to a decrease in the tyrosine phosphorylation of ERK1/2 MAP kinase that in turn links to the decline in DPPIV mRNA and protein. Tyrosine 24-32 dipeptidyl peptidase 4 Homo sapiens 164-169 16756746-3 2006 After secretion, dipeptidyl peptidase IV (DPP-IV) cleaves the N-terminal Tyrosine-Proline residues from PYY(1-36), producing PYY(3-36). Tyrosine 73-81 dipeptidyl peptidase 4 Homo sapiens 17-40 16756746-3 2006 After secretion, dipeptidyl peptidase IV (DPP-IV) cleaves the N-terminal Tyrosine-Proline residues from PYY(1-36), producing PYY(3-36). Tyrosine 73-81 dipeptidyl peptidase 4 Homo sapiens 42-48 16687037-7 2006 After release, dipeptidyl peptidase IV (DPP-IV; CD 26) cleaves the N-terminal tyrosine-proline residues forming PYY(3-36). Tyrosine 78-86 dipeptidyl peptidase 4 Homo sapiens 15-38 16687037-7 2006 After release, dipeptidyl peptidase IV (DPP-IV; CD 26) cleaves the N-terminal tyrosine-proline residues forming PYY(3-36). Tyrosine 78-86 dipeptidyl peptidase 4 Homo sapiens 40-46 15175333-7 2004 The kinetic and structural findings of the tyrosine residue are discussed in relation to the catalytic mechanism of DPP-IV and to the inhibitory mechanism of the 2-cyanopyrrolidine class of potent DPP-IV inhibitors, proposing an explanation for the specificity of this class of inhibitors for the S9b family among serine proteases. Tyrosine 43-51 dipeptidyl peptidase 4 Homo sapiens 116-122 15175333-7 2004 The kinetic and structural findings of the tyrosine residue are discussed in relation to the catalytic mechanism of DPP-IV and to the inhibitory mechanism of the 2-cyanopyrrolidine class of potent DPP-IV inhibitors, proposing an explanation for the specificity of this class of inhibitors for the S9b family among serine proteases. Tyrosine 43-51 dipeptidyl peptidase 4 Homo sapiens 197-203 12800091-2 2003 However, its biological activity is severely compromised by the ubiquitous enzyme dipeptidylpeptidase IV (DPP IV), which removes the N-terminal Tyr(1)-Ala(2) dipeptide from GIP. Tyrosine 144-147 dipeptidyl peptidase 4 Homo sapiens 82-104 12800091-2 2003 However, its biological activity is severely compromised by the ubiquitous enzyme dipeptidylpeptidase IV (DPP IV), which removes the N-terminal Tyr(1)-Ala(2) dipeptide from GIP. Tyrosine 144-147 dipeptidyl peptidase 4 Homo sapiens 106-112 10570924-2 1999 This paper reports the identification and possible significance of a novel conserved sequence motif Asp-Trp-(Val/Ile/Leu)-Tyr-Glu-Glu-Glu (DW(V/I/L)YEEE) in the predicted beta propeller domain of the DPP IV-like gene family. Tyrosine 122-125 dipeptidyl peptidase 4 Homo sapiens 200-206 9758695-5 1998 We have found that DPIV-specific inhibitors (Lys[Z(NO2)]-thiazolidide and -piperidide) are capable of inducing intracellular tyrosine phosphorylation in resting human T cells. Tyrosine 125-133 dipeptidyl peptidase 4 Homo sapiens 19-23 1356916-0 1992 CD26 induces T-cell proliferation by tyrosine protein phosphorylation. Tyrosine 37-45 dipeptidyl peptidase 4 Homo sapiens 0-4 1356916-4 1992 The stimulation of nylon wool-separated T cells and T-cell clones by the anti-CD26 mAb, 134-2C2, induced tyrosine phosphorylation on a subset of proteins of 50,000, 46,000, 26,000, 24,000 and 21,000 MW. Tyrosine 105-113 dipeptidyl peptidase 4 Homo sapiens 78-82 1356916-7 1992 Thus, protein tyrosine phosphorylation seems to play a major role in CD26-mediated T-cell proliferation. Tyrosine 14-22 dipeptidyl peptidase 4 Homo sapiens 69-73 1680916-1 1991 In the present report, we demonstrated that modulation of CD26 from T cell surface induced by antiCD26 (1F7) led to enhanced phosphorylation of CD3 zeta tyrosine residues and increased CD4 associated p56lck tyrosine kinase activity. Tyrosine 153-161 dipeptidyl peptidase 4 Homo sapiens 58-62 12150711-12 2002 These data indicate that novel N-terminal Tyr(1) modification of GIP with an Fmoc or palmitate group confers resistance to degradation by DPP IV in plasma, which is reflected by increased in vitro potency and greater insulinotropic and antihyperglycaemic activities in an animal model of Type II diabetes mellitus. Tyrosine 42-45 dipeptidyl peptidase 4 Homo sapiens 138-144 11593028-6 2001 Our results therefore indicate a mechanism whereby CD26 engagement promotes aggregation of lipid rafts and facilitates colocalization of CD45 to T cell receptor signaling molecules p56(Lck), ZAP-70, and TCRzeta, thereby enhancing protein tyrosine phosphorylation of various signaling molecules and subsequent interleukin-2 production. Tyrosine 238-246 dipeptidyl peptidase 4 Homo sapiens 51-55 11555388-3 2001 CD26 costimulates both the CD3 and the CD2 dependent T-cell activation and tyrosine phosphorylation of TCR/CD3 signal transduction pathway proteins. Tyrosine 75-83 dipeptidyl peptidase 4 Homo sapiens 0-4 11287101-2 2001 In HUVECs, NPY is co-localized with dipeptidyl peptidase IV (DPPIV) which cleaves Tyr(1)-Pro(2) from NPY(1-36) to form NPY(3-36) resulting in the formation of a non-Y1 receptor agonist, which remains angiogenic. Tyrosine 82-85 dipeptidyl peptidase 4 Homo sapiens 36-59 11287101-2 2001 In HUVECs, NPY is co-localized with dipeptidyl peptidase IV (DPPIV) which cleaves Tyr(1)-Pro(2) from NPY(1-36) to form NPY(3-36) resulting in the formation of a non-Y1 receptor agonist, which remains angiogenic. Tyrosine 82-85 dipeptidyl peptidase 4 Homo sapiens 61-66 9537431-4 1998 Engagement of CD26 in PLC/PRF/5 cells through a specific antibody induces tyrosine phosphorylation of several proteins with maximal intensity 15 minutes after the stimulation. Tyrosine 74-82 dipeptidyl peptidase 4 Homo sapiens 14-18 9161885-2 1997 Triggering or costimulation of T-cells via CD26 was shown to be dependent on the expression of the T-cell receptor (TCR) associated zeta-chain with at least one functional immune receptor tyrosine based activation motif (ITAM). Tyrosine 188-196 dipeptidyl peptidase 4 Homo sapiens 43-47 9135555-0 1997 Cross-linking of CD26 by antibody induces tyrosine phosphorylation and activation of mitogen-activated protein kinase. Tyrosine 42-50 dipeptidyl peptidase 4 Homo sapiens 17-21 9135555-3 1997 In this study we demonstrate that antibody-induced cross-linking of CD26-in CD26-transfected Jurkat cells induced tyrosine phosphorylation of several intracellular proteins with a similar pattern to that seen after TCR/CD3 stimulation. Tyrosine 114-122 dipeptidyl peptidase 4 Homo sapiens 68-72 9135555-3 1997 In this study we demonstrate that antibody-induced cross-linking of CD26-in CD26-transfected Jurkat cells induced tyrosine phosphorylation of several intracellular proteins with a similar pattern to that seen after TCR/CD3 stimulation. Tyrosine 114-122 dipeptidyl peptidase 4 Homo sapiens 76-80 9135555-4 1997 Herbimycin A, an inhibitor of the src family protein tyrosine kinases dramatically inhibited this CD26-mediated effect on tyrosine phosphorylation. Tyrosine 53-61 dipeptidyl peptidase 4 Homo sapiens 98-102 9135555-6 1997 CD26-induced tyrosine phosphorylation of MAP kinase correlated with increased MAP kinase activity. Tyrosine 13-21 dipeptidyl peptidase 4 Homo sapiens 0-4 9135555-7 1997 In addition, CD26 was costimulatory to CD3 signal transduction since co-cross-linking of CD26 and CD3 antigens induced prolonged and increased tyrosine phosphorylation in comparison with CD3 activation alone. Tyrosine 143-151 dipeptidyl peptidase 4 Homo sapiens 13-17 9135555-7 1997 In addition, CD26 was costimulatory to CD3 signal transduction since co-cross-linking of CD26 and CD3 antigens induced prolonged and increased tyrosine phosphorylation in comparison with CD3 activation alone. Tyrosine 143-151 dipeptidyl peptidase 4 Homo sapiens 89-93 8097057-0 1993 The CD26 antigen is coupled to protein tyrosine phosphorylation and implicated in CD16-mediated lysis in natural killer cells. Tyrosine 39-47 dipeptidyl peptidase 4 Homo sapiens 4-8 8097057-3 1993 The protein tyrosine phosphorylation mediated by means of CD26 activation was studied in NK cells treated with the anti-CD26 MoAb 134-2C2, and two new proteins of 50 and 21 kDa appeared phosphorylated in tyrosine residues. Tyrosine 12-20 dipeptidyl peptidase 4 Homo sapiens 58-62 8097057-3 1993 The protein tyrosine phosphorylation mediated by means of CD26 activation was studied in NK cells treated with the anti-CD26 MoAb 134-2C2, and two new proteins of 50 and 21 kDa appeared phosphorylated in tyrosine residues. Tyrosine 12-20 dipeptidyl peptidase 4 Homo sapiens 120-124 8097057-3 1993 The protein tyrosine phosphorylation mediated by means of CD26 activation was studied in NK cells treated with the anti-CD26 MoAb 134-2C2, and two new proteins of 50 and 21 kDa appeared phosphorylated in tyrosine residues. Tyrosine 204-212 dipeptidyl peptidase 4 Homo sapiens 58-62 8097057-3 1993 The protein tyrosine phosphorylation mediated by means of CD26 activation was studied in NK cells treated with the anti-CD26 MoAb 134-2C2, and two new proteins of 50 and 21 kDa appeared phosphorylated in tyrosine residues. Tyrosine 204-212 dipeptidyl peptidase 4 Homo sapiens 120-124 8097057-8 1993 These results indicate that CD26 is related to the CD16-dependent lysis but not to NK cytolysis which may be caused by mediation of protein tyrosine phosphorylation. Tyrosine 140-148 dipeptidyl peptidase 4 Homo sapiens 28-32