(Q43675801)

25 November 2017

title

ATP stimulates MDM2-mediated inhibition of the DNA-binding function of E2F1. (English)

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25 November 2017

3

Bartosz Wawrzynow

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25 November 2017

6

Alicja Zylicz

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25 November 2017

Craig Stevens

1

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25 November 2017

Susanne Pettersson

2

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25 November 2017

Maura Wallace

4

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25 November 2017

Kathryn Ball

5

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25 November 2017

Ted R Hupp

7

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25 November 2017

language of work or name

English

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publication date

27 August 2008

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25 November 2017

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25 November 2017

volume

275

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25 November 2017

issue

19

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25 November 2017

page(s)

4875-4886

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Roles of molecular chaperones in protein misfolding diseases

25 November 2017

cites work

1 reference

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Molecular chaperones and the stress of oncogenesis

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Heat shock response modulators as therapeutic tools for diseases of protein conformation

21 January 2018

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Therapeutic and diagnostic implications of Hsp90 activation

21 January 2018

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A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors

21 January 2018

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Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications

21 January 2018

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Heat-shock protein 90 inhibitors as novel cancer chemotherapeutics - an update

21 January 2018

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Specific interaction between the p53 cellular tumour antigen and major heat shock proteins

21 January 2018

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https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent

21 January 2018

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https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Geldanamycin-stimulated destabilization of mutated p53 is mediated by the proteasome in vivo

21 January 2018

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https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Hsp90 chaperones wild-type p53 tumor suppressor protein

21 January 2018

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Hsp70 interactions with the p53 tumour suppressor protein

21 January 2018

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Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.

21 January 2018

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P53: an ubiquitous target of anticancer drugs

21 January 2018

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Hsp90 is essential for restoring cellular functions of temperature-sensitive p53 mutant protein but not for stabilization and activation of wild-type p53: implications for cancer therapy.

21 January 2018

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https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Inhibition of MDM2 by hsp90 contributes to mutant p53 stabilization

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Expansion of protein interaction maps by phage peptide display using MDM2 as a prototypical conformationally flexible target protein

21 January 2018

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https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

MDM2 chaperones the p53 tumor suppressor

21 January 2018

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https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Nucleotide binding by the Mdm2 RING domain facilitates Arf-independent Mdm2 nucleolar localization

21 January 2018

1 reference

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Allosteric regulation of the thermostability and DNA binding activity of human p53 by specific interacting proteins. CRC Cell Transformation Group

21 January 2018

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Correcting temperature-sensitive protein folding defects

21 January 2018

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Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein

21 January 2018

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Mapping of the p53 and mdm-2 interaction domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Mdm2 promotes the rapid degradation of p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Destabilizing missense mutations in the tumour suppressor protein p53 enhance its ubiquitination in vitro and in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

E2F and cell cycle control: a double-edged sword

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Stimulation of E2F1/DP1 transcriptional activity by MDM2 oncoprotein

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

The central acidic domain of MDM2 is critical in inhibition of retinoblastoma-mediated suppression of E2F and cell growth

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Stabilization of E2F1 protein by MDM2 through the E2F1 ubiquitination pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Transcription factor E2F-1 is upregulated in response to DNA damage in a manner analogous to that of p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Apoptotic and growth-promoting activity of E2F modulated by MDM2

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Mouse double minute antagonist Nutlin-3a enhances chemotherapy-induced apoptosis in cancer cells with mutant p53 by activating E2F1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

Mdm2 inhibition of p53 induces E2F1 transactivation via p21.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

The E2F-1 transcription factor is negatively regulated by its interaction with the MDMX protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2008.06627.X

10.1111/J.1742-4658.2008.06627.X

21 January 2018

Identifiers

DOI

1 reference

25 November 2017

1 reference