PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8732754-14 1996 In trypsin, the D-Phe side chain of CtA fits between Tyr 39 and Phe 41 in a favorable manner, whereas in thrombin, these residues are Glu 39 and Leu 41. Leucine 145-148 coagulation factor II, thrombin Homo sapiens 105-113 7802348-4 1994 A large amino-terminal extracellular extension has a cleavage site for thrombin (Leu Asp Pro Arg/Ser Phe Leu Leu,/representing the cleavage site). Leucine 81-84 coagulation factor II, thrombin Homo sapiens 71-79 8664285-16 1996 These findings indicate that the sulfated tyrosine/anionic GP Ibalpha residues Tyr-276-Glu-282 are important for the binding of thrombin and botrocetin-dependent binding of thrombin and the botrocetin-dependent binding of vWF, but that vWF also interacts with residues within His-1-Leu-275. Leucine 282-285 coagulation factor II, thrombin Homo sapiens 128-136 8664285-16 1996 These findings indicate that the sulfated tyrosine/anionic GP Ibalpha residues Tyr-276-Glu-282 are important for the binding of thrombin and botrocetin-dependent binding of thrombin and the botrocetin-dependent binding of vWF, but that vWF also interacts with residues within His-1-Leu-275. Leucine 282-285 coagulation factor II, thrombin Homo sapiens 173-181 8615773-2 1996 We report that these cells, when exposed to thrombin or SFLLRN (the peptide Ser-Phe-Leu-Leu-Arg-Asn, a thrombin-receptor ligand) rapidly change shape, forming membrane "blebs", detectable by differential interference contrast or confocal microscopy, as well as labelled 3-phosphorylated phosphoinositides. Leucine 84-87 coagulation factor II, thrombin Homo sapiens 44-52 8615773-2 1996 We report that these cells, when exposed to thrombin or SFLLRN (the peptide Ser-Phe-Leu-Leu-Arg-Asn, a thrombin-receptor ligand) rapidly change shape, forming membrane "blebs", detectable by differential interference contrast or confocal microscopy, as well as labelled 3-phosphorylated phosphoinositides. Leucine 84-87 coagulation factor II, thrombin Homo sapiens 103-111 8745396-5 1996 Residues Leu 415, Phe 419, and Ile 420, which would have been buried in intact EGF-like domains, are unfavorably exposed in the complex of thrombin with the EGF-like thrombomodulin fragment, thus providing a rationale for the enhancement of binding affinity upon the deletion of Ile 420. Leucine 9-12 coagulation factor II, thrombin Homo sapiens 139-147 7911722-6 1994 3 Increases in [3H]-leucine incorporation in thrombin (0.3 u ml-1)-stimulated cells were reduced by salbutamol (100 nM) by 27.7 +/- 2.8%. Leucine 20-27 coagulation factor II, thrombin Homo sapiens 45-53 7911722-8 1994 Thus, the effect of salbutamol in decreasing thrombin-induced [3H]-leucine incorporation may, at least in part, be explained by inhibition of cell proliferation. Leucine 67-74 coagulation factor II, thrombin Homo sapiens 45-53 7802348-4 1994 A large amino-terminal extracellular extension has a cleavage site for thrombin (Leu Asp Pro Arg/Ser Phe Leu Leu,/representing the cleavage site). Leucine 105-108 coagulation factor II, thrombin Homo sapiens 71-79 7802348-4 1994 A large amino-terminal extracellular extension has a cleavage site for thrombin (Leu Asp Pro Arg/Ser Phe Leu Leu,/representing the cleavage site). Leucine 105-108 coagulation factor II, thrombin Homo sapiens 71-79 8384206-8 1993 A number of soluble and full-length TM analogs with the Met388-->Leu substitution are improved thrombin cofactors, whether produced in bacteria, insect, or mammalian cells. Leucine 68-71 coagulation factor II, thrombin Homo sapiens 98-106 1434539-9 1992 alpha-Thrombin enhanced the initial rate of IL-1, TNF-alpha and f-norLeu-Leu-Phe induced PMNL transendothelial migration in an additive or supradditive manner (e.g., with IL-1 alpha+alpha-thrombin, migration was 58% greater than additive at 15 to 30 minutes, p < 0.001). Leucine 69-72 coagulation factor II, thrombin Homo sapiens 6-14 8429008-8 1993 A three-dimensional molecular model of the Quick II active site compared to alpha-thrombin suggested that the heparin cofactor II Leu-Ser-reactive site sequence (P1-P1") is a compatible "pseudosubstrate" in contrast to the Arg-Ser sequence found in antithrombin. Leucine 130-133 coagulation factor II, thrombin Homo sapiens 82-90 8381415-8 1993 In EGF5-EGF6, critical residues within a proposed acidic thrombin-binding region were: Glu-408, Tyr-413, Ile-414, Leu-415, Asp-416, Asp-417, Asp-423, Ile-424, Asp-425, and Glu-426. Leucine 114-117 coagulation factor II, thrombin Homo sapiens 57-65 8381415-9 1993 A potential Ca(2+)-binding site, which is comprised of residues Asp-423, Asp-425, Glu-426, Asn-439, Leu-440, and Phe-444, was also identified and overlaps the thrombin-binding region. Leucine 100-103 coagulation factor II, thrombin Homo sapiens 159-167 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). Leucine 197-200 coagulation factor II, thrombin Homo sapiens 68-76 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. Leucine 12-19 coagulation factor II, thrombin Homo sapiens 182-190 2742826-7 1989 Peptides with Arg(16) replaced by Gly and Leu, respectively, i.e., F14 and F15, were also found to bind to thrombin but with a different conformation, as indicated by the absence of the long-range NOEs observed with fibrinopeptide A. Residues Asp(7)-Arg(16) constitute an essential structural element in the interaction of thrombin with fibrinogen. Leucine 42-45 coagulation factor II, thrombin Homo sapiens 107-115 2928328-3 1989 (i) Two peptides that inhibit the binding of fibrinogen and other ligands to gpIIb-IIIa, Arg-Gly-Asp-Ser and His-His-Leu-Gly-Gly-Ala-Lys-Gln-Ala-Gly-Asp-Val, also inhibited the thrombin-induced tyrosine phosphorylation of this subset of proteins. Leucine 117-120 coagulation factor II, thrombin Homo sapiens 177-185 3782093-7 1986 Glu56-Asp-Asp-Asp-Tyr(SO4)-Leu-Asp62 Glu69-Asp-Asp-Asp-Tyr(SO4)-Ile-Asp75 Sulfate-labeled heparin cofactor II formed a covalent complex with thrombin in a heparin-dependent manner. Leucine 27-30 coagulation factor II, thrombin Homo sapiens 141-149 17595115-13 2007 These investigations show that Leu at P4 in PAR1 or P5 in PAR4 critically influences the kinetics of alpha-thrombin binding and cleavage of PAR1 and PAR4 exodomains. Leucine 31-34 coagulation factor II, thrombin Homo sapiens 107-115 7150549-8 1982 182, 227] has demonstrated the importance of Phe-Leu at positions P9-P8 of the A alpha chain of fibrinogen for the thrombin-fibrinogen interaction. Leucine 49-52 coagulation factor II, thrombin Homo sapiens 115-123 18585267-1 2008 By designing and coupling a functional peptide, Gly-Leu-Ala-Cys-Ser-Gly-Phe-Pro-Arg-Gly-Arg-Trp, which could be cleaved by thrombin at the site of Arg-Gly (R-G), to the surface of gold nanoparticles (Au-NPs), we propose a simple spectrofluorometry for thrombin (TRB) in this contribution. Leucine 52-55 coagulation factor II, thrombin Homo sapiens 123-131 18585267-1 2008 By designing and coupling a functional peptide, Gly-Leu-Ala-Cys-Ser-Gly-Phe-Pro-Arg-Gly-Arg-Trp, which could be cleaved by thrombin at the site of Arg-Gly (R-G), to the surface of gold nanoparticles (Au-NPs), we propose a simple spectrofluorometry for thrombin (TRB) in this contribution. Leucine 52-55 coagulation factor II, thrombin Homo sapiens 252-260 18585267-1 2008 By designing and coupling a functional peptide, Gly-Leu-Ala-Cys-Ser-Gly-Phe-Pro-Arg-Gly-Arg-Trp, which could be cleaved by thrombin at the site of Arg-Gly (R-G), to the surface of gold nanoparticles (Au-NPs), we propose a simple spectrofluorometry for thrombin (TRB) in this contribution. Leucine 52-55 coagulation factor II, thrombin Homo sapiens 262-265 26802299-1 2016 OBJECTIVE: According to recent reports, a common polymorphism resulting in Val to Leu substitution, located 3 amino acids (Val34Leu) upstream of the thrombin cleavage site of FXIII A, has been related to a lower incidence of deep vein thrombosis (DVT). Leucine 82-85 coagulation factor II, thrombin Homo sapiens 149-157 24355462-1 2014 Comb structured gold microelectrode array (CSGMA) functionalized with self-assembled monolayer of thiol terminated coiled-coil peptide (CCP) linked together by the thrombin specific cleavage site (Leu-Val-Pro-Arg-Gly-Ser) has been used to fabricate an ultrasensitive, disposable, electrochemical thrombin biosensor. Leucine 197-200 coagulation factor II, thrombin Homo sapiens 164-172 19715676-6 2009 AT with a P2-Phe inhibited thrombin with >150-fold impaired reactivity, however, the defect was restored by either pentasaccharide or by replacing Leu-99 of thrombin with a Gly. Leucine 150-153 coagulation factor II, thrombin Homo sapiens 27-35 17001711-1 2006 In the completion of our fluorine scan of tricyclic inhibitors to map the fluorophilicity/fluorophobicity of the thrombin active site, a series of 11 new ligands featuring alkyl, alkenyl, and fluoroalkyl groups was prepared to explore fluorine effects on binding into the hydrophobic proximal (P) pocket, lined by Tyr 60A and Trp 60D, His 57, and Leu 99. Leucine 347-350 coagulation factor II, thrombin Homo sapiens 113-121 14978285-6 2004 Among residues constituting the interface, Phe-34, Ser-36A, Leu-65, Tyr-76, Arg-77A, Ile-82, and Lys-110 of thrombin and the A alpha chain Trp-33, Phe-35, Asp-38, Glu-39, the B beta chain Ala-68 and Asp-69, and the gamma chain Asp-27 and Ser-30 of E(ht) form a net of polar contacts surrounding a well defined hydrophobic interior. Leucine 60-63 coagulation factor II, thrombin Homo sapiens 108-116 14977877-7 2004 Serum, thrombin, and angiotensin II likewise stimulated L-leucine transport by inducing LAT1 expression. Leucine 56-65 coagulation factor II, thrombin Homo sapiens 7-15 14556624-4 2003 Comparison of the structures shows that the fifth domain has a somewhat different structure depending on the residue at position 388, and several of the thrombin-binding residues are packed into the fifth domain in the oxidized protein while they are exposed and free to interact with thrombin in the native structure and the Met-Leu mutant. Leucine 330-333 coagulation factor II, thrombin Homo sapiens 153-161 14556624-4 2003 Comparison of the structures shows that the fifth domain has a somewhat different structure depending on the residue at position 388, and several of the thrombin-binding residues are packed into the fifth domain in the oxidized protein while they are exposed and free to interact with thrombin in the native structure and the Met-Leu mutant. Leucine 330-333 coagulation factor II, thrombin Homo sapiens 285-293 10801785-8 2000 A review of the x-ray crystal structures of known substrates and inhibitors of thrombin leads to a hypothesis that the new Leu generates a peptide with more extensive interactions with the surface of thrombin. Leucine 123-126 coagulation factor II, thrombin Homo sapiens 79-87 12588872-9 2003 Strikingly, however, although meizothrombins modified by substitution of Asp(554) with either Ala or Leu or by deletion of loop-2 had 6-8 and <1%, respectively, of the clotting activity of alpha-thrombin, the activity of these meizothrombins for protein C was increased to >10 times that of alpha-thrombin. Leucine 101-104 coagulation factor II, thrombin Homo sapiens 35-43 10801785-8 2000 A review of the x-ray crystal structures of known substrates and inhibitors of thrombin leads to a hypothesis that the new Leu generates a peptide with more extensive interactions with the surface of thrombin. Leucine 123-126 coagulation factor II, thrombin Homo sapiens 200-208 10753952-9 2000 The Arg(103) --> Leu mutant bound to Ca-SP-Toyopearl with normal affinity and inhibited alpha-thrombin in a manner similar to native rHCII. Leucine 20-23 coagulation factor II, thrombin Homo sapiens 97-105 9033392-7 1997 Thrombin K60fA activated Gla-domainless protein C (GDPC) approximately 2- and approximately 4-fold faster than thrombin in the presence and absence of thrombomodulin (TM), respectively, consistent with an improved interaction of the Leu P1" residue with the mutant S1" pocket. Leucine 233-236 coagulation factor II, thrombin Homo sapiens 0-8 10752624-2 2000 We have tested the role of Y99 by replacing it with Leu, the residue found in more proficient proteases like trypsin and thrombin. Leucine 52-55 coagulation factor II, thrombin Homo sapiens 121-129 10089309-6 1999 The Glu192 residue of thrombin adopts an extended conformation, which allows the L-cyclohexylglycyl residue in the P2 retro-binding position of the inhibitors to occupy a similar site to the P3 aspartate in thrombin platelet-receptor peptides bound to thrombin. Leucine 81-82 coagulation factor II, thrombin Homo sapiens 22-30 10089309-6 1999 The Glu192 residue of thrombin adopts an extended conformation, which allows the L-cyclohexylglycyl residue in the P2 retro-binding position of the inhibitors to occupy a similar site to the P3 aspartate in thrombin platelet-receptor peptides bound to thrombin. Leucine 81-82 coagulation factor II, thrombin Homo sapiens 207-215 10089309-6 1999 The Glu192 residue of thrombin adopts an extended conformation, which allows the L-cyclohexylglycyl residue in the P2 retro-binding position of the inhibitors to occupy a similar site to the P3 aspartate in thrombin platelet-receptor peptides bound to thrombin. Leucine 81-82 coagulation factor II, thrombin Homo sapiens 207-215 9398287-10 1997 The cluster of hydrophobic amino acids (Phe-5, Leu-6, and Val-9) on the surface of prothrombin was electronegative, suggesting a role in the electrostatic architecture of the GLA domain. Leucine 47-50 coagulation factor II, thrombin Homo sapiens 83-94 9359863-8 1997 These data indicate the existence in astrocytoma cells of a signalling pathway triggered by thrombin receptor stimulation that activates a kinase cascade acting on the Pro-Leu-Ser-Pro consensus primary sequence, activates cPLA2, and associates the release of arachidonate with nuclear signalling pathways. Leucine 172-175 coagulation factor II, thrombin Homo sapiens 92-100