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ISOLATION OF CRYSTALLINE PHOSPHOGLUCOSE ISOMERASE FROM BREWERS' YEAST
ISOLATION OF CRYSTALLINE PHOSPHOGLUCOSE ISOMERASE FROM BREWERS' YEAST
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ISOLATION OF CRYSTALLINE PHOSPHOGLUCOSE ISOMERASE FROM BREWERS' YEAST

NAKAGAWA, Y ; NOLTMANN, E A

The Journal of biological chemistry, 1965-05, Vol.240 (5), p.1877-1881 [Periódico revisado por pares]

United States

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2
Studies on the Nature of the Inhibition by Gossypol of the Transformation of Pepsinogen to Pepsin
Studies on the Nature of the Inhibition by Gossypol of the Transformation of Pepsinogen to Pepsin
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Studies on the Nature of the Inhibition by Gossypol of the Transformation of Pepsinogen to Pepsin

Wong, Rosie C. ; Nakagawa, Yasushi ; Perlmann, Gertrude E.

The Journal of biological chemistry, 1972-03, Vol.247 (5), p.1625-1631 [Periódico revisado por pares]

United States: Elsevier Inc

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3
Physical and Chemical Properties of Yeast Phosphoglucose Isomerase Isoenzymes
Physical and Chemical Properties of Yeast Phosphoglucose Isomerase Isoenzymes
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Physical and Chemical Properties of Yeast Phosphoglucose Isomerase Isoenzymes

Kempe, Thomas D. ; Nakagawa, Yasushi ; Noltmann, Ernst A.

The Journal of biological chemistry, 1974-07, Vol.249 (14), p.4617-4624 [Periódico revisado por pares]

United States: Elsevier Inc

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4
Multiple forms of carboxypeptidase Y from Saccharomyces cerevisiae. kinetic demonstration of effects of carbohydrate residues on the catalytic mechanism of a glycoenzyme
Multiple forms of carboxypeptidase Y from Saccharomyces cerevisiae. kinetic demonstration of effects of carbohydrate residues on the catalytic mechanism of a glycoenzyme
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Multiple forms of carboxypeptidase Y from Saccharomyces cerevisiae. kinetic demonstration of effects of carbohydrate residues on the catalytic mechanism of a glycoenzyme

Margolis, H.C ; Nakagawa, Y ; Douglas, K.T ; Kaiser, E.T

The Journal of biological chemistry, 1978-11, Vol.253 (21), p.7891-7897 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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5
Purification and characterization of a calcium oxalate monohydrate crystal growth inhibitor from human kidney tissue culture medium
Purification and characterization of a calcium oxalate monohydrate crystal growth inhibitor from human kidney tissue culture medium
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Purification and characterization of a calcium oxalate monohydrate crystal growth inhibitor from human kidney tissue culture medium

Nakagawa, Y ; Margolis, H C ; Yokoyama, S ; Kézdy, F J ; Kaiser, E T ; Coe, F L

The Journal of biological chemistry, 1981-04, Vol.256 (8), p.3936-3944 [Periódico revisado por pares]

United States

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6
Glia Maturation Factor Promotes Contact Inhibition in Cancer Cells
Glia Maturation Factor Promotes Contact Inhibition in Cancer Cells
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Glia Maturation Factor Promotes Contact Inhibition in Cancer Cells

Lim, Ramon ; Nakagawa, Satoe ; Barry G. W. Arnason ; Turriff, David E.

Proceedings of the National Academy of Sciences - PNAS, 1981-07, Vol.78 (7), p.4373-4377 [Periódico revisado por pares]

United States: National Academy of Sciences of the United States of America

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7
Purification and characterization of the principal inhibitor of calcium oxalate monohydrate crystal growth in human urine
Purification and characterization of the principal inhibitor of calcium oxalate monohydrate crystal growth in human urine
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Purification and characterization of the principal inhibitor of calcium oxalate monohydrate crystal growth in human urine

Nakagawa, Y ; Abram, V ; Kézdy, F J ; Kaiser, E T ; Coe, F L

The Journal of biological chemistry, 1983-10, Vol.258 (20), p.12594-12600 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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8
A subunit of yeast site-specific endonuclease SceI is a mitochondrial version of the 70-kDa heat shock protein
A subunit of yeast site-specific endonuclease SceI is a mitochondrial version of the 70-kDa heat shock protein
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A subunit of yeast site-specific endonuclease SceI is a mitochondrial version of the 70-kDa heat shock protein

Morishima, N. (Riken Institute, Saitama, Japan) ; Nakagawa, K ; Yamamoto, E ; Shibata, T

The Journal of biological chemistry, 1990-09, Vol.265 (25), p.15189-15197 [Periódico revisado por pares]

Bethesda, MD: American Society for Biochemistry and Molecular Biology

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9
Rabbit liver microsomal endopeptidase with substrate specificity for processing proproteins is structurally related to rat testes metalloendopeptidase 24.15
Rabbit liver microsomal endopeptidase with substrate specificity for processing proproteins is structurally related to rat testes metalloendopeptidase 24.15
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Rabbit liver microsomal endopeptidase with substrate specificity for processing proproteins is structurally related to rat testes metalloendopeptidase 24.15

KAWABATA, S.-I ; NAKAGAWA, K ; MUTA, T ; IWANAGA, S ; DAVIE, E. W

The Journal of biological chemistry, 1993-06, Vol.268 (17), p.12498-12503 [Periódico revisado por pares]

Bethesda, MD: American Society for Biochemistry and Molecular Biology

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10
Vision in the ctenid spider Cupiennius salei: spectral range and absolute sensitivity
Vision in the ctenid spider Cupiennius salei: spectral range and absolute sensitivity
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Vision in the ctenid spider Cupiennius salei: spectral range and absolute sensitivity

BARTH, F. G ; NAKAGAWA, T ; EGUCHI, E

Journal of experimental biology, 1993-08, Vol.181 (1), p.63-79 [Periódico revisado por pares]

Cambridge: Company of Biologists

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