Proteomic identification of heat shock protein 90 as a candidate target for p53 mutation reactivation by PRIMA-1 in breast cancer cells - Wikidata - wikimedia - TriplyDB

Proteomic identification of heat shock protein 90 as a candidate target for p53 mutation reactivation by PRIMA-1 in breast cancer cells

Proteomic identification of heat shock protein 90 as a candidate target for p53 mutation reactivation by PRIMA-1 in breast cancer cells

http://www.wikidata.org/entity/Q24813658

about

p53 transactivation and the impact of mutations, cofactors and small molecules using a simplified yeast-based screening system PRIMA-1MET induces nucleolar translocation of Epstein-Barr virus-encoded EBNA-5 protein.Targeting p53 for Novel Anticancer Therapy.SCH529074, a small molecule activator of mutant p53, which binds p53 DNA binding domain (DBD), restores growth-suppressive function to mutant p53 and interrupts HDM2-mediated ubiquitination of wild type p53 Dysregulation of apoptotic signaling in cancer: molecular mechanisms and therapeutic opportunities Small-Molecule Reactivation of Mutant p53 to Wild-Type-like p53 through the p53-Hsp40 Regulatory Axis Strategies for therapeutic targeting of the p53 pathway in cancer.Breast cancer proteomics: clinical perspectives.Risk assessment, disease prevention and personalised treatments in breast cancer: is clinically qualified integrative approach in the horizon?Reactivation of mutant p53: molecular mechanisms and therapeutic potential.PRIMA-1 increases cisplatin sensitivity in chemoresistant ovarian cancer cells with p53 mutation: a requirement for Akt down-regulation.[The use of p53 as a tool for human cancer therapy].Pharmacological activation of p53 in cancer cells Targeting cancer stem cells with p53 modulators.Sequential transcription factor targeting for diffuse large B-cell lymphomas.New Insights in Thyroid Cancer and p53 Family Proteins.Reactivation of p53 mutants by prima-1 [corrected] in thyroid cancer cells.PRIMA-1(MET) induces nucleolar accumulation of mutant p53 and PML nuclear body-associated proteins.PRIMA-1 and PRIMA-1Met (APR-246): From Mutant/Wild Type p53 Reactivation to Unexpected Mechanisms Underlying Their Potent Anti-Tumor Effect in Combinatorial Therapies.Catalytic Role of Thermostable Metalloproteases from Bacillus subtilis KT004404 as Dehairing and Destaining Agent.Antitumor effects of anlotinib in thyroid cancer

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Proteomic identification of heat shock protein 90 as a candidate target for p53 mutation reactivation by PRIMA-1 in breast cancer cells

http://www.wikidata.org/entity/Q24813658

description

2005 nî lūn-bûn

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Proteomic identification of he ...... PRIMA-1 in breast cancer cells

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Proteomic identification of he ...... PRIMA-1 in breast cancer cells

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Proteomic identification of he ...... PRIMA-1 in breast cancer cells

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Proteomic identification of he ...... PRIMA-1 in breast cancer cells

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Proteomic identification of he ...... PRIMA-1 in breast cancer cells

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Proteomic identification of he ...... PRIMA-1 in breast cancer cells

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Proteomic identification of he ...... PRIMA-1 in breast cancer cells

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Proteomic identification of he ...... PRIMA-1 in breast cancer cells

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Breast Cancer Research

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Proteomic identification of he ...... PRIMA-1 in breast cancer cells

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Abdur Rehman

http://www.w3.org/2001/XMLSchema#string

James E Bruce

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Manpreet S Chahal

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Sayed S Daoud

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Xiaoting Tang

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P2860

T RANSPORT B ETWEEN THE C ELL N UCLEUS AND THE C YTOPLASM

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

Mutations in residues of TP53 that directly contact DNA predict poor outcome in human primary breast cancer.

WAF1, a potential mediator of p53 tumor suppression

Phosphorylation and hsp90 binding mediate heat shock stabilization of p53

Evidence for reversible, non-microtubule and non-microfilament-dependent nuclear translocation of hsp90 after heat shock in human fibroblasts.

Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound.

Mutations in the p53 tumor suppressor gene and early onset breast cancer.

Nuclear translocation of the Hsp70/Hsp90 organizing protein mSTI1 is regulated by cell cycle kinases.

Regulation of tumor suppressors by nuclear-cytoplasmic shuttling.

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10.1186/BCR1290

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