Mutant p53 aggregates into prion-like amyloid oligomers and fibrils: implications for cancer. (Q36201740)

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5 February 2020

title

Mutant p53 aggregates into prion-like amyloid oligomers and fibrils: implications for cancer (English)

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8

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Ana Carolina Stumbo

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Yraima Cordeiro

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Jerson Lima

13

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Guilherme A P de Oliveira

5 February 2020

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author name string

Ana P D Ano Bom

1

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Luciana P Rangel

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Danielly C F Costa

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Guilherme A P de Oliveira

4

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5 February 2020

Daniel Sanches

5

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Carolina A Braga

6

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Lisandra M Gava

7

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Ana O T Cepeda

9

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Claudia V De Moura Gallo

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language of work or name

English

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publication date

19 June 2012

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Journal of Biological Chemistry

5 February 2020

published in

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volume

287

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issue

33

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5 February 2020

page(s)

28152-28162

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The two faces of Janus: functional interactions and protein aggregation

5 February 2020

cites work

1 reference

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1 October 2017

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1 October 2017

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The transcellular spread of cytosolic amyloids, prions, and prionoids

1 October 2017

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1 October 2017

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Ligand binding and hydration in protein misfolding: insights from studies of prion and p53 tumor suppressor proteins

1 October 2017

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1 October 2017

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The peculiar interaction between mammalian prion protein and RNA

1 October 2017

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Prion protein complexed to N2a cellular RNAs through its N-terminal domain forms aggregates and is toxic to murine neuroblastoma cells

1 October 2017

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Structural biology of the tumor suppressor p53.

1 October 2017

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The (1-63) region of the p53 transactivation domain aggregates in vitro into cytotoxic amyloid assemblies.

1 October 2017

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1 October 2017

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Prions and transmissible spongiform encephalopathy (TSE) chemotherapeutics: A common mechanism for anti-TSE compounds?

1 October 2017

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1 October 2017

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Potent antiscrapie activities of degenerate phosphorothioate oligonucleotides

1 October 2017

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Unfolding, aggregation, and amyloid formation by the tetramerization domain from mutant p53 associated with lung cancer

1 October 2017

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Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils.

1 October 2017

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The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation

1 October 2017

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Conformation-dependent antibodies target diseases of protein misfolding

1 October 2017

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Reversible aggregation plays a crucial role on the folding landscape of p53 core domain

1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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1 October 2017

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Cognate DNA stabilizes the tumor suppressor p53 and prevents misfolding and aggregation.

1 October 2017

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Physical basis of colors seen in Congo red-stained amyloid in polarized light.

22 September 2018

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Hydration and packing effects on prion folding and beta-sheet conversion. High pressure spectroscopy and pressure perturbation calorimetry studies.

22 September 2018

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Fibrillar aggregates of the tumor suppressor p53 core domain

22 September 2018

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Structure, function, and aggregation of the zinc-free form of the p53 DNA binding domain

22 September 2018

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Co-localization of mutant p53 and amyloid-like protein aggregates in breast tumors

22 September 2018

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Heparin Binding by Murine Recombinant Prion Protein Leads to Transient Aggregation and Formation of RNA-Resistant Species

21 January 2018

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Gain of function of mutant p53 by coaggregation with multiple tumor suppressors

21 January 2018

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Amyloid Fibrils of Mammalian Prion Protein Are Highly Toxic to Cultured Cells and Primary Neurons

21 January 2018

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p53 protein accumulation detected by five different antibodies: relationship to prognosis and heat shock protein 70 in breast cancer

21 January 2018

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12 December 2020

Role of p53 alteration in primary peritoneal carcinoma

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12 December 2020

Tumor pH: implications for treatment and novel drug design

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12 December 2020

Soluble oligomers from a non-disease related protein mimic Abeta-induced tau hyperphosphorylation and neurodegeneration

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12 December 2020

Identifiers

DOI

10.1074/JBC.M112.340638

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22715097%20AND%20SRC:MED&resulttype=core&format=json

5 February 2020

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5 February 2020

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