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Proceedings of the National Academy of Sciences of the United States of America|July 1, 1978
Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization of fibrin monomersA P Laudano, R F DoolittleBiochimica Et Biophysica Acta|December 22, 1976
Amino acid sequences of lamprey fibrinopeptides A and B and characterizations of the junctions split by lamprey and mammalian thrombinsB A Cottrell, R F DoolittleBiochemistry|April 26, 1983
Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientationP D Hoeprich, R F DoolittleJournal of Molecular Evolution|May 1, 1995
Phylogenetic analysis of the aminoacyl-tRNA synthetasesG M Nagel, R F DoolittleBiochemistry|January 1, 1985
Determination of the relative positions of amino acids by partial specific cleavages of end-labeled proteinsR A Jue, R F DoolittleJournal of Molecular Evolution|February 1, 1992
A comparison of evolutionary rates of the two major kinds of superoxide dismutaseM W Smith, R F DoolittleJournal of Molecular Evolution|January 1, 1986
A method for the simultaneous alignment of three or more amino acid sequencesM S Johnson, R F DoolittleAnnals of the New York Academy of Sciences|July 20, 2001
Crystal structure studies on fibrinogen and fibrinR F Doolittle, Z Yang, I MochalkinProceedings of the National Academy of Sciences of the United States of America|February 14, 1995
The minor form alpha' chain from lamprey fibrinogen is rapidly crosslinked during clottingE Shipwash, Y Pan, R F DoolittleProceedings of the National Academy of Sciences of the United States of America|December 20, 2000
A model of fibrin formation based on crystal structures of fibrinogen and fibrin fragments complexed with synthetic peptidesZ Yang, I Mochalkin, R F DoolittlePageof 12