Mark A. Saper

University of Michigan, Ann Arbor, Ann Arbor, MI 
"Mark Saper"
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Sathiyamoorthy K, Vijayalakshmi J, Tirupati B, et al. (2017) Structural analyses of the Haemophilus influenzae peptidoglycan synthase activator LpoA suggest multiple conformations in solution. The Journal of Biological Chemistry
Nadler C, Koby S, Peleg A, et al. (2012) Cycling of Etk and Etp phosphorylation states is involved in formation of group 4 capsule by Escherichia coli. Plos One. 7: e37984
Rojviriya C, Pratumrat T, Saper MA, et al. (2011) Improved X-ray diffraction from Bacillus megaterium penicillin G acylase crystals through long cryosoaking dehydration. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 67: 1570-4
Sathiyamoorthy K, Mills E, Franzmann TM, et al. (2011) The crystal structure of Escherichia coli group 4 capsule protein GfcC reveals a domain organization resembling that of Wza. Biochemistry. 50: 5465-76
Vijayalakshmi J, Akerley BJ, Saper MA. (2008) Structure of YraM, a protein essential for growth of Haemophilus influenzae. Proteins. 73: 204-17
Peleg A, Shifrin Y, Ilan O, et al. (2005) Identification of an Escherichia coli operon required for formation of the O-antigen capsule. Journal of Bacteriology. 187: 5259-66
Ivanov MI, Stuckey JA, Schubert HL, et al. (2005) Two substrate-targeting sites in the Yersinia protein tyrosine phosphatase co-operate to promote bacterial virulence. Molecular Microbiology. 55: 1346-56
Bjorkman PJ, Saper MA, Samraoui B, et al. (2005) Structure of the human class I histocompatibility antigen, HLA-A2. Journal of Immunology (Baltimore, Md. : 1950). 174: 6-19
Khandelwal P, Keliikuli K, Smith CL, et al. (2002) Solution structure and phosphopeptide binding to the N-terminal domain of Yersinia YopH: comparison with a crystal structure. Biochemistry. 41: 11425-37
Smith CL, Khandelwal P, Keliikuli K, et al. (2001) Structure of the type III secretion and substrate-binding domain of Yersinia YopH phosphatase. Molecular Microbiology. 42: 967-79
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