Skip to main content
SpringerLink
Log in

Molecular Chaperones

  • Reference work entry
  • First Online:
Book cover Encyclopedia of Cancer

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 2,499.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Hardcover Book
USD 3,999.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

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

    Google Scholar 

  • Kim YE, Hipp MS, Bracher A et al (2013) Molecular chaperone functions in protein folding and proteostasis. Annu Rev Biochem 82:323–355

    Article  CAS  PubMed  Google Scholar 

  • Lopez T, Dalton K, Frydman J (2015) The mechanism and function of group II chaperonins. J Mol Biol.11; 427(18): 2919–30

    Google Scholar 

  • Neckers L, Workman P (2012) HSP90 molecular chaperone inhibitors: are we there yet? Clin Cancer Res 18(1):64–76

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Powers MV, Jones K, Barillari C et al (2010) Targeting HSP70: the second potentially druggable heat shock protein and molecular chaperone? Cell Cycle 9(8):1542–1550

    Article  CAS  PubMed  Google Scholar 

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

    Google Scholar 

  • (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

    Google Scholar 

  • (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

    Google Scholar 

  • (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

    Google Scholar 

  • (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

    Google Scholar 

  • (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

    Google Scholar 

Download references

Author information

Authors and Affiliations

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

    Marissa V. Powers

  2. Cancer Research UK Center for Cancer Therapeutics, The Institute of Cancer Research, Sutton, Surrey, UK

    Paul Workman

Authors
  1. Marissa V. Powers
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Paul Workman
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Marissa V. Powers .

Editor information

Editors and Affiliations

  1. German Cancer Research Center (DKFZ), Tumorgenetik, 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.

Rights and permissions

Reprints and permissions

Copyright information

© 2015 Springer-Verlag Berlin Heidelberg

About this entry

Cite this entry

Powers, M.V., Workman, P. (2015). Molecular Chaperones. In: Schwab, M. (eds) Encyclopedia of Cancer. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-46875-3_3810

Download citation

Publish with us

Policies and ethics

Search

Navigation