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Molekuliarnaia Biologiia|November 1, 1994
[How and why is pepsin stable and active at pH 2?]N S AndreevaBioorganicheskaia Khimiia|November 7, 2003
[How the features of three-dimensional structure of aspartate proteinases determine their properties]N S AndreevaMolekuliarnaia Biologiia|January 1, 1985
[The structure of pepsin. I. Molecular self-symmetry of the enzyme and implications for the evolution of aspartate proteinases]N S AndreevaScandinavian Journal of Clinical and Laboratory Investigation. Supplementum|January 1, 1992
Some aspects of structural studies on aspartic proteinasesN S AndreevaMolekuliarnaia Biologiia|October 24, 2002
[Conserved interactions of the active carboxyls in pepsin-like enzymes and retroviral proteases]N S Andreeva, M E PopovEksperimentalna Meditsina I Morfologiia|January 1, 1973
[Changes in the bioelectrical activity of the stomach and duodenum in dogs with acute phosphoorganic compound poisoning before and after treatment with preparation H-5/T]G Kotev, M Papzova, S AndreevaMolekuliarnaia Biologiia|July 4, 2006
[Interdomain interactions in aspartic proteases of higher organisms and their analogs in retroviral enzymes]N S Andreeva, G V GurskaiaMolekuliarnaia Biologiia|January 1, 1985
[The structure of pepsin. II. Structure of the enzyme active site (at 2 angstroms resolution)]A E Gushchina, N S AndreevaBiochemistry International|January 1, 1990
On the role of peripheral interactions in specificity of chymosinM G Safro, N S AndreevaZhurnal Mikrobiologii, Epidemiologii I Immunobiologii|November 11, 2005
[Role of neutrophils in the regulation of the reproductive tract microbiocenosis in women]I I Dolgushin, Iu S AndreevaPageof 8