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  • Book
    [edited by] Michel Tibayrenc.
    Contents:
    Recent developments in the definition and official names of virus species / M.H.V. Van Regenmortel
    A theory-based pragmatism for discovering and classifying newly divergent species of bacterial pathogens / F.M. Cohan, Sarah Kopac
    Population structure of pathogenic bacteria / C.P. Andam, L. Challagundla, T. Azarian, W.P. Hanage, D.A. Robinson
    Epidemiology and evolution of fungal pathogens in plants / P. Gladieux, E.J. Byrnes III, G. Aguileta, M. Fisher, R.B. Billmyre, J. Heitman, T. Giraud
    Clonal evolution / T. de Meeûs, F. Prugnolle
    Coevolution of host and pathogen / A.D. Morgan, B. Koskella
    Microbes as tracers of past human demography and migrations / J.-P. Rasigade, A. Gilabert, T. Wirth
    Phylogenetic analysis of pathogens / D.A. Morrison
    Evolutionary responses of infectous diseases / G. Cochran, H. Harpending
    Infectous disease genomics / Y.-T. Liu
    Proteomics and host-pathogen interactions / D.G. Biron, D. Nedelkov, D. Missé, P. Holzmuller
    The evolution of antibiotic resistance / F. González-Candelas, I. Comas, J.L. Martinez, J.C. Galán, F. Baquero
    Modern morphometrics of medically important anthropods / J.-P. Dujardin
    Evolution of resistance to insecticide in disease vectors / P. Labbé, J.-P. David, H. Alout, P. Milesi, L. Djogbénou, N. Pasteur, M. Weill
    Genetics of major insect vectors / P.L. Dorn, S. Justi, E.S. Krasfur, G.C. Lanzaro, A.J. Cornel, Y. Lee, C.A. Hill
    Multilocus sequence typing of pathogens / M. Pérez-Losada, M. Arenas, E. Castro-Nallar
    Next-generation sequencing, bioinformatics, and infectous diseases / R. van Aerle, M. van der Giezen
    Genomics of infectous diseases and private industry / G. Vernet
    Current progress in the pharmacogenetics of infectous disease tehrapy / E. Elliot, T. Mahungu, A. Owen
    Genetic exchange in trypanosomatids and its relevance to epidemiology / W. Gibson, M.D. Lewis, M. Yeo, M.A. Miles
    Genomic insights into the past, current, and future evolution of human parasites of the genus plasmodium / C.J. Sutherland, S.D. Polley
    Integrated genetic epidemiology of chagas disease / M. Tibayrenc, M.A. Shaw
    Adaptive evolution of the mycobacterium tuberculosis complex to different hosts / E. Broset, J. Gonzalo-Asensio
    The evolution and dynamics of methicillin-resistant staphylococcus aureus / M.M.H. Adelbary, P. Basset, D.S. Blanc, E.J. Feil
    Origin and emergence of HIV/AIDS / M. D'arc, L. Etienne, E. Delaporte, M. Peeters
    Evolution of SARS coronavirus and the relevance of modern molecular epidemiology / Z. Shi, L.-F. Wang
    Ecology and evolution of avian influenza viruses / A.C. Hurt, R.A.M. Fouchier, D. Vijaykrishna.
    Digital Access ScienceDirect 2017
  • Book
    von Matthias Jacob Schleiden, Theodor Schwann, Max Schultze ; eingeleitet und bearbeitet von Ilse Jahn.
    Contents:
    Beiträge zur Phytogenese / Matthias Jacob Schleiden
    Mikroskopische Untersuchungen über die Übereinstimmung in der Struktur und dem Wachstum der Tiere und Pflanzen / Theodor Schwann
    Über Muskelkörperchen und das, was man eine Zelle zu nennen habe.
    Print 1987
  • Article
    Faller LD, Baroudy BM, Johnson AM, Ewall RX.
    Biochemistry. 1977 Aug 23;16(17):3864-9.
    It has generally been concluded that two divalent cations are required for enolase activity, even though the enzyme is a homodimer that specifically binds four metal ions in the presence of substrate. This paper reports a reinvestigation of the stoichiometry of enolase activation. Specific ion electrode measurements of Mg2+ binding in the presence and absence of substrate are compared with stopped-flow measurements of the velocity of 2-phosphoglycerate dehydration. It is concluded that the enzyme is inactive when only two metal-binding sites are filled and that four sites must be populated with Mg2+ for full activity. An ordered binding mechanism is proposed that quantitatively predicts the activation of enolase by the four Mg2+ ions from their measured dissociation constants and the Michaelis constant for the dehydration reaction. To explain the loss of enzymatic activity at still higher metal concentrations, the binding of additional, inhibitory Mg2+ ions is postulated.
    Digital Access Access Options