PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23717569-2 2013 Srr1 is a serine-rich repeat glycoprotein of Streptococcus agalactiae that binds directly to the Aalpha chain of human fibrinogen. Serine 10-16 fibrinogen beta chain Homo sapiens 119-129 15601711-5 2005 The most active of all these enzyme forms against several substrates, including human fibrinogen and beta-chain insulin, was the Ser-1-Glu227 (-1S-SprE) isolated from TX5264; -1S-SprE, in contrast to other forms of SprE, was unstable at 37 degrees C, apparently due to autodegradation. Serine 129-132 fibrinogen beta chain Homo sapiens 86-96 16406498-1 2006 Fibrinogen Guarenas is a dysfibrinogenemia with a nonsense mutation at G4731T that causes an Aalpha-chain truncation at Ser 466. Serine 120-123 fibrinogen beta chain Homo sapiens 0-10 17559410-6 2007 For C. lipolytica, a approximately 60-kDa gelatin-degrading serine proteolytic activity was found in the TSB supernantant as well as a metallopeptidase activity capable of hydrolysing human albumin, IgG and human fibrinogen. Serine 60-66 fibrinogen beta chain Homo sapiens 213-223 17885889-3 2007 The depletion of SER in clotting is associated with fibrinogen, as shown by crossed-affinity immunoelectrophoresis with antisera to plasma proteins. Serine 17-20 fibrinogen beta chain Homo sapiens 52-62 17885889-4 2007 The SER-associated fibrinogen was purified and analysed by the SDS-polyacrylamide gel electrophoresis and immunoblotting. Serine 4-7 fibrinogen beta chain Homo sapiens 19-29 16607083-0 2006 Novel fibrinogen mutation (gamma 313 Ser-->Asn) associated with hypofibrinogenemia in two unrelated families. Serine 37-40 fibrinogen beta chain Homo sapiens 6-16 15632207-4 2005 DNA sequence analysis of the fibrinogen genes A, B, and G revealed a T>C transition in exon 9 resulting in a serine-to-proline substitution near the gamma chain C-terminus (S378P). Serine 112-118 fibrinogen beta chain Homo sapiens 29-39 12729597-3 2003 Both serine-3 and serine-345 (both in Aalpha) of fibrinogen were clearly recognized. Serine 5-11 fibrinogen beta chain Homo sapiens 49-59 15166913-0 2004 Biophysical characterization of fibrinogen Caracas I with an Aalpha-chain truncation at Aalpha-466 Ser: identification of the mutation and biophysical characterization of properties of clots from plasma and purified fibrinogen. Serine 99-102 fibrinogen beta chain Homo sapiens 32-42 15007078-4 2004 These differences could be ascribed to an enhanced interaction of the Ser-700 variant with fibrinogen on the platelet surface and are consistent with a prothrombotic phenotype in Ser-700 individuals. Serine 70-73 fibrinogen beta chain Homo sapiens 91-101 15007078-4 2004 These differences could be ascribed to an enhanced interaction of the Ser-700 variant with fibrinogen on the platelet surface and are consistent with a prothrombotic phenotype in Ser-700 individuals. Serine 179-182 fibrinogen beta chain Homo sapiens 91-101 12729597-3 2003 Both serine-3 and serine-345 (both in Aalpha) of fibrinogen were clearly recognized. Serine 18-24 fibrinogen beta chain Homo sapiens 49-59 10946093-2 2000 Fibrinogen Caracas V is a thrombotic dysfibrinogenemia with an Aalpha 532 Ser-->Cys mutation characterized by a tight fibrin network formed of thin fibers responsible for a less porous clot than a normal one. Serine 74-77 fibrinogen beta chain Homo sapiens 0-10 12062406-6 2002 Further experiments showed that the peptide Arg-Gly-Asp-Ser blocked both fibrinogen-induced aggregation of intact erythrocytes and specific binding of fibrinogen to the erythrocyte membranes. Serine 56-59 fibrinogen beta chain Homo sapiens 73-83 12062406-6 2002 Further experiments showed that the peptide Arg-Gly-Asp-Ser blocked both fibrinogen-induced aggregation of intact erythrocytes and specific binding of fibrinogen to the erythrocyte membranes. Serine 56-59 fibrinogen beta chain Homo sapiens 151-161 10946093-7 2000 Furthermore, this abnormal fibrinogen binds more albumin than does normal fibrinogen, a phenomenon attributed to the mutation of serine in Aalpha-532 by cysteine. Serine 129-135 fibrinogen beta chain Homo sapiens 27-37 10946093-7 2000 Furthermore, this abnormal fibrinogen binds more albumin than does normal fibrinogen, a phenomenon attributed to the mutation of serine in Aalpha-532 by cysteine. Serine 129-135 fibrinogen beta chain Homo sapiens 74-84 1328443-3 1992 Substitution of serine for cysteine was associated with a reduction in the effectiveness of interleukin-6 in both fibrinogen secretion assays. Serine 16-22 fibrinogen beta chain Homo sapiens 114-124 10572095-1 1999 A novel BbetaAsn-160 (TAA) to Ser (TGA) substitution has been identified in fibrinogen Niigata derived from a 64-year-old asymptomatic woman, who is heterozygotic for this abnormality. Serine 30-33 fibrinogen beta chain Homo sapiens 76-86 9630497-0 1998 Role of the gamma chain Ala-Gly-Asp-Val and Aalpha chain Arg-Gly-Asp-Ser sites of fibrinogen in coaggregation of platelets and fibrinogen-coated beads. Serine 69-72 fibrinogen beta chain Homo sapiens 82-92 9630497-0 1998 Role of the gamma chain Ala-Gly-Asp-Val and Aalpha chain Arg-Gly-Asp-Ser sites of fibrinogen in coaggregation of platelets and fibrinogen-coated beads. Serine 69-72 fibrinogen beta chain Homo sapiens 127-137 8883274-7 1996 The shortest thrombin clotting time and the earliest onset of turbidity increase were observed in fibrinogen gamma 358 Ser-->Cys; both parameters were little affected by calcium concentration. Serine 119-122 fibrinogen beta chain Homo sapiens 98-108 8276866-1 1994 The cysteines involved in joining the 2 half-molecules of fibrinogen and also those located on either side of the alpha-helical coiled-coil region, were substituted, by site-directed mutagenesis, with serine. Serine 201-207 fibrinogen beta chain Homo sapiens 58-68 34169424-1 2021 Recombinant batroxobin (S3101) is a thrombin-like serine protease that binds to fibrinogen or is taken up by the reticuloendothelial system. Serine 50-56 fibrinogen beta chain Homo sapiens 80-90 1920361-1 1991 The development of potent antithrombotic agents from the fibrinogen platelet receptor binding sequences Fg-alpha 572-575 -Arg-Gly-Asp-Ser- and Fg-gamma 400-411 -HHLGGAKQAGDV, believed to be a cryptic RGD-type sequence, is described. Serine 134-137 fibrinogen beta chain Homo sapiens 57-67 33815366-10 2021 Conversely, the serine protease inhibitor 4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride (AEBSF) inhibited the direct fibrinogen cleaving actions of C. mictlantecuhtli venom, thereby revealing that the pseudo-procoagulant action is driven by kallikrein-type serine proteases. Serine 16-22 fibrinogen beta chain Homo sapiens 126-136 2573600-5 1989 Calcium-dependent binding was completely inhibited by unlabeled fibrinogen, partially inhibited by a monoclonal antibody (7E3) against glycoprotein IIb-IIIa, but not inhibited by fibrinogen fragments D or E, an anti-glycoprotein IIIa polyclonal antibody, or the Arg-Gly-Asp-Ser tetrapeptide. Serine 274-277 fibrinogen beta chain Homo sapiens 64-74 2613766-10 1989 Migration over intact FGN was almost totally blocked by 230 microM-Arg-Gly-Asp-Ser (RGDS), a peptide known to interact with integrin-type receptors. Serine 79-82 fibrinogen beta chain Homo sapiens 22-25 2573600-6 1989 In contrast, the Arg-Gly-Asp-Ser tetrapeptide as well as the monoclonal antibody 7E3 markedly inhibited attachment of endothelial cells to substrate-immobilized fibrinogen, whereas fragment D or E did not. Serine 29-32 fibrinogen beta chain Homo sapiens 161-171 3101598-1 1987 Phosphorylation of human fibrinogen in vitro by incubation with [gamma-32P]ATP and protein kinase C purified from pig spleen, led to incorporation of [32P]phosphate at serine residues located in the A alpha-chain. Serine 168-174 fibrinogen beta chain Homo sapiens 25-35 2773809-8 1989 Clustering was also induced by the addition of the GPIIb-IIIa binding domains of fibrinogen--namely, the tetrapeptide Arg-Gly-Asp-Ser on the alpha-chain or the gamma-chain decapeptide gamma 402-411. Serine 130-133 fibrinogen beta chain Homo sapiens 81-91 2460346-0 1988 Anti-(Arg-Gly-Asp-Ser) antibody and its interaction with fibronectin, fibrinogen and platelets. Serine 18-21 fibrinogen beta chain Homo sapiens 70-80 3603434-1 1987 Human fibrinogen is phosphorylated in vivo to an equal extent at two positions, one at Ser 3 located on fibrinopeptide A, the other at Ser 345 of the A alpha-chain. Serine 87-90 fibrinogen beta chain Homo sapiens 6-16 3603434-1 1987 Human fibrinogen is phosphorylated in vivo to an equal extent at two positions, one at Ser 3 located on fibrinopeptide A, the other at Ser 345 of the A alpha-chain. Serine 135-138 fibrinogen beta chain Homo sapiens 6-16 3814824-1 1987 The alpha chain 572-574 Arg-Gly-Asp sequence of fibrinogen appears to play only a minor role in platelet aggregation based on the ability of fibrinogen preparations lacking alpha chain carboxyterminal segments to support platelet aggregation, but synthetic Arg-Gly-Asp-Ser (RGDS) peptides are capable of inhibiting platelet aggregation and fibrinogen binding. Serine 269-272 fibrinogen beta chain Homo sapiens 48-58 3036276-1 1987 Human fibrinogen has an Arg-Gly-Asp-Ser (RGDS) sequence at residues 572-575 of its A alpha-chain. Serine 36-39 fibrinogen beta chain Homo sapiens 6-16 3584243-10 1987 Clustering was also induced by the addition of the GPIIb-IIIa-binding domains of fibrinogen, namely the tetrapeptide Arg-Gly-Asp-Ser on the alpha-chain or the gamma-chain decapeptide gamma 402-411. Serine 129-132 fibrinogen beta chain Homo sapiens 81-91 2995350-4 1985 Moreover, the amino acid sequence Arg-Gly-Asp-Ser, corresponding to the cell attachment site of fibronectin, is located near the carboxyl-terminal region of the alpha-chain of fibrinogen. Serine 46-49 fibrinogen beta chain Homo sapiens 176-186 505412-2 1979 The fibrinogen is characterized by (1) abnormal side-to-side and end-to-end polymerization, (2) abnormal fibrinopeptide release, (3) a delayed gamma-gamma dimerization of the non cross-linked fibrin, (4) a pH optimum of 7--7.8, and (5) a deviation from normal amino acid composition with regard to lysine, aspartic acid, glutamic acid and serine. Serine 339-345 fibrinogen beta chain Homo sapiens 4-14 3876125-6 1985 Peptides containing the arg-gly-asp-ser sequence were also capable of inhibiting the adhesion of platelets to fibrinogen and von Willebrand factor substrates. Serine 36-39 fibrinogen beta chain Homo sapiens 110-120 6719396-4 1984 There is only one sequence homology between the two now known in vivo phosphorylation sites of human fibrinogen, namely that the second amino acid to the carboxyl side of the phosphorylated Ser is Glu. Serine 190-193 fibrinogen beta chain Homo sapiens 101-111 6238619-3 1984 Phosphorylation of Ser-3 of the A alpha chain appears to increase the rate of release of the corresponding phosphorylated peptide A from fibrinogen, due to enhanced binding of thrombin (lower value of the Michaelis-Menten constant KM). Serine 19-22 fibrinogen beta chain Homo sapiens 137-147 25330904-10 2014 Filamin A, an actin crosslinking phosphoprotein that is known to associate with beta3 , was dephosphorylated on Ser(2152) in fibrinogen-adhered wild-type but not in PP2B-Abeta(-/-) platelets. Serine 112-115 fibrinogen beta chain Homo sapiens 125-135 277910-8 1978 The last-named corresponds to the serine/arginine amino acid replacement previously reported for a defective human fibrinogen. Serine 34-40 fibrinogen beta chain Homo sapiens 115-125 33411219-6 2021 Thrombin is a serine protease capable of cleaving multiple substrates, including protease activated receptors (PARs), fibrinogen, and protein C. Cleavage of all three of these substrates represent pathways through which thrombin activity may exert immuno-regulatory effects and regulate permeability of the BBB during MS and EAE. Serine 14-20 fibrinogen beta chain Homo sapiens 118-128 27221710-4 2016 We found that synthetic monomeric Abeta40 bound through its RHDS (Arg-His-Asp-Ser) sequence to integrin alphaIIbbeta3, which is the receptor for the extracellular matrix protein fibrinogen, and stimulated the secretion of adenosine diphosphate (ADP) and the chaperone protein clusterin from platelets. Serine 78-81 fibrinogen beta chain Homo sapiens 178-188