Jack Peisach

Physiology & Biophysics Albert Einstein College of Medicine, New York, New York, United States 
"Jack Peisach"
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Cheves Walling grad student 1958 Columbia
 (The dimerization of isoprene at ultra high pressures)
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Hirota S, Tanaka N, Micetic I, et al. (2010) Structural basis of the lactate-dependent allosteric regulation of oxygen binding in arthropod hemocyanin. The Journal of Biological Chemistry. 285: 19338-45
Vergara A, Franzese M, Merlino A, et al. (2009) Correlation between hemichrome stability and the root effect in tetrameric hemoglobins. Biophysical Journal. 97: 866-74
Colaneri MJ, Vitali J, Peisach J. (2009) Aspects of structure and bonding in copper-amino acid complexes revealed by single-crystal EPR/ENDOR spectroscopy and density functional calculations. The Journal of Physical Chemistry. A. 113: 5700-9
Hirota S, Kawahara T, Beltramini M, et al. (2008) Molecular basis of the Bohr effect in arthropod hemocyanin. The Journal of Biological Chemistry. 283: 31941-8
Vergara A, Franzese M, Merlino A, et al. (2007) Structural characterization of ferric hemoglobins from three antarctic fish species of the suborder notothenioidei. Biophysical Journal. 93: 2822-9
Chattopadhyay M, Walter ED, Newell DJ, et al. (2005) The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4. Journal of the American Chemical Society. 127: 12647-56
Burns CS, Aronoff-Spencer E, Legname G, et al. (2003) Copper coordination in the full-length, recombinant prion protein. Biochemistry. 42: 6794-803
Peisach J. (2003) An appreciation of William H. Orme-Johnson III. Journal of Inorganic Biochemistry. 93: 6-10
Legler PM, Lee HC, Peisach J, et al. (2002) Kinetic and magnetic resonance studies of the role of metal ions in the mechanism of Escherichia coli GDP-mannose mannosyl hydrolase, an unusual nudix enzyme. Biochemistry. 41: 4655-68
Burns CS, Aronoff-Spencer E, Dunham CM, et al. (2002) Molecular features of the copper binding sites in the octarepeat domain of the prion protein. Biochemistry. 41: 3991-4001
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