For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
21
views
26
references
 Top references
cited by
11
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      119
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      HSP90 as a novel molecular target in non-small-cell lung cancer

      review-article

      Read this article at

      ScienceOpenPublisherPMC
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Lung cancer remains the most lethal cancer, with over 160,000 annual deaths in the USA alone. Over the past decade, the discovery of driver mutations has changed the landscape for the treatment of non-small-cell lung cancer (NSCLC). Targeted therapies against epidermal growth factor receptor (EGFR) or anaplastic lymphoma kinase (ALK) have now been approved by the Food and Drug Administration as part of the standard first-line treatment of NSCLC. Despite good initial responses, most patients develop resistance within 8–12 months and have disease progression.

          Related collections

          Most cited references26

          • Record: found
          • Abstract: found
          • Article: not found

          Heat shock proteins in cancer: chaperones of tumorigenesis.

          Stuart K. Calderwood, Md Khaleque, Douglas B. Sawyer … (2006)
          The heat shock proteins (HSPs) induced by cell stress are expressed at high levels in a wide range of tumors and are closely associated with a poor prognosis and resistance to therapy. The increased transcription of HSPs in tumor cells is due to loss of p53 function and to higher expression of the proto-oncogenes HER2 and c-Myc, and is crucial to tumorigenesis. The HSP family members play overlapping, essential roles in tumor growth both by promoting autonomous cell proliferation and by inhibiting death pathways. The HSPs have thus become targets for rational anti-cancer drug design: HSP90 inhibitors are currently showing much promise in clinical trials, whereas the increased expression of HSPs in tumors is forming the basis of chaperone-based immunotherapy.
          Article 0 comments Cited 271 times – based on 0 reviews     Review now
            • Record: found
            • Abstract: found
            • Article: not found

            Inhibition of HSP90 molecular chaperones: moving into the clinic.

            Rocio Garcia-Carbonero, Amancio Carnero, Luis Paz-Ares (2013)
            Heat shock protein 90 (HSP90) is a molecular chaperone that is crucial for the stability and function of many proteins essential for cell survival. Many oncogenes, including tyrosine kinases, transcription factors, and cell-cycle regulatory proteins, are client proteins of HSP90. Inhibition of HSP90 causes client protein degradation via the ubiquitin-proteasome pathway, and is a mechanism that might simultaneously downregulate several redundant pathways crucial for cell viability and tumour development. HSP90 inhibitors are currently being developed as anticancer agents, and have shown early promising results in molecularly defined subgroups of solid tumours (eg, ALK-rearranged non-small-cell lung cancer and HER2-amplified breast cancer) and some haematological malignancies (eg, multiple myeloma). Here, we review the current status of HSP90 inhibitors in clinical development, including geldanamycin derivatives, resorcinol derivatives, purine analogues, and other synthetic inhibitors. We also discuss novel strategies and future perspectives on how to optimise the therapeutic potential of this exciting new class of drugs. Copyright © 2013 Elsevier Ltd. All rights reserved.
            Article 0 comments Cited 137 times – based on 0 reviews     Review now
              • Record: found
              • Abstract: found
              • Article: not found

              Targeting HSP90 for cancer therapy

              D Mahalingam, R Swords, J S Carew … (2009)
              Heat-shock proteins (HSPs) are molecular chaperones that regulate protein folding to ensure correct conformation and translocation and to avoid protein aggregation. Heat-shock proteins are increased in many solid tumours and haematological malignancies. Many oncogenic proteins responsible for the transformation of cells to cancerous forms are client proteins of HSP90. Targeting HSP90 with chemical inhibitors would degrade these oncogenic proteins, and thus serve as useful anticancer agents. This review provides an overview of the HSP chaperone machinery and the structure and function of HSP90. We also highlight the key oncogenic proteins that are regulated by HSP90 and describe how inhibition of HSP90 could alter the activity of multiple signalling proteins, receptors and transcriptional factors implicated in carcinogenesis.
              Article 0 comments Cited 84 times – based on 0 reviews     Review now
                All references

                Author and article information

                Journal
                Journal ID (nlm-ta): Lung Cancer (Auckl)
                Journal ID (iso-abbrev): Lung Cancer (Auckl)
                Journal ID (publisher-id): Lung Cancer: Targets and Therapy
                Title: Lung Cancer: Targets and Therapy
                Publisher: Dove Medical Press
                ISSN (Electronic): 1179-2728
                Publication date Collection: 2016
                Publication date (Electronic): 01 March 2016
                Volume: 7
                Pages: 11-17
                Affiliations
                Segal Cancer Center, Jewish General Hospital, McGill University, Montreal, QC, Canada
                Author notes
                Correspondence: Victor Cohen, Segal Cancer Center, Jewish General Hospital, McGill University, 3755 Chemin de la Côte-Sainte-Catherine, Montreal, QC, H3T 1E2, Canada, Email vcohen@ 123456jgh.mcgill.ca
                Article
                Publisher ID: lctt-7-011
                DOI: 10.2147/LCTT.S60344
                PMC ID: 5310695
                PubMed ID: 28210156
                SO-VID: 104a6bcd-1d5c-4c5f-af40-b05e44ce1552
                Copyright © © 2016 Esfahani and Cohen. This work is published and licensed by Dove Medical Press Limited
                License:

                The full terms of this license are available at https://www.dovepress.com/terms.php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License ( http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed.

                History
                Categories
                Subject: Review

                Keywords: non-small-cell lung cancer,driver mutations,targeted therapy,heat shock protein 90 (hsp90)
                Data availability:
                Keywords: non-small-cell lung cancer, driver mutations, targeted therapy, heat shock protein 90 (hsp90)

                Comments

                Comment on this article

                Related Documents Log
                scite_

                Similar content119

                See all similar

                Cited by11

                See all cited by

                Most referenced authors574

                See all reference authors