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  • Book
    Timothy L. Lash, Tyler J. VanderWeele, Sebastien Haneuse, Kenneth J. Rothman.
    Summary: The thoroughly revised and updated Third Edition of Dr. Rothman's acclaimed Modern Epidemiology reflects the conceptual development of this evolving science and the engagement of epidemiologists with an increasing range of current public health concerns.
    Digital Access Ovid 2021
  • Article
    Zakin MM, Garel JR, Dautry-Varsat A, Cohen GN, Boulot G.
    Biochemistry. 1978 Oct 03;17(20):4318-23.
    The two isofunctional enzymes aspartokinases-homoserine dehydrogenases I and II from Escherichia coli K 12 are compared using immunochemical techniques. The antibodies raised against one of these two proteins when in its native state can only recognize the homologous antigen, whether it is native or denatured. Contrarily, the antibodies raised against one of these two proteins when in its denatured state can recognize both the homologous and heterologous denatured antigens. The existence of this cross-reaction only between the two denatured aspartokinases-homoserine dehydrogenases suggests that these two enzymes have some similarity since such a reaction is not detected with several other denatured proteins. The regions involved in this similarity are buried inside the native proteins, and become exposed only upon denaturation. The same results, the existence of a cross-reaction between denatured species and none between the native ones, is obtained with proteolytic fragments derived from these two proteins and endowed with homoserine dehydrogenase activity. This resemblance between the two aspartokinases-homoserine dehydrogenases suggests that these proteins derive from a common ancestor. It is also proposed that such a cross-reaction between two denatured proteins is evidence for an homology between their amino acid sequences, and that the use of denatured proteins as both immunogens and antigens could be useful in detecting sequence homologies.
    Digital Access Access Options