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Targeting protein quality control pathways in breast cancer

Overview of attention for article published in BMC Biology, November 2017
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Title
Targeting protein quality control pathways in breast cancer
Published in
BMC Biology, November 2017
DOI 10.1186/s12915-017-0449-4
Pubmed ID
Authors

Sara Sannino, Jeffrey L. Brodsky

Abstract

The efficient production, folding, and secretion of proteins is critical for cancer cell survival. However, cancer cells thrive under stress conditions that damage proteins, so many cancer cells overexpress molecular chaperones that facilitate protein folding and target misfolded proteins for degradation via the ubiquitin-proteasome or autophagy pathway. Stress response pathway induction is also important for cancer cell survival. Indeed, validated targets for anti-cancer treatments include molecular chaperones, components of the unfolded protein response, the ubiquitin-proteasome system, and autophagy. We will focus on links between breast cancer and these processes, as well as the development of drug resistance, relapse, and treatment.

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The data shown below were collected from the profiles of 25 X users who shared this research output. Click here to find out more about how the information was compiled.
Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 61 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 61 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 12 20%
Student > Bachelor 9 15%
Student > Ph. D. Student 7 11%
Student > Master 5 8%
Student > Doctoral Student 4 7%
Other 9 15%
Unknown 15 25%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 25 41%
Medicine and Dentistry 5 8%
Agricultural and Biological Sciences 4 7%
Pharmacology, Toxicology and Pharmaceutical Science 3 5%
Immunology and Microbiology 3 5%
Other 4 7%
Unknown 17 28%