PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 429103-4 1979 It is proposed that this feature (in which Phe could be situated near Val and near the Arg-Gly bond of the A alpha chain in the three-dimensional structure of fibrinogen) may be especially advantageous for binding to the enzyme. Valine 70-73 fibrinogen beta chain Homo sapiens 159-169 3166991-3 1988 The previous suggestion that there is a hairpin loop involving residues Gly(12) to Val(15) in the A alpha chain of human fibrinogen is supported by the slow backbone NH exchange rates of Gly(14) and Val(15), by an unusually small NH chemical shift of Val(15), and by strong sequential NOE"s involving this region in F10. Valine 83-86 fibrinogen beta chain Homo sapiens 121-131 3166991-3 1988 The previous suggestion that there is a hairpin loop involving residues Gly(12) to Val(15) in the A alpha chain of human fibrinogen is supported by the slow backbone NH exchange rates of Gly(14) and Val(15), by an unusually small NH chemical shift of Val(15), and by strong sequential NOE"s involving this region in F10. Valine 199-202 fibrinogen beta chain Homo sapiens 121-131 3106345-3 1987 We found that the peptides with sequences identical with A alpha 148-161 and A alpha 149-161 of human fibrinogen accelerate the plasminogen activation by t-PA, whereas the corresponding peptides in which lysine residues A alpha 157 had been replaced by valine or arginine had no accelerating capacity. Valine 253-259 fibrinogen beta chain Homo sapiens 102-112 8113408-6 1994 By restriction fragment length polymorphism analysis, 7 affected individuals and 14 asymptomatic individuals in these two kindreds were positive for the fibrinogen A alpha chain Val 526 gene. Valine 178-181 fibrinogen beta chain Homo sapiens 153-163 15583736-2 2004 DNA sequencing revealed a single heterozygous GCC-->GTC transition in exon 8 of the fibrinogen gamma ?gene in both subjects, predicting a novel gamma289 Ala-->Val substitution. Valine 159-162 fibrinogen beta chain Homo sapiens 84-94 8883274-9 1996 In contrast, the abnormal fibrin polymerization of fibrinogen gamma 330 Asp-->Val was barely improved at increasing calcium concentrations. Valine 81-84 fibrinogen beta chain Homo sapiens 51-61 11452384-2 1971 The C-terminal ends of bovine fibrinogen and fibrin were identified as proline and valine, in the molar ratio of approximately 1:2. Valine 83-89 fibrinogen beta chain Homo sapiens 30-40 11452384-4 1971 On hydrazinolysis after selective tritium labelling of fibrinogen, radioactive C-terminal valine was also identified. Valine 90-96 fibrinogen beta chain Homo sapiens 55-65 11452384-9 1971 It should be noted that hydrophobic amino acids, like isoleucine, valine and proline, are mainly located in the C-terminal ends of all three chain peptides in the fibrinogen molecule. Valine 66-72 fibrinogen beta chain Homo sapiens 163-173 27005882-3 2016 Because Ala289 plays a crucial role in maintaining the structure of the polymerization site of hole "a" via a hydrogen bond, it is speculated that the gamma 289Ala Val substitution can change not only the fibrinogen structure, but also the function of polymerization. Valine 166-169 fibrinogen beta chain Homo sapiens 207-217 15583736-0 2004 Hypofibrinogenaemia associated with a novel heterozygous gamma289 Ala -->Val substitution (fibrinogen Dorfen). Valine 73-76 fibrinogen beta chain Homo sapiens 4-14 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. Valine 91-94 fibrinogen beta chain Homo sapiens 112-122