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Interactions of fructose 1,6-diphosphate, substrates, and monovalent cations with yeast pyruvate kinase monitored by changes in enzyme fluorescence

Data up to Jan 2025

Published1971
Citations21
References22

Total Citations Per Year

Abstract

References (22)

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Enzymes Activated by Monovalent Cations

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1969 • 78 citations

Thallium-205 nuclear magnetic resonance as a probe for studying metal ion binding to biological macromolecules. Estimate of the distance between the monovalent and divalent activators of pyruvate kinase

1970 • 74 citations

Yeast Pyruvate Kinase

1969 • 70 citations

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1966 • 69 citations

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1969 • 69 citations

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1968 • 62 citations

Unusual difference spectra of proteins containing tryptophan. II. Proteins

1969 • 59 citations

Effect of temperature and effectors on the conformations of yeast pyruvate kinase

1970 • 48 citations

Effects of Temperature and Activating Cations on the Fluorescence of Pyruvate Kinase*

1967 • 42 citations

Interaction between Potassium-, Ammonium- and Fructose-1,6-diphosphate Activation of Yeast Pyruvate Kinase

1967 • 29 citations

Amino-Acid Composition and Subunit Structure of Yeast-Pyruvate Kinase

1970 • 22 citations

Yeast pyruvate kinase. Native and subunit molecular weight

1970 • 21 citations

Fructose 1,6-diphosphate enhanced inactivation of yeast pyruvate kinase at 23°. Evidence for a stabilized dimer intermediate

1971 • 18 citations

STUDIES ON PYRUVATE KINASE FROM BAKER'S YEAST*

1960 • 10 citations

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Interactions of fructose 1,6-diphosphate, substrates, and monovalent cations with yeast… (1971) – Biochemistry | Metascience Observatory Explorer