PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17384076-1 2007 Molecular dynamics simulations followed by quantum mechanical calculation and Molecular Mechanics Poisson-Boltzmann Surface Area (MM-PBSA) analysis have been carried out to study binding of proline- and pyrazinone-based macrocyclic inhibitors (L86 and T76) to human alpha-thrombin. Proline 190-197 coagulation factor II, thrombin Homo sapiens 272-280 19371038-3 2009 Proline, a common P2 in many thrombin inhibitors, was combined with known P3 residues and P1 substituents of varying size and lipophilicity. Proline 0-7 coagulation factor II, thrombin Homo sapiens 29-37 17284929-0 2007 Lys, pro and trp are critical core amino acid residues recognized by FUM20, a monoclonal antibody against serine protease pan-fungal allergens. Proline 5-8 coagulation factor II, thrombin Homo sapiens 106-121 17284929-14 2007 CONCLUSIONS: The lysine, proline and tryptophan residues located on the N-terminal region of fungal serine proteases are critical core amino acid residues recognized by FUM20, a monoclonal antibody against serine protease pan-fungal allergens. Proline 25-32 coagulation factor II, thrombin Homo sapiens 100-115 16176095-3 2005 The thrombin cleavage site Arg156 in pro-UK was mutated into His156, and named as pro-UKM1; PAI binding sites Arg178, Arg179, Arg181 were mutated into Lys178, Lys179, His181, named as pro-UKM2; The mutant containing His156, Lys178, Lys179, His181 as pro-UKM3. Proline 37-40 coagulation factor II, thrombin Homo sapiens 4-12 16176095-3 2005 The thrombin cleavage site Arg156 in pro-UK was mutated into His156, and named as pro-UKM1; PAI binding sites Arg178, Arg179, Arg181 were mutated into Lys178, Lys179, His181, named as pro-UKM2; The mutant containing His156, Lys178, Lys179, His181 as pro-UKM3. Proline 82-85 coagulation factor II, thrombin Homo sapiens 4-12 14750503-5 2003 The inhibitory activity against thrombin or botrocetin is mainly linked to Arg-Arg-Pro-Phe or Trp-Ile-Arg-Arg-Pro, respectively, among nine amino acids. Proline 83-86 coagulation factor II, thrombin Homo sapiens 32-40 15826939-3 2005 When compared with Pro(33)-negative platelets, Pro(33)-positive platelets demonstrated significantly greater serine/threonine phosphorylation of extracellular signal-regulated kinase (ERK2) and myosin light chain (MLC) but not cytoplasmic phospholipase A2 upon thrombin-induced aggregation. Proline 47-50 coagulation factor II, thrombin Homo sapiens 261-269 13678420-0 2003 Protease-activated receptor-4 uses dual prolines and an anionic retention motif for thrombin recognition and cleavage. Proline 40-48 coagulation factor II, thrombin Homo sapiens 84-92 13678420-9 2003 Thus, to compensate for the lack of exosite I binding, PAR4 utilizes proline residues in its P(4)-P(1) sequence to provide high-affinity interactions with the active site and an anionic cluster to slow dissociation from the cationic thrombin. Proline 69-76 coagulation factor II, thrombin Homo sapiens 233-241 12873514-1 2003 A series of potent and selective proline- and pyrazinone-based macrocyclic thrombin inhibitors is described. Proline 33-40 coagulation factor II, thrombin Homo sapiens 75-83 14654359-6 2003 Unlike wild-type hirudin, the variant comprising Pro(50)- ...-His(56)-Asp(57)- ...-Pro(62)-Pro(63)-His(64) is completely resistant to pepsin and chymotrypsin cleavage; however, this is at the expense of thrombin inhibition activity where there is a 100-fold increase in the IC50 value. Proline 49-52 coagulation factor II, thrombin Homo sapiens 203-211 14654359-6 2003 Unlike wild-type hirudin, the variant comprising Pro(50)- ...-His(56)-Asp(57)- ...-Pro(62)-Pro(63)-His(64) is completely resistant to pepsin and chymotrypsin cleavage; however, this is at the expense of thrombin inhibition activity where there is a 100-fold increase in the IC50 value. Proline 83-86 coagulation factor II, thrombin Homo sapiens 203-211 14654359-6 2003 Unlike wild-type hirudin, the variant comprising Pro(50)- ...-His(56)-Asp(57)- ...-Pro(62)-Pro(63)-His(64) is completely resistant to pepsin and chymotrypsin cleavage; however, this is at the expense of thrombin inhibition activity where there is a 100-fold increase in the IC50 value. Proline 83-86 coagulation factor II, thrombin Homo sapiens 203-211 9850596-5 1998 Thrombin (5-20 U/ml) also stimulated the protein synthesis rate (assayed by [3H]proline incorporation) to 1.88-2.13 fold that of the control. Proline 80-87 coagulation factor II, thrombin Homo sapiens 0-8 12646027-2 2003 The thrombin inhibitory tripeptide d-Phe-Pro-Arg has been mimicked using either cyclopentenedicarboxylic derivatives or a cyclohexenedicarboxylic derivative as surrogate for the P2 proline. Proline 181-188 coagulation factor II, thrombin Homo sapiens 4-12 10836047-0 1999 7-Azabicycloheptane carboxylic acid: a proline replacement in a boroarginine thrombin inhibitor. Proline 39-46 coagulation factor II, thrombin Homo sapiens 77-85 10836047-1 1999 [formula: see text] The synthesis of thrombin inhibitor 3, which incorporates conformationally constrained 7-azabicycloheptane carboxylic acid (1) as a proline replacement, is described. Proline 152-159 coagulation factor II, thrombin Homo sapiens 37-45 10836047-2 1999 The inhibition constant (Ki(thrombin) = 2.9 nM) indicates that 1 is a reasonable replacement of proline in the formation of a beta-turn tripeptide mimetic. Proline 96-103 coagulation factor II, thrombin Homo sapiens 28-36 10051558-6 1999 The activity profiles obtained for thrombin also suggest that the conversion of Pro to Tyr or Phe documented in the vertebrates occurred through Ser and was driven by a significant gain (up to 50-fold) in catalytic activity. Proline 80-83 coagulation factor II, thrombin Homo sapiens 35-43 9790668-6 1998 The IgG affects the rate at which thrombin cleaves various peptide p-nitroanilide substrates with arginine in the P1 position, increasing the kcat for substrates with a P2 glycine residue but generally decreasing the kcat for substrates with a P2 proline. Proline 247-254 coagulation factor II, thrombin Homo sapiens 34-42 9790668-7 1998 The allosteric effect of the IgG is altered by deletion of Pro-60b, Pro-60c, and Trp-60d from the 60-loop of thrombin, which lies between exosite II and the catalytic triad. Proline 59-62 coagulation factor II, thrombin Homo sapiens 109-117 9790668-7 1998 The allosteric effect of the IgG is altered by deletion of Pro-60b, Pro-60c, and Trp-60d from the 60-loop of thrombin, which lies between exosite II and the catalytic triad. Proline 68-71 coagulation factor II, thrombin Homo sapiens 109-117 10794688-0 2000 New proline mimetics: synthesis of thrombin inhibitors incorporating cyclopentane- and cyclopentenedicarboxylic acid templates in the P2 position. Proline 4-11 coagulation factor II, thrombin Homo sapiens 35-43 9364988-10 1997 These results indicate that the size of the thrombin hydrophobic pocket S2 is sufficient to accept larger residues than proline in the P2 position of Ac-D-Phe-X-boroArg derivatives while this is not the case for other important serine-proteases of the fibrinolysis, coagulation and complement pathways. Proline 120-127 coagulation factor II, thrombin Homo sapiens 44-52 9716158-11 1998 Nevertheless, the lack of effect of R2 on thrombin-induced platelet activation suggests that proline 280 is important for thrombin interaction with GPIb. Proline 93-100 coagulation factor II, thrombin Homo sapiens 122-130 8910365-9 1996 Furthermore, in the presence of inhibitors of p38 kinase, the proline-directed phosphorylation of cPLA2 was completely blocked in platelets stimulated with the thrombin receptor agonist peptide SFLLRN and was suppressed during the early (up to 2 min) phase of platelet stimulation caused by thrombin. Proline 62-69 coagulation factor II, thrombin Homo sapiens 160-168 8910365-9 1996 Furthermore, in the presence of inhibitors of p38 kinase, the proline-directed phosphorylation of cPLA2 was completely blocked in platelets stimulated with the thrombin receptor agonist peptide SFLLRN and was suppressed during the early (up to 2 min) phase of platelet stimulation caused by thrombin. Proline 62-69 coagulation factor II, thrombin Homo sapiens 291-299 8784202-4 1996 A 1000-fold difference in Kon values was observed between the fastest (P2 proline) and the slowest (P2 threonine) inhibitors of thrombin. Proline 74-81 coagulation factor II, thrombin Homo sapiens 128-136 7537275-8 1995 This association with F-actin appeared to be at least partly indirect, since we demonstrated a thrombin-dependent interaction of p85 alpha with a proline-rich sequence of the tyrosine-phosphorylated cytoskeletal focal adhesion kinase, p125FAK. Proline 146-153 coagulation factor II, thrombin Homo sapiens 95-103 7548057-6 1995 The best inhibitors of thrombin contained Pro or Gly at the P2 position in place of Phe353, with 2- and 7-fold increases in activity, respectively. Proline 42-45 coagulation factor II, thrombin Homo sapiens 23-31 8944419-2 1996 Substitution of proline by m-Abz-residue may result in the development of novel substrates and inhibitors for thrombin. Proline 16-23 coagulation factor II, thrombin Homo sapiens 110-118 7499191-1 1995 In human platelets a proline-directed kinase distinct from the ERK MAP kinases is stimulated by both thrombin and the thrombin receptor agonist peptide SFLLRN and may be involved in the activation of Ca(2+)-dependent cytosolic phospholipase A2 (Kramer, R. M., Roberts, E. F., Hyslop, P. A., Utterback, B. G., Hui, K. Y., and Jakubowski, J.A. Proline 21-28 coagulation factor II, thrombin Homo sapiens 101-109 7499191-1 1995 In human platelets a proline-directed kinase distinct from the ERK MAP kinases is stimulated by both thrombin and the thrombin receptor agonist peptide SFLLRN and may be involved in the activation of Ca(2+)-dependent cytosolic phospholipase A2 (Kramer, R. M., Roberts, E. F., Hyslop, P. A., Utterback, B. G., Hui, K. Y., and Jakubowski, J.A. Proline 21-28 coagulation factor II, thrombin Homo sapiens 118-126 7563081-2 1995 Analogs of FpA and FpA Rouen have been designed that include a Pro15 to replace Val15 in natural FpA and to mimic the frequent occurrences of a proline residue at equivalent positions of other protein substrates of thrombin. Proline 144-151 coagulation factor II, thrombin Homo sapiens 215-223 7744836-6 1995 For example, replacement of the P2 proline of Arg-alpha 1-antitrypsin by glycine decreased the association rate constant (kass) with thrombin by 37-fold while the kass value with APC was reduced by only 16-fold. Proline 35-42 coagulation factor II, thrombin Homo sapiens 133-141 7744836-11 1995 Substitution of proline for the P2 glycine of this chimeric serpin increased the kass values with thrombin and APC by 7- and 90-fold, respectively. Proline 16-23 coagulation factor II, thrombin Homo sapiens 98-106 1290488-1 1992 Hirulog-1 [D-Phe-Pro-Arg-Pro-[Gly]4-desulphohirudin-(53-64) (HV1)] was designed to bind by its first four and last 12 residues to the alpha-thrombin catalytic site and anion-binding exosite for fibrin(ogen) recognition respectively, with a [Gly]4 bridge and an Arg-Pro bond at the scissional position. Proline 17-20 coagulation factor II, thrombin Homo sapiens 140-148 1304349-4 1992 The crystallographic refinement of the PPACK-thrombin model has now been completed at an R value of 0.156 (8 to 1.92 A); in particular, the amino- and the carboxy-termini of the thrombin A-chain are now defined and all side-chain atoms localized; only proline 37 was found to be in a cis-peptidyl conformation. Proline 252-259 coagulation factor II, thrombin Homo sapiens 178-186 35053615-7 2022 CD26/dipeptidyl peptidase 4 (DPP4) functions as a serine protease, selectively cleaving polypeptides with a proline or alanine at the penultimate N-terminal position, such as chemokines. Proline 108-115 coagulation factor II, thrombin Homo sapiens 50-65 1547237-6 1992 The global folding of these conformations is similar to that in the thrombin-bound state, as indicated by NOE"s involving the side-chain protons of residues Phe(56), Ile(59), Pro(60), Tyr(63), and Leu(64). Proline 175-178 coagulation factor II, thrombin Homo sapiens 68-76 6860783-1 1983 It is shown that thrombin (0.1-7 units/ml) stimulates calcium mobilization and bone matrix degradation, as indicated by release of [3H]proline, from cultured calvarial bones. Proline 135-142 coagulation factor II, thrombin Homo sapiens 17-25 3755044-4 1986 Proline and leucine were identified in the P2 and P1 positions of the protease cleavage site, providing a possible explanation for the ability of heparin cofactor II to inhibit both thrombin and chymotrypsin-like proteases. Proline 0-7 coagulation factor II, thrombin Homo sapiens 182-190 2974999-5 1988 The substitution of the pyrrolidine residue by L-proline in this type of inhibitors decreased the activity against serine proteases, especially against thrombin. Proline 47-56 coagulation factor II, thrombin Homo sapiens 152-160 30468644-3 2019 The FAP serine protease has the rare property of both dipeptidyl peptidase and endopeptidase activities capable of cleaving the post-proline bond at two or more residues from the N-terminus. Proline 133-140 coagulation factor II, thrombin Homo sapiens 8-23 6776531-7 1980 The NH2-terminal sequence of CNBr II revealed the active site serine of factor D. The typical serine protease active site sequence (Gly-Asp-Ser-Gly-Gly-Pro was found at residues 12-17. Proline 152-155 coagulation factor II, thrombin Homo sapiens 94-109 30419598-3 2018 However, the role of proline 36, which is adjacent to the thrombin cleavage site at Arg37, has not yet been studied in detail. Proline 21-28 coagulation factor II, thrombin Homo sapiens 58-66 24470260-2 2014 This atypical serine protease has both dipeptidyl peptidase and endopeptidase activities, cleaving substrates at a post-proline bond. Proline 120-127 coagulation factor II, thrombin Homo sapiens 14-29 25140306-1 2014 A cell surface serine protease, dipeptidyl peptidase 4 (DPP-4), cleaves dipeptide from peptides containing proline or alanine in the N-terminal penultimate position. Proline 107-114 coagulation factor II, thrombin Homo sapiens 15-30 24412428-1 2014 Here, an ultrasensitive electrochemiluminescence (ECL) aptasensor using in situ generated proline and polyamidoamine (PAMAM) dendrimers as coreactant for bis(2,2"-bipyridyl)(5-amino-1,10-phenanthroline) ruthenium(II) (Ru) was successfully constructed for detection of thrombin (TB). Proline 90-97 coagulation factor II, thrombin Homo sapiens 268-276