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Molecular Chaperones

  • Living reference work entry
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Encyclopedia of Cancer

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References

  • Butler LM, Ferraldeschi R, Armstrong H et al (2015) Maximizing the therapeutic potential of HSP90 inhibitors. Mol Can Res; 13(11):1445–51

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See Also

  • (2012) ATPase. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 302. doi:10.1007/978-3-642-16483-5_442

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  • (2012) Biomarkers. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, pp 408–409. doi:10.1007/978-3-642-16483-5_6601

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  • (2012) Chaperonins. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 754. doi:10.1007/978-3-642-16483-5_1047

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  • (2012) J-Domain. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 1926. doi:10.1007/978-3-642-16483-5_3176

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  • (2012) Kinase. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 1943. doi:10.1007/978-3-642-16483-5_3217

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  • (2012) Tetracopeptide repeat TPR domains. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 3660. doi:10.1007/978-3-642-16483-5_5743

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Author information

Authors and Affiliations

  1. Cancer Research UK Cancer Therapeutics Unit, The Institute of Cancer Research, Sutton, London, UK

    Marissa V. Powers & Paul Workman

Authors
  1. Marissa V. Powers
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  2. Paul Workman
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Corresponding author

Correspondence to Marissa V. Powers .

Editor information

Editors and Affiliations

  1. Abt. Tumorgenetik, Deutsches Krebsforschungszentrum, Heidelberg, Germany

    Manfred Schwab

Glossary

ATPase

Enzymes that use ATP hydrolysis to yield energy to drive an energetically unfavorable reaction.

Proteasome

A protein degradation complex which can digest a variety of proteins into short polypeptides and amino acids.

Ubiquitination

A posttranslational modification involving the attachment of ubiquitin molecules to specific lysine residues in target proteins. Often this modification acts as a tag for the rapid cellular degradation of the protein by the proteasome.

WD40 repeat

A poorly conserved motif consisting of a repeat sequence containing 40–60 amino acids, which usually contains a Trp-Asp (WD). Several consecutive repeats fold into a domain structure known as a β-propeller in which each section of the structure is a four-stranded β-sheet.

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Powers, M.V., Workman, P. (2015). Molecular Chaperones. In: Schwab, M. (eds) Encyclopedia of Cancer. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-27841-9_3810-2

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  • DOI: https://doi.org/10.1007/978-3-642-27841-9_3810-2

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  • Publisher Name: Springer, Berlin, Heidelberg

  • Online ISBN: 978-3-642-27841-9

  • eBook Packages: Springer Reference Biomedicine and Life SciencesReference Module Biomedical and Life Sciences

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