HSP90AB1: Helping the good and the bad
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HSP90AB1 is commonly overexpressed in a variety of cancers, and this upregulation is typically linked to poor prognostic outcomes and increased resistance to standard chemotherapy and radiotherapy.
“HSP90AB1 is commonly overexpressed in a variety of cancers, with this upregulation typically linked to poor prognostic outcomes and increased resistance to standard chemotherapy and radiotherapy treatments [12, 42, 43].”
From Celastrol attenuates the invasion and migration and augments the anticancer effects of olaparib in prostate cancer (2024) · cites this paper as [12]
The Cancer section reports HSP90AB1 upregulation in several cancers and links it to poor survival in lung cancer and poor prognosis in a breast-cancer subtype. It also describes radiation resistance in lung cancer cell lines and a possible resistance mechanism during valproic-acid treatment of AML, but does not establish that HSP90AB1 upregulation typically causes resistance to standard chemotherapy and radiotherapy across cancers. Page numbers are unavailable in our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measuredHSP90AB1 functions as a molecular chaperone that is pivotal in maintaining cellular proteostasis.
“HSP90AB1, a member of the HSP90 family, functions as a molecular chaperone that is pivotal in maintaining cellular proteostasis [12].”
From Celastrol attenuates the invasion and migration and augments the anticancer effects of olaparib in prostate cancer (2024) · cites this paper as [12]
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References 307 · Cited by 179
Research works printed but not linked: 1
- Senftleben U Karin M 2002 The IKK/NF-kappaB pathway Crit Care Med 30 S18 S26 11891403
- Authors
- Haase, M., & Fitze, G.
- Affiliations
- University Hospital Carl Gustav Carus (DE)
- Corresponding author
- Haase, Michael
- Venue
- Gene
- Publisher
- Elsevier BV
- Published
- 2016-01
- Volume
- 575
- Issue
- 2
- Pages
- 171-186
- ISSN
- 0378-1119 (ISSN-L)
- PMC
- PMC5675009
- OpenAlex
- W1431954835
- Cited by
- 179
- References
- 307
- Citations by year
- 2026: 18 · 2025: 37 · 2024: 27 · 2023: 14 · 2022: 21 · 2021: 20 · 2020: 11 · 2019: 16 · 2018: 9 · 2017: 4 · 2016: 1
- FWCI
- 0.45
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Gene (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (GM089820)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- HSP90AB1, HSP90β, HSP90AA1, heat shock proteins, molecular chaperones, client proteins, co-chaperones, protein folding, protein stability, cellular stress, kinases, ubiquitin ligase, transcription factors, tumor formation, tumor cell proliferation, cancer therapy targets
- MeSH terms
- Adenosine Triphosphatases, Animals, Cell Survival, Humans, Neoplasm Proteins, Neoplasms, Protein Folding, HSP90 Heat-Shock Proteins, Cell Proliferation
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