Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 101 to 103 of 103

Publication Record


Factor XI activation in a revised model of blood coagulation.
Gailani D, Broze GJ
(1991) Science 253: 909-12
MeSH Terms: Blood Coagulation, Chromogenic Compounds, Dextran Sulfate, Factor XI, Factor XIIa, Hemostasis, Kininogens, Macromolecular Substances, Models, Biological, Oligopeptides, Pyrrolidonecarboxylic Acid, Receptors, Cell Surface, Receptors, Thrombin, Recombinant Proteins, Thrombin
Show Abstract · Added May 19, 2014
Coagulation factor XI is activated in vitro by factor XIIa in the presence of high molecular weight kininogen (HMWK) and a negatively charged surface. Factor XII deficiency is not associated with bleeding, which suggests that another mechanism for factor XI activation exists in vivo. A revised model of coagulation is proposed in which factor XI is activated by thrombin. In the absence of cofactors, thrombin is more effective (kcat/Km = 1.6 x 10(5)) than factor XIIa (1.7 x 10(4)) in activating factor XI. Dextran sulfate enhances activation of factor XI by thrombin 2000-fold; part of this effect is due to autoactivation of factor XI by activated factor XI.
0 Communities
1 Members
0 Resources
15 MeSH Terms
Preparation of soluble peptide libraries: application to studies of platelet adhesion sequences.
Hortin GL, Staatz WD, Santoro SA
(1992) Biochem Int 26: 731-8
MeSH Terms: Amino Acid Sequence, Drug Evaluation, Preclinical, Humans, In Vitro Techniques, Molecular Sequence Data, Oligopeptides, Platelet Adhesiveness, Structure-Activity Relationship
Show Abstract · Added March 5, 2014
We describe chemical synthesis of peptide mixtures that equally express many sequence combinations. Using 65 couplings of single amino acids, five mixtures were prepared with the sequences Tyr-Gly-Arg-Gly-Yyy-Xxx-Xxx, where Yyy is Ser, Asp, Arg, Asn, or Glu, and Xxx is any amino acids. Compositional and sequence analyses supported full representation of all amino acids, except isoleucine was deficient in the sixth position. The data suggest formation of a repertoire of 1,900 sequence combinations (5 x 19 x 20). The mixture with Asp as the fifth residue inhibited platelet adhesion to fibronectin more effectively than the other mixtures. Peptide libraries offer a new tool for investigating bioactive peptides.
1 Communities
1 Members
0 Resources
8 MeSH Terms
Platelet activation leads to increased c-src kinase activity and association of c-src with an 85-kDa tyrosine phosphoprotein.
Wong S, Reynolds AB, Papkoff J
(1992) Oncogene 7: 2407-15
MeSH Terms: Amino Acid Sequence, Antibodies, Blood Platelets, Electrophoresis, Polyacrylamide Gel, Genes, src, Humans, Molecular Sequence Data, Molecular Weight, Oligopeptides, Phosphoproteins, Phosphotyrosine, Platelet Activation, Platelet Aggregation, Platelet Aggregation Inhibitors, Protein-Tyrosine Kinases, Proto-Oncogene Proteins pp60(c-src), Signal Transduction, Tyrosine
Show Abstract · Added March 5, 2014
We have used platelets as a model system to study the function of c-src in signal transduction and cell adhesion. Numerous proteins were found to be phosphorylated on tyrosine in response to thrombin-induced platelet activation and aggregation. Two phases of phosphorylation were observed, with the second phase, but not the first, being inhibited by blocking platelet aggregation with an Arg-Gly-Asp-Ser tetrapeptide. As a first step towards identifying those proteins phosphorylated on tyrosine and to determine the specific role of p60src during platelet activation, we looked for changes in p60src kinase activity and for associations of p60src with other tyrosine phosphoproteins. The data presented here demonstrate an increase in p60src kinase activity within 1 min of thrombin-induced activation. Furthermore, p60src transiently associates with a tyrosine phosphoprotein during platelet activation and aggregation. This tyrosine phosphoprotein, p80/85, is a previously characterized cytoskeletal substrate for v-src in transformed cells. The data presented here suggest a model in which p60src functions in platelets to link upstream events, such as cell-surface adhesive interactions, with changes in platelet shape and cytoskeletal organization.
1 Communities
1 Members
0 Resources
18 MeSH Terms