Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: Implications for bacterial agglutination(414 views visite) Esposito C, Carullo C, Pedone E, Graziano G, Del Vecchio P, Berisio R
Febs Lett (ISSN: 0014-5793, 0014-5793print, 0014-5793linking), 2010 Mar 19; 584(6): 1091-1096.
Keywords Parole chiave: Agglutination, Coiled Coil, Dimerisation, Stability, Tuberculosis, Heparin Binding Hemagglutinin Adhesin, Monomer, Protein, Unclassified Drug, Virulence Factor, Article, Cell Interaction, Controlled Study, Dimerization, Epithelium Cell, Experiment, Molecular Model, Molecular Stability, Mycobacterium Tuberculosis, Primary Infection, Priority Journal, Protein Conformation, Protein Denaturation, Protein Structure, Amino Acid Sequence, Antigens, Bacterial Adhesion, Lectins, Light, Molecular Sequence Data, Protein Folding, Protein Multimerization, Protein Stability, Scattering, Radiation, Temperature, Bacteria (microorganisms),
Affiliations Affiliazioni: *** IBB - CNR ***
Istitute of Biostructures and Bioimaging, C.N.R., I-80134 - Naples, Italy Department of Chemistry Paolo Corradini, University of Naples Federico II, Complesso Universitario Monte S. Angelo, I-80126, Naples, Italy Department of Biological and Environmental Sciences, University of Sannio, I-82100 Benevento, Italy
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