Publications

DNA replication: enzymology and mechanisms.
Kelman Z, O'Donnell M. 1994. DNA replication: enzymology and mechanisms. Current opinion in genetics & development 4(2): 185-95.
Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein.
Liao DI, Kapadia G, Ahmed H, Vasta GR, Herzberg O. 1994. Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein. Proceedings of the National Academy of Sciences of the United States of America 91(4): 1428-32.
Tyrosinase reaction and subsequent chitosan adsorption for selective removal of a contaminant from a fermentation recycle stream.
Payne GF, Sun WQ. 1994. Tyrosinase reaction and subsequent chitosan adsorption for selective removal of a contaminant from a fermentation recycle stream. Applied and environmental microbiology 60(2): 397-401.
Structure of a phosphonate-inhibited beta-lactamase. An analog of the tetrahedral transition state/intermediate of beta-lactam hydrolysis.
Chen CC, Rahil J, Pratt RF, Herzberg O. 1993. Structure of a phosphonate-inhibited beta-lactamase. An analog of the tetrahedral transition state/intermediate of beta-lactam hydrolysis. Journal of molecular biology 234(1): 165-78.
The murine vik gene (chromosome 9) encodes a putative receptor with unique protein kinase motifs.
Kelman Z, Simon-Chazottes D, Guénet JL, Yarden Y. 1993. The murine vik gene (chromosome 9) encodes a putative receptor with unique protein kinase motifs. Oncogene 8(1): 37-44.
An atomic model for protein-protein phosphoryl group transfer.
Herzberg O. 1992. An atomic model for protein-protein phosphoryl group transfer. The Journal of biological chemistry 267(34): 24819-23.
Tyrosinase reaction/chitosan adsorption for selectively removing phenols from aqueous mixtures.
Payne GF, Sun WQ, Sohrabi A. 1992. Tyrosinase reaction/chitosan adsorption for selectively removing phenols from aqueous mixtures. Biotechnology and bioengineering 40(9): 1011-8.
Signal transduction by the neu/erbB-2 receptor: a potential target for anti-tumor therapy.
Stancovski I, Peles E, Ben Levy R, Lemprecht R, Kelman Z, Goldman-Michael R, Hurwitz E, Bacus S, Sela M, Yarden Y. 1992. Signal transduction by the neu/erbB-2 receptor: a potential target for anti-tumor therapy. The Journal of steroid biochemistry and molecular biology 43(1-3): 95-103.
Bioprocess development to improve foreign protein production from recombinant Streptomyces.
DelaCruz N, Payne GF, Smith JM, Coppella SJ. 2022. Bioprocess development to improve foreign protein production from recombinant Streptomyces. Biotechnology progress 8(4): 307-15.
Inhibition of beta-lactamase by clavulanate. Trapped intermediates in cryocrystallographic studies.
Chen CC, Herzberg O. 1992. Inhibition of beta-lactamase by clavulanate. Trapped intermediates in cryocrystallographic studies. Journal of molecular biology 224(4): 1103-13.
Enzyme-based strategy for toxic waste treatment and waste minimization.
Smith JM, Payne GF, Lumpkin JA, Karns JS. 1992. Enzyme-based strategy for toxic waste treatment and waste minimization. Biotechnology and bioengineering 39(7): 741-52.
Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution.
Herzberg O, Reddy P, Sutrina S, Saier MH, Reizer J, Kapadia G. 1992. Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution. Proceedings of the National Academy of Sciences of the United States of America 89(6): 2499-503.
Crystallization of the IIA domain of the glucose permease of Bacillus subtilis.
Kapadia G, Chen CC, Reddy P, Saier MH, Reizer J, Herzberg O. 1991. Crystallization of the IIA domain of the glucose permease of Bacillus subtilis. Journal of molecular biology 221(4): 1079-80.
Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2-A resolution.
Liao DI, Kapadia G, Reddy P, Saier MH, Reizer J, Herzberg O. 1991. Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2-A resolution. Biochemistry 30(40): 9583-94.
Structural basis for the inactivation of the P54 mutant of beta-lactamase from Staphylococcus aureus PC1.
Herzberg O, Kapadia G, Blanco B, Smith TS, Coulson A. 1991. Structural basis for the inactivation of the P54 mutant of beta-lactamase from Staphylococcus aureus PC1. Biochemistry 30(39): 9503-9.