S. Bernhard

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Automatic Determination of Amino Acid Sequences

Dan F. Bradley, Sidney A. Bernhard, William L. Duda, 1963, IBM J. Res. Dev..

Specific Effects in Acid Catalysis by Ion Exchange Resins. III. Some Observations on the Effect of Polyvalent Cations1

E. Garfield, S. Bernhard, L. Hammett, 1954 .

Catalytic steps during the single-turnover reduction of aldehydes by alcohol dehydrogenase.

S. Bernhard, J. McFarland, 1972, Biochemistry.

Noncovalent modulation by ATP of the acyl transfer from acyl-glyceraldehyde-3-phosphate dehydrogenase to phosphate.

S. Bernhard, O. Malhotra, 1989, Biochemistry.

Role of nicotinamide adenine dinucleotide as an effector in formation and reactions of acylglyceraldehyde-3-phosphate dehydrogenase.

S. Bernhard, O. Malhotra, 1981, Biochemistry.

Structural and functional consequences of subunit interactions in glyceraldehyde 3-phosphate dehydrogenase.

S. Bernhard, F. Seydoux, O. Malhotra, 1981, Biochimie.

Half-site reactivity.

S. Bernhard, F. Seydoux, O. Malhotra, 1974, CRC critical reviews in biochemistry.

On site heterogeneity in sturgeon muscle GPDH: a kinetic approach.

S. Bernhard, F. Seydoux, 1974, Biophysical chemistry.

Preparation and active-site specific properties of sturgeon muscle glyceraldehyde-3-phoshate dehydrogenase.

S. Bernhard, F. Seydoux, O. Malhotra, 1973, Biochemistry.

Half-site reactivity and the "induced-fit" hypothesis.

S. Bernhard, R. MacQuarrie, 1973, Journal of molecular biology.

Direct transfer of reduced nicotinamide adenine dinucleotide from glyceraldehyde-3-phosphate dehydrogenase to liver alcohol dehydrogenase.

S. Bernhard, D. K. Srivastava, D. Srivastava, 1984, Biochemistry.

Mechanistic studies on equine liver alcohol dehydrogenase. I. The stoichiometry relationship of the coenzyme binding sites to the catalytic sites active in the reduction of aromatic aldehydes in the transient state.

P. Luisi, S. Bernhard, M. Dunn, 1970, Biochemistry.

The intracellular equilibrium thermodynamic and steady-state concentrations of metabolites

S. Bernhard, 2008, Cell Biophysics.

The optical detection of transients in trypsin- and chymotrypsin-catalyzed reactions.

S. Bernhard, H. Gutfreund, 1965, Proceedings of the National Academy of Sciences of the United States of America.

Structure and symmetry of oligomeric enzymes.

B. Matthews, S. Bernhard, 1973, Annual review of biophysics and bioengineering.

Major component of acetylcholinesterase in Torpedo electroplax is not basal lamina associated.

S. Bernhard, O. Viratelle, 1980, Biochemistry.

Neighboring Group Effects on Ester Hydrolysis. II. Neighboring Carbonyl Groups

S. Bernhard, Y. Shalitin, 1964 .

Co-operative Effects of Functional Groups in Peptides. I. Aspartyl-serine Derivatives

S. Bernhard, M. Sela, A. Berger, 1962 .

The Influence of pH on the Rate of Hydrolysis of Acylchymotrypsins

S. Bernhard, E. Hershberger, J. Keizer, 1966 .

Spectrophotometric identification of acyl enzyme intermediates.

H. Noller, S. Bernhard, S. Lau, 1965, Biochemistry.

Studies of catalysis by acetylcholinesterase. Synergistic effects of inhibitors during the hydrolysis of acetic acid esters.

S. Bernhard, T. Rosenberry, 1972, Biochemistry.

Isolation and structural determination of chromophoric acyl peptides from subtilisin enzymes.

H. Noller, S. Bernhard, 1965, Biochemistry.

On the function of half-site reactivity: intersubunit NAD+-dependent activation of acyl-glyceraldehyde 3-phosphate dehydrogenase reduction by NADH.

S. Bernhard, D. Ingbar, B. Schwendimann, 1976, Journal of molecular biology.

The structure of Meldrum's supposed beta-lactonic acid.

S. Bernhard, D. Davidson, 1948, Journal of the American Chemical Society.

Mechanism of Enzyme Inhibition by Phosphate Esters

L. Orgel, S. Bernhard, 1959, Science.

NUCLEOPHILIC DISPLACEMENT REACTIONS AT ESTER AND THIOLESTER BONDS

S. Bernhard, 1983, Annals of the New York Academy of Sciences.

Color, Conformation, and Catalysis

S. Bernhard, O. Malhotra, 1974 .

On the relationship between the conformation and the catalyzed reactivity of acyl-chymotrypsin.

S. Bernhard, G. Rossi, 1971, Journal of molecular biology.

On the interaction of the active side of alpha-chymotrypsin with chromophores: proflavin binding and enzyme conformation during catalysis.

B. Lee, S. Bernhard, Z. H. Tashjian, 1966, Journal of molecular biology.

Direct Transfer of Metabolites Via Enzyme-Enzyme Complexes: Evidence and Physiological Significance

S. Bernhard, D. K. Srivastava, D. Srivastava, 1986 .

Enzyme-enzyme interactions and the regulation of metabolic reaction pathways.

S. Bernhard, D. K. Srivastava, D K Srivastava, 1986, Current topics in cellular regulation.

Subunit conformation and catalytic function in rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase.

S. Bernhard, R. MacQuarrie, 1971, Journal of molecular biology.

Spectrophotometric identification of an active site-specific acyl glyceraldehyde 3-phosphate dehydrogenase. The regulation of its kinetic and equilibrium properties by coenzyme.

S. Bernhard, O. Malhotra, 1968, The Journal of biological chemistry.

The nucleotide and acyl group content of native rabbit muscle glyceraldehyde 3-phosphate dehydrogenase.

S. Bernhard, R. MacQuarrie, W. Bloch, 1971, The Journal of biological chemistry.

Activation of a covalent enzyme-substrate bond by noncovalent interaction with an effector.

S. Bernhard, O. Malhotra, 1973, Proceedings of the National Academy of Sciences of the United States of America.

Transient-state kinetic studies on the mechanism of furylacryloylphosphatase-coupled calcium ion transport with sarcoplasmic reticulum adenosine triphosphatase.

S. Bernhard, G. Inesi, M. Kurzmack, 1981, Biochemistry.

The structure and function of enzymes

S. Bernhard, 1968 .

On site--site interactions in the liver alcohol dehydrogenase catalytic mechanism.

S. Bernhard, J. Roque, M. Dunn, 1979, Biochemistry.

Specific Effects in Acid Catalysis by Ion Exchange Resins. II. Hydrolysis of Esters in Water Solution1

S. Bernhard, L. Hammett, 1953 .

Specific Effects in Acid Catalysis by Ion Exchange Resins. I. Hydrolysis of Esters in 70% Aqueous Acetone1

S. Bernhard, L. Hammett, 1953 .

Mechanism of transfer of reduced nicotinamide adenine dinucleotide among dehydrogenases. Transfer rates and equilibria with enzyme-enzyme complexes.

S. Bernhard, D. K. Srivastava, D. Srivastava, 1987, Biochemistry.

Mechanism of transfer of reduced nicotinamide adenine dinucleotide among dehydrogenases.

S. Bernhard, D. K. Srivastava, D. Srivastava, 1985, Biochemistry.

Metabolite transfer via enzyme-enzyme complexes.

S. Bernhard, D. K. Srivastava, D K Srivastava, 1986, Science.

Composition of the Grignard Reagent

S. Bernhard, J. Aston, 1950 .

Rapid kinetic evidence for adduct formation between the substrate analog p-nitroso-N,N-dimethylaniline and reduced nicotinamide-adenine dinucleotide during enzymic reduction.

S. Bernhard, M. Dunn, 1971, Biochemistry.

Spectrophotometric and structural evidence as to the mechanism of portease catalysis at chemical bonding resolution.

S. Bernhard, S. Lau, 1972, Cold Spring Harbor symposia on quantitative biology.

Ficincatalysed reactions: the affinity of ficin for some arginine derivatives.

S. Bernhard, H. Gutfreund, 1956, The Biochemical journal.

A new method for the determination of the amidase activity of trypsin: kinetics of the hydrolysis of benzoyl-L-arginineamide.

S. Bernhard, 1955, The Biochemical journal.

Studies of catalysis by acetylcholinesterase. I. Fluorescent titration with a carbamoylating agent.

S. Bernhard, T. Rosenberry, 1971, Biochemistry.

Biophysical chemistry of metabolic reaction sequences in concentrated enzyme solution and in the cell.

S. Bernhard, D. K. Srivastava, D. Srivastava, 1987, Annual review of biophysics and biophysical chemistry.

Uncoupling of calcium control and phosphohydrolase activity in sarcoplasmic reticulum vesicles.

S. Bernhard, R. Nakamoto, L. de Meis, 1980, The Journal of biological chemistry.

Transfer of 1,3-diphosphoglycerate between glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase via an enzyme-substrate-enzyme complex.

S. Bernhard, J. Weber, 1982, Biochemistry.

Functional consequences of the direct transfer of metabolites in muscle glycolysis.

S. Bernhard, D. K. Srivastava, 1987, Biochemical Society transactions.

The Protonic Equilibrium Accompanying the Acylation of Chymotrypsin and Subtilisin

S. Bernhard, J. Keizer, 1966 .

The mechanism of succinate or fumarate transfer in the tricarboxylic acid cycle allows molecular rotation of the intermediate.

S. Bernhard, P. Tompa, 1990, Archives of biochemistry and biophysics.

Molecular basis for the transfer of nicotinamide adenine dinucleotide among dehydrogenases.

R. Langridge, S. Bernhard, D. K. Srivastava, 1985, Biochemistry.

Halibut muscle 3-phosphoglycerate kinase. Chemical and physical properties of the enzyme and its substrate complexes.

S. Bernhard, F. Dahlquist, K. R. Huskins, 1982, Biochemistry.

Optical properties and the chemical nature of acyl-chymotrypsin linkages.

S. Bernhard, E. Charney, 1967, Journal of the American Chemical Society.

Chromophoric cinnamic acid substrates as resonance Raman probes of the active site environment in native and unfolded alpha-chymotrypsin.

S. Bernhard, W. Peticolas, P. Turpin, 1986, Biochemistry.

Kinetics of the System α-Chymotrypsin Methyl Hippurate Water Hydroxylamine: the Role of Water in Enzymatic Hydrolysis1

S. Bernhard, J. Nowell, W. Coles, 1960 .

Are the structure and function of an enzyme the same in aqueous solution and in the wet crystal?

S. Bernhard, G. Rossi, 1970, Journal of molecular biology.

Multiple ion-dependent and substrate-dependent Na+/K+-ATPase conformational states. Transient and steady-state kinetic studies.

S. Bernhard, D. F. Senear, G. Betts, 1985, Biochemistry.

Ionization constants and heats of tris(hydroxymethyl)aminomethane and phosphate buffers.

S. Bernhard, 1956, The Journal of biological chemistry.

Structure and symmetry of oligomeric enzymes.

B. Matthews, S. Bernhard, 1973, Annual review of biophysics and bioengineering.

Transient and steady-state kinetic studies of sodium-potassium adenosine triphosphatase using beta-(2-furyl)acryloyl phosphate as chromophoric substrate assay.

S. Bernhard, G. Betts, D. Chipman, 1981, Biochemistry.

Steps in the reactions of proteolytic enzymes with their substrates.

S. Bernhard, H. Gutfreund, 1970, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

Direct transfer of NADH between alpha-glycerol phosphate dehydrogenase and lactate dehydrogenase: fact or misinterpretation?

S. Bernhard, P. Smolen, G. Betts, 1989, Proceedings of the National Academy of Sciences of the United States of America.

SEQUENCE DETERMINATION IN BIOPOLYMERS

S. Bernhard, 1964 .

On the Relationship between Protein Conformation and Enzyme-Substrate Covalent Bond Formation in Glyceraldehyde-3-Phosphate Dehydrogenase

S. Bernhard, R. MacQuarrie, 1970 .