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Protein Science : a Publication of the Protein Society|April 1, 1992
The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationshipsW Bode, D Turk, A KarshikovProtein Science : a Publication of the Protein Society|June 1, 1992
Electrostatic interactions in the association of proteins: an analysis of the thrombin-hirudin complexA Karshikov, W Bode, A Tulinsky, et al.The EMBO Journal|August 1, 1988
The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinasesW Bode, R Engh, D Musil, et al.Proteins|January 1, 1989
Electrostatic effects in a large enzyme complex: subunit interactions and electrostatic potential field of the icosahedral beta 60 capsid of heavy riboflavin synthaseA Karshikov, R LadensteinProtein Engineering|August 1, 1991
Role of electrostatic interaction in the stability of the hexamer of constitutive phycocyanin from Fremyella diplosiphonA Karshikov, M Duerring, R HuberBehring Institute Mitteilungen|April 1, 1992
Annexin V-crystal structure and its implications on functionR Huber, R Berendes, A Burger, et al.Journal of Virology|October 1, 1979
Regulation of late functions in Salmonella bacteriophages P22 and L studied by assaying endolysin synthesisW BodeStructure (London, England : 1993)|June 15, 1995
A helping hand for collagenases: the haemopexin-like domainW BodeMolekuliarnaia Biologiia|November 1, 1988
[Theoretical studies of the electrostatic interactions in aspartic proteinases, intramolecular interactions in pepsin and penicillopepsin]A Miteva, A Karshikov, B Atanasov, et al.Pageof 50