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Overexpression in Escherichia coli, purification and characterization of the molecular chaperone HSC70

Data up to Jan 2025

Published1994
Citations22
References67

Total Citations Per Year

Abstract

References (67)

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1988 • 194 citations

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1991 • 191 citations

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1992 • 176 citations

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1985 • 164 citations

Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis

1990 • 159 citations

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1984 • 153 citations

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Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange

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Coated vesicles

1980 • 75 citations

ATP catalyzes the sequestration of clathrin during enzymatic uncoating.

1985 • 73 citations

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1989 • 59 citations

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1992 • 42 citations

Aspartyl residue 10 is essential for ATPase activity of rat hsc70.

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Propagation of allosteric changes through the catalytic-regulatory interface of Escherichia coli aspartate transcarbamylase

1988 • 23 citations

Inhibitory effects of HSP70 chaperones on nascent polypeptides

1992 • 19 citations

Biochemical and Biophysical Comparison of Bacterial DnaK and Mammalian hsc73, Two Members of an Ancient Stress Protein Family

1990 • 8 citations

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Overexpression in Escherichia coli, purification and characterization of the molecular… (1994) – European Journal of Biochemistry | Metascience Observatory Explorer