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Phosphorylation at Ser-15 and Ser-392 in mutant p53 molecules from human tumors is altered compared to wild-type p53.

Data up to Jan 2025

Published1993
Citations91
References55

Total Citations Per Year

Abstract

References (55)

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Human DNA-Activated Protein Kinase Phosphorylates Serines 15 and 37 in the Amino-Terminal Transactivation Domain of Human p53

1992 • 473 citations

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1991 • 419 citations

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1990 • 415 citations

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1990 • 409 citations

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1992 • 278 citations

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1990 • 277 citations

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1991 • 251 citations

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1992 • 193 citations

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1992 • 192 citations

The p53 tumor suppressor protein, a modulator of cell proliferation.

1992 • 171 citations

Mutant p53 proteins bind DNA abnormally in vitro.

1991 • 166 citations

Modulation of cellular and viral promoters by mutant human p53 proteins found in tumor cells

1992 • 161 citations

p53 interacts with p34cdc2 in mammalian cells: implications for cell cycle control and oncogenesis.

1990 • 156 citations

Human Cells Contain a DNA-Activated Protein Kinase that Phosphorylates Simian Virus 40 T Antigen, Mouse p53, and the Human Ku Autoantigen

1990 • 144 citations

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1992 • 135 citations

Phosphorylation of the p53 tumour-suppressor protein at three N-terminal sites by a novel casein kinase I-like enzyme.

1992 • 121 citations

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1991 • 113 citations

Analysis of p53 mutants for transcriptional activity.

1991 • 106 citations

Mutation of the casein kinase II phosphorylation site abolishes the anti-proliferative activity of p53

1992 • 105 citations

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1992 • 99 citations

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1992 • 96 citations

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1991 • 86 citations

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1992 • 74 citations

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1990 • 72 citations

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1991 • 41 citations

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1985 • 17 citations

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1992 • 11 citations

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1990 • 10 citations

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Phosphorylation at Ser-15 and Ser-392 in mutant p53 molecules from human tumors is… (1993) – Proceedings of the National Academy of Sciences | Metascience Observatory Explorer