Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy. - Wikidata - wikimedia - TriplyDB

Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.

Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.

http://www.wikidata.org/entity/Q36465517

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Structure of human heat-shock transcription factor 1 in complex with DNA Selective targeting of the stress chaperome as a therapeutic strategy Immune-associated proteins with potential inï¿½vivo anti-tumor activities are upregulated in lung cancer cells treated with umbelliprenin: A proteomic approach Combined HSP90 and kinase inhibitor therapy: Insights from The Cancer Genome Atlas.Inhibition of COP9-signalosome (CSN) deneddylating activity and tumor growth of diffuse large B-cell lymphomas by doxycycline.Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease.Y-632 inhibits heat shock protein 90 (Hsp90) function by disrupting the interaction between Hsp90 and Hsp70/Hsp90 organizing protein, and exerts antitumor activity in vitro and in vivo X66, a novel N-terminal heat shock protein 90 inhibitor, exerts antitumor effects without induction of heat shock response A novel HSP90 inhibitor with reduced hepatotoxicity synergizes with radiotherapy to induce apoptosis, abrogate clonogenic survival, and improve tumor control in models of colorectal cancer.Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.The epichaperome is an integrated chaperome network that facilitates tumour survival Wee1-Hsp90 inhibitor combination treatment: molecular therapy with potentially broad applicability A Novel HSP90 Inhibitor-Drug Conjugate to SN38 Is Highly Effective in Small Cell Lung Cancer.Chaperoning parasitism: the importance of molecular chaperones in pathogen virulence.Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90.Clinical Evaluation and Biomarker Profiling of Hsp90 Inhibitors.Proteomic interrogation of HSP90 and insights for medical research.Adapting to stress - chaperome networks in cancer.HSP90 inhibitors disrupt a transient HSP90-HSF1 interaction and identify a noncanonical model of HSP90-mediated HSF1 regulation.Intrinsic proteotoxic stress levels vary and act as a predictive marker for sensitivity of cancer cells to Hsp90 inhibition Dual targeting of HSP70 does not induce the heat shock response and synergistically reduces cell viability in muscle invasive bladder cancer

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Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.

http://www.wikidata.org/entity/Q36465517

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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2012年學術文章

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2012年學術文章

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Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.

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Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.

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Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.

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Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.

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Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.

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Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.

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Current Molecular Medicine

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Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.

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A B Apolo

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G Giaccone

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J B Trepel

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L M Neckers

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M Mollapour

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M-J Lee

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S Lee

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S Tsutsumi

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S V Alarcon

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T Prince

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P2860

Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone

S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities

Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha.

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR

Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.

A ceRNA hypothesis: the Rosetta Stone of a hidden RNA language?

Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers

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