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  • Book
    [edited by] James P. Stannard, James L. Cook, Lisa A. Fortier.
    Contents:
    US definitions, current use, and FDA stance on use of platelet-rich plasma in sports medicine / Knut Beitzel, Donald Allen, John Apostolakos, Ryan P. Russell, Mary Beth McCarthy, Gregory J. Gallo, Mark P. Cote, and Augustus D. Mazzocca
    European definitions, current use, and EMA stance of platelet-rich plasma in sports medicine / Stefano Fiorentino, Alice Roffi, Giuseppe Filardo, Maurilio Marcacci, and Elizaveta Kon
    FDA regulation of adult stem cell therapies as used in sports medicine / Mary Ann Chirba, Berkley Sweetapple, Charles P. Hannon, and John A. Anderson
    Cellular chondroplasty : a new technology for joint regeneration / Mary Murphy and Frank Barry
    Autologous-conditioned serum : evidence for use in the knee / David D. Frisbie
    Role of platelet-rich plasma in articular cartilage injury and disease / Randy Mascarenhas, Bryan M. Saltzman, Lisa A. Fortier, and Brian J. Cole
    Use of platelet-rich plasma for patellar tendon and medial collateral ligament injuries : best current clinical practice / Isabel Andia and Nicola Maffulli
    Can platelet-rich plasma enhance anterior cruciate ligament and meniscal repair? / Ian D. Hutchinson, Scott A. Rodeo, Gabriel S. Perrone, Martha M. Murray
    How should we evaluate outcomes for use of biologics in the knee? / Christopher M. LaPrade, Evan W. James, Robert F. LaPrade, Lars Engebretsen
    Biologics used in bone healing / Brett D. Crist and Gregory J. Della Rocca
    Clinical decision making for use of biologics in orthopaedic practice / James L. Cook and James P. Stannard.
    Digital Access Thieme-Connect 2015
  • Book
    Mary Ellen Huls.
    Print [1985]
  • Article
    Robertson DE, Kroon PA, Ho C.
    Biochemistry. 1977 Apr 05;16(7):1443-51.
    The histidine-binding protein J of Salmonella typhimurium binds L-histidine as a first step in the high-affinity active transport of this amino acid across the cytoplasmic membrane. High-resolution nuclear magnetic resonance spectroscopy has been used to monitor the conformation of histidine-binding protein J in the presence and absence of substrate. Evidence is presented to show that this binding protein undergoes a conformational change involving a substantial number of amino-acid residues (including tryptophans) in the presence of L-histidine and that this change is specific for L-histidine. In order to monitor the involvement of tryptophan residues in the substrate-induced conformational change, 5-fluorotryptophan has been incorporated biosynthetically into the histidine-binding protein J using a tryptophan autotroph of Salmonella typhimurium. There are no significant differences in the conformation and binding activity between the 5-fluorotryptophan-labeled and the normal histidine-binding protein J. Proton and fluorine-19 nuclear magnetic resonance studies of the 5-fluorotryptophan-labeled binding protein show that at least one (and possibly two) of the tryptophan residues undergo(es) a change toward a more hydrophobic environment in the presence of L-histidine. These observations are supported by fluorescence data and by differences in the reactivity of the tryptophan residues of this protein toward N-bromosuccinimide in the presence and absence of substrate. The present results are consistent with models for the action of periplasmic-binding proteins in shock-sensitive transport systems of gram-negative bacteria which require a substrate-induced conformational change prior to the energy-dependent translocation of substrates.
    Digital Access Access Options