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Amino acid substitutions that increase the thermal stability of the λ Cro protein

Data up to Jan 2025

Published1989
Citations91
References29

Total Citations Per Year

Abstract

References (29)

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Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein

1987 • 253 citations

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1985 • 189 citations

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1984 • 153 citations

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1978 • 145 citations

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1986 • 145 citations

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1983 • 139 citations

Lambda repressor mutations that increase the affinity and specificity of operator binding

1985 • 136 citations

Is protein turnover thermodynamically controlled?

1978 • 97 citations

Comparison of the structures of Cro and λ repressor proteins from bacteriophage λ

1983 • 91 citations

Effect on protein stability of reversing the charge on amino groups

1982 • 89 citations

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1984 • 82 citations

Identification of C-terminal extensions that protect proteins from intracellular proteolysis

1989 • 76 citations

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1971 • 70 citations

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1985 • 61 citations

Purification and properties of a DNA-binding protein with characteristics expected for the Cro protein of bacteriophage lambda, a repressor essential for lytic growth.

1976 • 51 citations

Increasing and decreasing protein stability: Effects of revertant substitutions on the thermal denaturation of phage λ repressor

1985 • 42 citations

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1971 • 7 citations

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Amino acid substitutions that increase the thermal stability of the λ Cro protein (1989) – Proteins Structure Function and Bioinformatics | Metascience Observatory Explorer