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Structure of the Glycyl-L-histidyl-L-lysine--copper(II) complex in solution.
Freedman JH, Pickart L, Weinstein B, Mims WB, Peisach J. Freedman JH, et al. Among authors: peisach j. Biochemistry. 1982 Sep 14;21(19):4540-4. doi: 10.1021/bi00262a004. Biochemistry. 1982. PMID: 6291585
H., Loker, W. J., Peisach, J., Perkins, C. M., Steinkamp, R. E., & Weinstein, B. (1980) Nature (London) 288, 715-717; C. M. Perkins, N. ...
H., Loker, W. J., Peisach, J., Perkins, C. M., Steinkamp, R. E., & Weinstein, B. (1980) Nature (London) 288, 715-717; C. M …
Structural basis of the lactate-dependent allosteric regulation of oxygen binding in arthropod hemocyanin.
Hirota S, Tanaka N, Micetic I, Di Muro P, Nagao S, Kitagishi H, Kano K, Magliozzo RS, Peisach J, Beltramini M, Bubacco L. Hirota S, et al. Among authors: peisach j. J Biol Chem. 2010 Jun 18;285(25):19338-45. doi: 10.1074/jbc.M109.076067. Epub 2010 Apr 20. J Biol Chem. 2010. PMID: 20406810 Free PMC article.
In contrast to this, the active site structure of deoxy-Hc is affected by changes in pH (Hirota, S., Kawahara, T., Beltramini, M., Di Muro, P., Magliozzo, R. S., Peisach, J., Powers, L. S., Tanaka, N., Nagao, S., and Bubacco, L. (2008) J. ...
In contrast to this, the active site structure of deoxy-Hc is affected by changes in pH (Hirota, S., Kawahara, T., Beltramini, M., Di …
Intracellular copper transport in cultured hepatoma cells.
Freedman JH, Peisach J. Freedman JH, et al. Among authors: peisach j. Biochem Biophys Res Commun. 1989 Oct 16;164(1):134-40. doi: 10.1016/0006-291x(89)91693-8. Biochem Biophys Res Commun. 1989. PMID: 2553012
These results suggest that the chelation of copper by metallothionein from a copper-glutathione complex (Freedman, J. H., Ciriolo, M. R., and Peisach, J. (1989) J. Biol. Chem. 264, 5598-5605) is a reversible process. ...
These results suggest that the chelation of copper by metallothionein from a copper-glutathione complex (Freedman, J. H., Ciriolo, M. …
Restraint validation of biomolecular structures determined by NMR in the Protein Data Bank.
Baskaran K, Ploskon E, Tejero R, Yokochi M, Harrus D, Liang Y, Peisach E, Persikova I, Ramelot TA, Sekharan M, Tolchard J, Westbrook JD, Bardiaux B, Schwieters CD, Patwardhan A, Velankar S, Burley SK, Kurisu G, Hoch JC, Montelione GT, Vuister GW, Young JY. Baskaran K, et al. Among authors: peisach e. Structure. 2024 Jun 6;32(6):824-837.e1. doi: 10.1016/j.str.2024.02.011. Epub 2024 Mar 14. Structure. 2024. PMID: 38490206 Free article.
Restraint Validation of Biomolecular Structures Determined by NMR in the Protein Data Bank.
Baskaran K, Ploskon E, Tejero R, Yokochi M, Harrus D, Liang Y, Peisach E, Persikova I, Ramelot TA, Sekharan M, Tolchard J, Westbrook JD, Bardiaux B, Schwieters CD, Patwardhan A, Velankar S, Burley SK, Kurisu G, Hoch JC, Montelione GT, Vuister GW, Young JY. Baskaran K, et al. Among authors: peisach e. bioRxiv [Preprint]. 2024 Jan 22:2024.01.15.575520. doi: 10.1101/2024.01.15.575520. bioRxiv. 2024. Update in: Structure. 2024 Jun 6;32(6):824-837.e1. doi: 10.1016/j.str.2024.02.011. PMID: 38328042 Free PMC article. Updated. Preprint.
Epinephrine as an inotropic agent in septic shock: a dose-profile analysis.
Moran JL, O'Fathartaigh MS, Peisach AR, Chapman MJ, Leppard P. Moran JL, et al. Among authors: peisach ar. Crit Care Med. 1993 Jan;21(1):70-7. doi: 10.1097/00003246-199301000-00015. Crit Care Med. 1993. PMID: 8420733
MEASUREMENTS AND MAIN RESULTS: After volume loading, mean hemodynamic indices were as follows: mean arterial pressure (MAP) 62 +/- 7 mm Hg; cardiac index 3.8 +/- 1.1 L/min/m2; left ventricular stroke work index 25 +/- 11 g.m/m2; oxygen delivery (Do2) index 460 +/- 168 mL/m …
MEASUREMENTS AND MAIN RESULTS: After volume loading, mean hemodynamic indices were as follows: mean arterial pressure (MAP) 62 +/- 7 mm Hg; …
Oxygenated iron bleomycin. A short-lived intermediate in the reaction of ferrous bleomycin with O2.
Burger RM, Horwitz SB, Peisach J, Wittenberg JB. Burger RM, et al. Among authors: peisach j. J Biol Chem. 1979 Dec 25;254(24):12999-302. J Biol Chem. 1979. PMID: 91616 Free article.
The first event is first order with respect to both bleomycin and O2 and may be regarded as a second order reaction (k = 6.1 x 10(3) M-1s-1 at 2 degrees C). The first product has no EPR spectrum. The optical spectrum resembles those of Fe(II) . bleomycin complexes with CO, …
The first event is first order with respect to both bleomycin and O2 and may be regarded as a second order reaction (k = 6.1 x 10(3) M …
Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination.
Sugio S, Kashima A, Kishimoto K, Peisach D, Petsko GA, Ringe D, Yoshimura T, Esaki N. Sugio S, et al. Among authors: peisach d. Protein Eng. 1998 Aug;11(8):613-9. doi: 10.1093/protein/11.8.613. Protein Eng. 1998. PMID: 9749913
The leucine-to-alanine mutation at residue 201 of D-amino acid aminotransferase provides a unique enzyme which gradually loses its activity while catalyzing the normal transamination; the co-enzyme form is converted from pyridoxal 5'-phosphate to pyridoxamine 5'-phosphate upon th …
The leucine-to-alanine mutation at residue 201 of D-amino acid aminotransferase provides a unique enzyme which gradually loses its activity …
Determination of copper in biological materials by atomic absorption spectroscopy: a reevaluation of the extinction coefficients for azurin and stellacyanin.
Freedman JH, Peisach J. Freedman JH, et al. Among authors: peisach j. Anal Biochem. 1984 Sep;141(2):301-10. doi: 10.1016/0003-2697(84)90046-0. Anal Biochem. 1984. PMID: 6496940
The values obtained, 4.33 X 10(3) and 3.75 X 10(3) M-1 cm-1, respectively, are considerably different from those determined by the method of standard additions on nitric acid digests of these proteins, but were close to values previously reported and determined colorimetri …
The values obtained, 4.33 X 10(3) and 3.75 X 10(3) M-1 cm-1, respectively, are considerably different from those determined by the me …
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.
Legler PM, Lee HC, Peisach J, Mildvan AS. Legler PM, et al. Among authors: peisach j. Biochemistry. 2002 Apr 9;41(14):4655-68. doi: 10.1021/bi012118d. Biochemistry. 2002. PMID: 11926828
Escherichia coli GDP-mannose mannosyl hydrolase (GDPMH), a homodimer, catalyzes the hydrolysis of GDP-alpha-D-sugars to yield the beta-D-sugar and GDP by nucleophilic substitution with inversion at the C1' carbon of the sugar [Legler, P. M., Massiah, M. A., Bessman, …
Escherichia coli GDP-mannose mannosyl hydrolase (GDPMH), a homodimer, catalyzes the hydrolysis of GDP-alpha-D-sugars to yield the beta-D-sug …
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