Control mechanisms of differential translation of Hsp90 isoforms in 9L rat gliosarcoma cells

No abstract is available for this paper.

• Publication year

  2009

• Venue

  Journal of Cellular Biochemistry

• Publication date

  2009-06-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1002/jcb.22138PMID 19308988
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Concerted actions of multiple transcription elements confer differential transactivation of HSP90 isoforms in geldanamycin‐treated 9L rat gliosarcoma cells

  2008cited by this paper
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• RACK1 Competes with HSP90 for Binding to HIF-1α and is Required for O2-independent and HSP90 Inhibitor-induced Degradation of HIF-1α

  2007cited by this paper
• RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha.

  2007cited by this paper
• Some thoughts about translational regulation: Forward and backward glances

  2007cited by this paper
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  2006cited by this paper
• Alternative mechanisms of initiating translation of mammalian mRNAs.

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• The HSP90 family of genes in the human genome: insights into their divergence and evolution.

  2005cited by this paper
• Transactivation of hsp70‐1/2 in geldanamycin‐treated human non‐small cell lung cancer H460 cells: Involvement of intracellular calcium and protein kinase C

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• Hsp90 isoforms: functions, expression and clinical importance

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• The 9L rat brain tumor: Description and application of an animal model

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• Translational Regulation of Hsp90 mRNA

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• Hsp90 Inhibition Accelerates Cell Lysis ANTI-Hsp90 RIBOZYME REVEALS A COMPLEX MECHANISM OF Hsp90 INHIBITORS INVOLVING BOTH SUPEROXIDE- AND Hsp90-DEPENDENT EVENTS*

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• Hsp90 Inhibition Accelerates Cell Lysis

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• Heat shock protein 90

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• Regulation of Signaling Protein Function and Trafficking by the hsp90/hsp70-Based Chaperone Machinery 1

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• Heat-shock protein 90, a chaperone for folding and regulation

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• Involvement of human heat shock protein 90α in nicotine‐induced apoptosis

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• Emerging links between initiation of translation and human diseases

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• Structure, function, and mechanism of the Hsp90 molecular chaperone.

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