PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15613026-6 2004 This novel His-->Tyr substitution was not detected when plasma fibrinogen was analyzed by electrospray ionization mass spectrometry. Histidine 11-14 fibrinogen beta chain Homo sapiens 63-73 17890955-0 2007 The role of ascorbate and histidine in fibrinogen protection against changes following exposure to a sterilizing dose of gamma-irradiation. Histidine 26-35 fibrinogen beta chain Homo sapiens 39-49 17890955-1 2007 Sodium ascorbate and histidine were employed to protect fibrinogen against modifications followed by a gamma-irradiation process that could potentially inactivate the blood-borne viruses in plasma-derived products. Histidine 21-30 fibrinogen beta chain Homo sapiens 56-66 17890955-8 2007 Contrary to ascorbate, which alone delayed the fibrinogen polymerization rate, histidine abolished irradiation-induced inhibition of fibrinogen polymerization (by 80% at 50 mmol/l; P < 0.001). Histidine 79-88 fibrinogen beta chain Homo sapiens 133-143 17890955-10 2007 On the contrary, the first definite evidence is provided that radiation-sterilized fibrinogen in the presence of histidine greatly retains its clotting capability. Histidine 113-122 fibrinogen beta chain Homo sapiens 83-93 15613026-10 2004 However, the histidine residue appears critical in maintaining structure of the fibrinogen gammaD domain, rather than in determining function. Histidine 13-22 fibrinogen beta chain Homo sapiens 80-90 15304042-8 2004 Moreover, the existence of a subsequent disulfide-linked Cys in gamma 275C fibrinogen augments the impairment caused by a His or Ala substitution. Histidine 122-125 fibrinogen beta chain Homo sapiens 75-85 12573244-0 2003 Familial hypofibrinogenaemia associated with heterozygous substitution of a conserved arginine residue; Bbeta255 Arg-->His (Fibrinogen Merivale). Histidine 119-122 fibrinogen beta chain Homo sapiens 124-134 12573244-2 2003 Family studies showed the mutations Bbeta255 Arg-->His (Fibrinogen Merivale) and Bbeta148 Lys-->Asn (Fibrinogen Merivale II) were on different alleles and that only the Bbeta255 Arg-->His mutation segregated with hypofibrinogenaemia. Histidine 51-54 fibrinogen beta chain Homo sapiens 56-66 12324470-7 2002 Among these sequences, Gln(199)-Ala(203), Leu(225)-Leu(230), and Gly(305)-His(309) are important for the binding of both ligands, whereas Arg(144)-Lys(148) is more critical for fibrinogen than for C3bi binding. Histidine 74-77 fibrinogen beta chain Homo sapiens 177-187 8747529-0 1996 Fibrinogen Claro--another dysfunctional fibrinogen variant with gamma 275 arginine-->histidine substitution. Histidine 88-97 fibrinogen beta chain Homo sapiens 0-10 9117995-0 1997 Photo-oxidation of histidine as a probe for aminoterminal conformational changes during fibrinogen-fibrin conversion. Histidine 19-28 fibrinogen beta chain Homo sapiens 88-98 9117995-1 1997 Fibrinogen is known to become unclottable when irradiated with light in the presence of methylene blue, the loss of clottability being due to photo-oxidation of the histidine at position 16 of the B beta chain. Histidine 165-174 fibrinogen beta chain Homo sapiens 0-10 8747529-0 1996 Fibrinogen Claro--another dysfunctional fibrinogen variant with gamma 275 arginine-->histidine substitution. Histidine 88-97 fibrinogen beta chain Homo sapiens 40-50 1716370-0 1991 The peptide Glu-His-Ile-Pro-Ala binds fibrinogen and inhibits platelet aggregation and adhesion to fibrinogen and vitronectin. Histidine 16-19 fibrinogen beta chain Homo sapiens 38-48 1716370-0 1991 The peptide Glu-His-Ile-Pro-Ala binds fibrinogen and inhibits platelet aggregation and adhesion to fibrinogen and vitronectin. Histidine 16-19 fibrinogen beta chain Homo sapiens 99-109 1716370-6 1991 The resulting peptide (Glu-His-Ile-Pro-Ala) has the characteristics of a fibrinogen binding site mimic: It binds fibrinogen and inhibits both the adhesion of platelets to fibrinogen and platelet aggregation. Histidine 27-30 fibrinogen beta chain Homo sapiens 73-83 1716370-6 1991 The resulting peptide (Glu-His-Ile-Pro-Ala) has the characteristics of a fibrinogen binding site mimic: It binds fibrinogen and inhibits both the adhesion of platelets to fibrinogen and platelet aggregation. Histidine 27-30 fibrinogen beta chain Homo sapiens 113-123 1716370-4 1991 Unlike peptides related to Arg-Gly-Asp-Ser and His-His-Leu-Gly-Gly-Ala-Lys-Gln-Ala-Gly-Asp-Val that bind to the fibrinogen receptor, this peptide binds to fibrinogen. Histidine 47-50 fibrinogen beta chain Homo sapiens 112-122 1716370-6 1991 The resulting peptide (Glu-His-Ile-Pro-Ala) has the characteristics of a fibrinogen binding site mimic: It binds fibrinogen and inhibits both the adhesion of platelets to fibrinogen and platelet aggregation. Histidine 27-30 fibrinogen beta chain Homo sapiens 113-123 1716370-4 1991 Unlike peptides related to Arg-Gly-Asp-Ser and His-His-Leu-Gly-Gly-Ala-Lys-Gln-Ala-Gly-Asp-Val that bind to the fibrinogen receptor, this peptide binds to fibrinogen. Histidine 47-50 fibrinogen beta chain Homo sapiens 155-165 1716370-4 1991 Unlike peptides related to Arg-Gly-Asp-Ser and His-His-Leu-Gly-Gly-Ala-Lys-Gln-Ala-Gly-Asp-Val that bind to the fibrinogen receptor, this peptide binds to fibrinogen. Histidine 51-54 fibrinogen beta chain Homo sapiens 112-122 1716370-4 1991 Unlike peptides related to Arg-Gly-Asp-Ser and His-His-Leu-Gly-Gly-Ala-Lys-Gln-Ala-Gly-Asp-Val that bind to the fibrinogen receptor, this peptide binds to fibrinogen. Histidine 51-54 fibrinogen beta chain Homo sapiens 155-165 7055572-1 1982 Fibrinogen absorbed to zinc chelate columns at pH 7.8 and was eluted sharply with a pK of 5.8 indicative of the involvement of a histidine residue. Histidine 129-138 fibrinogen beta chain Homo sapiens 0-10 1768762-1 1991 A congenital fibrinogen variant in a German family is described which has been identified as a substitution of His in position 16 of the A alpha-chain for Arg, manifested over three generations in heterozygous form. Histidine 111-114 fibrinogen beta chain Homo sapiens 13-23 3886645-8 1985 Statistical analysis of residual enzyme activity and extent of modification indicates that among 7 histidyl residues modified per molecule, there is 1 essential histidine (not in the active site) involved in the potential fibrinogen-clotting activity of prothrombin. Histidine 161-170 fibrinogen beta chain Homo sapiens 222-232 3456154-0 1986 Distinctive role of histidine-16 of the B beta chain of fibrinogen in the end-to-end association of fibrin. Histidine 20-29 fibrinogen beta chain Homo sapiens 56-66 3456154-8 1986 This shows that histidine-16 of the B beta chain of fibrinogen is essential for site A but may not be essential for site B. Histidine 16-25 fibrinogen beta chain Homo sapiens 52-62 6648427-5 1983 It is therefore concluded that fibrinogen Bern II undergoes substitution of arginine in position 16 of the A alpha-chain by histidine. Histidine 124-133 fibrinogen beta chain Homo sapiens 31-41 6849832-0 1983 Fibrinogen Manchester: identification of an abnormal fibrinopeptide A with a C-terminal arginine leads to histidine substitution. Histidine 106-115 fibrinogen beta chain Homo sapiens 0-10 7209542-1 1981 The affinity of the amino terminal tetrapeptide of the beta chain of fibrin, Gly-His-Arg-Pro, for fibrinogen dramatically increases in the presence of 2 millimolar calcium ion. Histidine 81-84 fibrinogen beta chain Homo sapiens 98-108 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. Histidine 70-73 fibrinogen beta chain Homo sapiens 178-188 620051-4 1978 It was shown that illumination of photooxidized fibrinogen and photooxidized fragment N-DSK caused the modification of histidine residues. Histidine 119-128 fibrinogen beta chain Homo sapiens 48-58 30512152-6 2018 Genetic analysis showed that g.7476 G>A heterozygous missense mutation in exon 8 of FGG gene resulted in mutations in arginine at position 275 of fibrinogen gamma D domain to histidine (Arg275His). Histidine 178-187 fibrinogen beta chain Homo sapiens 149-159