J. Nishimura

发表

Effect of glycerol on Lowry and biuret methods of protein determination.

M. K. Zishka, J. Nishimura, 1970, Analytical biochemistry.

Porcine heart succinate thiokinase Reactivity of sulfhydryl groups, cross-linking and immunochemical properties of the enzyme

Y. Murakami, J. Nishimura, 1974 .

Succinate thiokinase of Escherichia coli. Purification, phosphorylation of the enzyme, and exchange reactions catalyzed by the enzyme.

F. Grinnell, J. Nishimura, 1969, Biochemistry.

Site-directed mutagenesis of Escherichia coli succinyl-CoA synthetase. Histidine 142 alpha is a facilitative catalytic residue.

J. Nishimura, G. Luo, 1991, The Journal of biological chemistry.

Modular structure of neuronal nitric oxide synthase: localization of the arginine binding site and modulation by pterin.

P. Martásek, Q. Liu, K. McMillan, 1995, Biochemical and biophysical research communications.

Phosphorylation and formation of hybrid enzyme species test the "half of sites" reactivity of Escherichia coli succinyl-CoA synthetase.

J. Nishimura, C. J. Mann, T. Mitchell, 1991, Biochemistry.

Studies on the mechanism of activation acid beta-decarboxylase by alpha-keto acids and pyridoxal 5'-phosphate.

A. Meister, J. Manning, J. Nishimura, 1962, Biochemistry.

Evidence for Succinyl Phosphate as an Enzyme-bound Intermediate in the Reaction Catalyzed by Succinyl Coenzyme A Synthetase*

A. Meister, J. Nishimura, 1965 .

Phenoxazinone Synthetase from Streptomyces antibioticus: Multiple Activities of the Enzyme

E. Golub, J. Nishimura, 1972, Journal of bacteriology.

On the effects of cyanide on phenoxazinone synthetase.

E. Golub, J. Nishimura, 1969, Biochimica et biophysica acta.

Involvement of the reductase domain of neuronal nitric oxide synthase in superoxide anion production.

R. T. Miller, B. Masters, P. Martásek, 1997, Biochemistry.

Intrinsic fluorescence of succinyl-CoA synthetase and four tryptophan mutants. Tryptophan 76 and tryptophan 248 of the beta-subunit are responsive to CoA binding.

P. Horowitz, J. Ybarra, J. Nishimura, 1990, Biochemistry.

Affinity labeling of succinyl-CoA synthetase from Escherichia coli by the 2',3'-dialdehyde derivative of adenosine 5'-diphosphate.

D. J. Ball, G. E. Collier, J. Nishimura, 1983, European journal of biochemistry.

Succinyl-CoA synthetase structure-function relationships and other considerations.

J. Nishimura, 2006, Advances in enzymology and related areas of molecular biology.

Nucleotide specificity of Escherichia coli succinic thiokinase. Succinyl coenzyme A-stimulated nucleoside diphosphate kinase activity of the enzyme.

J. Nishimura, T. Mitchell, K. Murakami, 1972, The Journal of biological chemistry.

INTERMEDIATE FORMATION OF DIPEPTIDE-PHOSPHATE ANHYDRIDE IN ENZYMATIC TRIPEPTIDE SYNTHESIS.

A. Meister, J. Nishimura, E. A. Dodd, 1964, The Journal of biological chemistry.

Acetate kinase from Veillonella alcalescens. Regulation of enzyme activity by succinate and substrates.

R. Valdez, C. Bowman, J. Nishimura, 1976, The Journal of biological chemistry.

Reversible modification of the sulfhydryl groups of Escherichia coli succinic thiokinase with methanethiolating reagents, 5.5'-Dithio-bis(2-nitrobenzoic acid), p-hydroxymercuribenzoate, and ethylmercurithiosalicylate.

G. L. Kenyon, D. J. Smith, J. Nishimura, 1975, Archives of biochemistry and biophysics.

Biosynthesis of the Actinomycin Chromophore: Incorporation of 3-Hydroxy-4-Methylanthranilic Acid into Actinomycins by Streptomyces antibioticus

E. Golub, M. A. Ward, J. Nishimura, 1969, Journal of bacteriology.

Mechanism of Action and Other Properties of Succinyl Coenzyme A Synthetase

F. Grinnell, J. Nishimura, 2006 .

The influence of chaotropic reagents on neuronal nitric oxide synthase and its flavoprotein module. Urea and guanidine hydrochloride stimulate NADPH-cytochrome c reductase activity of both proteins.

B. Masters, P. Horowitz, K. McMillan, 1997, Nitric oxide : biology and chemistry.

Biosynthesis oftheActinomycin Chromophore: Incorporation of3-Hydroxy-4-Meth ylanthranilic AcidintoActinomycins by Streptomyces antibioticus

M. A. Ward, J. Nishimura, 1969 .

Erratum: Neuronal nitric oxide synthase, a modular enzyme formed by convergent evolution: Structure studies of a cysteine thiolate-liganded heme protein that hydroxylates L-arginine to produce NO· as a cellular signal (The FASEB Journal (1996) 10 (552-558))

B. Masters, E. Sheta, P. Martásek, 1996 .

Isolation, amino acid analyses and refolding of subunits of pig heart succinyl-CoA synthetase.

P. Horowitz, J. Ybarra, J. Nishimura, 1988, Biochemical Journal.

Neuronal nitric oxide synthase, a modular enzyme formed by convergent evolution: structure studies of a cysteine thiolate‐liganded heme protein that hydroxylates L‐arginine to produce NO as a cellular signal

E. Sheta, P. Martásek, K. McMillan, 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Chemical modification of tryptophan residues in Escherichia coli succinyl-CoA synthetase. Effect on structure and enzyme activity.

J. Ybarra, A. R. Prasad, J. Nishimura, 1986, Biochemistry.

Chemical modification of Escherichia coli succinyl-CoA synthetase with the adenine nucleotide analogue 5'-p-fluorosulphonylbenzoyladenosine.

J. Ybarra, A. R. Prasad, J. Nishimura, 1983, The Biochemical journal.

A study of the quenching of the intrinsic fluorescence of succinyl-CoA synthetase from Escherichia coli by acrylamide, iodide, and coenzyme A.

P. Horowitz, A. R. Prasad, J. Nishimura, 1983, Biochemistry.

Affinity labeling of succinyl-CoA synthetase from porcine heart and Escherichia coli with oxidized coenzyme A disulfide.

G. E. Collier, J. Nishimura, 1978, The Journal of biological chemistry.

Inactivation of Escherichia coli succinic thiokinase by selective oxidation of thiol groups by permanganate.

J. Nishimura, J. Matula, T. Mitchell, 1976, Biochemical and biophysical research communications.

Escherichia coli succinic thiolinase. Stoichiometry of phosphorylation and coenzyme A binding.

C. Bowman, J. Nishimura, 1975, The Journal of biological chemistry.

Purification and properties of L-threonine dehydrase of sheep liver.

D. M. Greenberg, J. Nishimura, 1961, The Journal of biological chemistry.

[12] Prokaryotic expression, purification, and characterization of intact and modular constructs of neuronal nitric oxide synthase

B. Masters, P. Martásek, K. McMillan, 1996 .

Formation of succinyl phosphate by reaction of phosphorylated succinic thiokinase with succinate.

J. Nishimura, 1967, Biochemistry.

A rapid and simple procedure for preparation of - 32 P-labeled nucleoside triphosphates.

M. K. Zishka, J. Nishimura, R. W. Keenan, 1972, Analytical biochemistry.

Protein Crosslinking: Nutritional and Medical Consequences

J. Nishimura, 1979 .

Transamination and beta-decarboxylation of aspartate catalyzed by the same pyridoxal phosphate-enzyme.

A. Meister, A. Novogrodsky, J. Nishimura, 1963, The Journal of biological chemistry.

The Stimulatory Effects of Hofmeister Ions on the Activities of Neuronal Nitric-oxide Synthase

R. T. Miller, B. Masters, L. Roman, 1999, The Journal of Biological Chemistry.

Native-like intermediate on the folding pathway of Escherichia coli succinyl-CoA synthetase.

I. A. Khan, J. Nishimura, 1988, The Journal of biological chemistry.

Fluorescence detection of increased local flexibility induced by coenzyme A in succinyl-coA synthetase from Escherichia coli.

P. Horowitz, A. R. Prasad, J. Nishimura, 1982, Biochemistry.

The inactivation and dissociation of Escherichia coli succinyl-CoA synthetase by sulfhydryl reagents.

F. Grinnell, J. Nishimura, 1970, Biochimica et biophysica acta.

Understanding the structural aspects of neuronal nitric oxide synthase (NOS) using microdissection by molecular cloning techniques: molecular dissection of neuronal NOS.

B. Masters, E. Sheta, P. Martásek, 1996, Advances in experimental medicine and biology.

The mechanism of the succinic thiokinase reaction. Effector role of desulfo-coenzyme A in succinyl phosphate formation.

F. Grinnell, J. Nishimura, 1969, Biochemistry.

Coenzyme A thiosulfonate (coenzyme A disulfide-S,S-dioxide), an affinity analog of coenzyme A.

K. A. Hill, G. E. Collier, J. Nishimura, 1982, The Journal of biological chemistry.

Acetate kinase from Veillonella alcalescens. Regulation by succinate and substrates.

M. Griffith, J. Nishimura, 1979, Journal of Biological Chemistry.

[37] Acetate kinase from Veillonella alcalescens: EC 2.7.2.1 ATP:acetate phosphotransferase

M. Griffith, J. Nishimura, 1981 .

Reversible disaggregation of Escherichia coli succinyl-CoA synthetase.

F. Grinnell, B. Stollar, J. Nishimura, 1969, Biochimica et biophysica acta.

The effects of various N-substituted maleimides on succinic thiokinase of Escherichia coli.

J. Nishimura, J. Matula, 1978, International Journal of Biochemistry.

Cross-linking of Escherichia coli succinic thiokinase. I. Reaction with diiminoesters and dimaleimides.

J. Nishimura, J. Teherani, 1975, The Journal of biological chemistry.

Immunochemical studies of Escherichia coli succinic thiokinase. Effects of sulfhydryl reagents and other treatments on the enzyme.

F. Grinnell, J. Nishimura, T. Mitchell, 1973, The Journal of biological chemistry.

N,N'-o-Phenylenedi[1,4-14C]maleimide. Its synthesis and application in the cross-linking of Escherichia coli succinic thiokinase.

J. Nishimura, T. Mitchell, A. Milne, 1978, The International journal of biochemistry.

Site-directed mutagenesis of Escherichia coli succinyl-CoA synthetase. beta-Cys325 is a nonessential active site residue.

S. Hardies, J. Nishimura, C. J. Mann, 1989, The Journal of biological chemistry.

Reaction of substrates with 35S-thiophosphorylated succinyl-CoA synthetase of pig heart. Similarities to the case of the Escherichia coli enzyme.

J. Nishimura, T. Mitchell, 1985, The Journal of biological chemistry.

Adenosine 5'-O-(3-thio)triphosphate, a substrate and potent inhibitor of Escherichia coli succinyl-CoA synthetase. Additional evidence for a cooperative alternating-sites mechanism.

J. Nishimura, T. Mitchell, 1984, The Journal of biological chemistry.

Escherichia coli succinyl coenzyme A synthetase. Inhibition of ATP-stimulated succinate----succinyl coenzyme A exchange at low succinyl coenzyme A concentrations by an ADP trap.

J. Nishimura, T. Mitchell, 1984, The Journal of biological chemistry.