Conversion of Wild-type p53 Core Domain into a Conformation that Mimics a Hot-spot Mutant-Reference-Cited by-同舟云学术

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Conversion of Wild-type p53 Core Domain into a Conformation that Mimics a Hot-spot Mutant

Published:2003-10 Issue:2 Volume:333 Page:443-451
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Ishimaru Daniella,Maia Lenize F.,Maiolino Larissa M.,Quesado Pablo A.,Lopez Priscila C.M.,Almeida Fabio C.L.,Valente Ana Paula,Silva Jerson L.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference47 articles.

1. p53—integrating the complexity;Hall;J. Pathol.,1996

2. The p53 pathway;Prives;J. Pathol.,1999

3. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations;Cho;Science,1994

4. IARC p53 mutation database: a relational database to compile and analyze p53 mutations in human tumors and cell lines. International Agency for Research on Cancer;Hernandez-Boussard;Hum. Mutat.,1999

5. Hot-spot mutants of p53 core domain evince characteristic local structural changes;Wong;Proc. Natl Acad. Sci. USA,1999

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1. Multiscale simulations reveal the driving forces of p53C phase separation accelerated by oncogenic mutations;Chemical Science;2024

2. Protein of a thousand faces: The tumor-suppressive and oncogenic responses of p53;Frontiers in Molecular Biosciences;2022-08-25

3. Field exposure to 50 Hz significantly affects wild‑type and unfolded p53 expression in NB69 neuroblastoma cells;Oncology Letters;2022-07-05

4. Relevance of Amorphous and Amyloid-Like Aggregates of the p53 Core Domain to Loss of its DNA-Binding Activity;Frontiers in Molecular Biosciences;2022-04-26

5. Nucleic acid actions on abnormal protein aggregation, phase transitions and phase separation;Current Opinion in Structural Biology;2022-04

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