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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Structure, Function, and Regulation of the Hsp90 Machinery
Maximilian M. Biebl, Johannes Büchner
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 9, pp. a034017-a034017
Open Access | Times Cited: 251

Showing 1-25 of 251 citing articles:

Post-translational modifications of Hsp90 and translating the chaperone code
Sarah J. Backe, Rebecca Sager, Mark R. Woodford, et al.
Journal of Biological Chemistry (2020) Vol. 295, Iss. 32, pp. 11099-11117
Open Access | Times Cited: 163
Structural and functional complexity of HSP90 in cellular homeostasis and disease
Gabriela Chiosis, Chander Singh Digwal, Jane B. Trepel, et al.
Nature Reviews Molecular Cell Biology (2023) Vol. 24, Iss. 11, pp. 797-815
Open Access | Times Cited: 77
Heat shock protein 90: biological functions, diseases, and therapeutic targets
Huiyun Wei, Yingying Zhang, Yilin Jia, et al.
MedComm (2024) Vol. 5, Iss. 2
Open Access | Times Cited: 27
Protein Phase Separation as a Stress Survival Strategy
Titus M. Franzmann, Simon Alberti
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 6, pp. a034058-a034058
Open Access | Times Cited: 145
The functions and regulation of heat shock proteins; key orchestrators of proteostasis and the heat shock response
Benjamin Lang, Martín Guerrero, Thomas L. Prince, et al.
Archives of Toxicology (2021) Vol. 95, Iss. 6, pp. 1943-1970
Closed Access | Times Cited: 96
Cell-Nonautonomous Regulation of Proteostasis in Aging and Disease
Richard I. Morimoto
Cold Spring Harbor Perspectives in Biology (2019) Vol. 12, Iss. 4, pp. a034074-a034074
Open Access | Times Cited: 84
Modulation of Amyloid States by Molecular Chaperones
Anne S. Wentink, Carmen Nussbaum‐Krammer, Bernd Bukau
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 7, pp. a033969-a033969
Open Access | Times Cited: 79
The landscape of molecular chaperones across human tissues reveals a layered architecture of core and variable chaperones
Netta Shemesh, Juman Jubran, Shiran Dror, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 79
Molecular Chaperones: A Double-Edged Sword in Neurodegenerative Diseases
Jessica Tittelmeier, Eliana Nachman, Carmen Nussbaum‐Krammer
Frontiers in Aging Neuroscience (2020) Vol. 12
Open Access | Times Cited: 78
Hsf1 on a leash – controlling the heat shock response by chaperone titration
Anna E. Masser, Michela Ciccarelli, Claes Andréasson
Experimental Cell Research (2020) Vol. 396, Iss. 1, pp. 112246-112246
Open Access | Times Cited: 71
HSP90 mediates the connection of multiple programmed cell death in diseases
Caiwang Peng, Fengyan Zhao, Hengli Li, et al.
Cell Death and Disease (2022) Vol. 13, Iss. 11
Open Access | Times Cited: 64
Progesterone as an Anti-Inflammatory Drug and Immunomodulator: New Aspects in Hormonal Regulation of the Inflammation
Т. А. Федотчева, Н. И. Федотчева, Nikolai L. Shimanovsky
Biomolecules (2022) Vol. 12, Iss. 9, pp. 1299-1299
Open Access | Times Cited: 63
The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state
Kanghyun Lee, Aye C. Thwin, Cory M. Nadel, et al.
Molecular Cell (2021) Vol. 81, Iss. 17, pp. 3496-3508.e5
Open Access | Times Cited: 60
Hsp90‐mediated regulation of DYRK3 couples stress granule disassembly and growth via mTORC1 signaling
Laura Mediani, Francesco Antoniani, Veronica Galli, et al.
EMBO Reports (2021) Vol. 22, Iss. 5
Open Access | Times Cited: 59
Targeting the HSP90–CDC37–kinase chaperone cycle: A promising therapeutic strategy for cancer
Lei Wang, Qiuyue Zhang, Qidong You
Medicinal Research Reviews (2021) Vol. 42, Iss. 1, pp. 156-182
Closed Access | Times Cited: 56
Cytosolic Hsp90 Isoform-Specific Functions and Clinical Significance
Samarpan Maiti, Didier Picard
Biomolecules (2022) Vol. 12, Iss. 9, pp. 1166-1166
Open Access | Times Cited: 47
LncRNA NNT-AS1/hsa-miR-485–5p/HSP90 axis in-silico and clinical prospect correlated-to histologic grades-based CRC stratification: A step toward ncRNA Precision
Nada M. El-Sheikh, Ahmed I. Abulsoud, Amal Fawzy, et al.
Pathology - Research and Practice (2023) Vol. 247, pp. 154570-154570
Closed Access | Times Cited: 41
Small molecules targeting protein–protein interactions for cancer therapy
Defa Wu, Yang Li, Lang Zheng, et al.
Acta Pharmaceutica Sinica B (2023) Vol. 13, Iss. 10, pp. 4060-4088
Open Access | Times Cited: 33
Hippocampal HDAC6 promotes POCD by regulating NLRP3-induced microglia pyroptosis via HSP90/HSP70 in aged mice
Qi-Cheng Lin, Jiao Wang, Xinlin Wang, et al.
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2024) Vol. 1870, Iss. 5, pp. 167137-167137
Open Access | Times Cited: 10
Structural transitions modulate the chaperone activities of Grp94
Yaa S. Amankwah, Yasmeen Fleifil, Erin Unruh, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 12
Closed Access | Times Cited: 8
Advances in the structures, mechanisms and targeting of molecular chaperones
Jinying Gu, Yanyi He, Chenxi He, et al.
Signal Transduction and Targeted Therapy (2025) Vol. 10, Iss. 1
Open Access | Times Cited: 1
The Hsp70–Hsp90 go-between Hop/Stip1/Sti1 is a proteostatic switch and may be a drug target in cancer and neurodegeneration
Kaushik Bhattacharya, Didier Picard
Cellular and Molecular Life Sciences (2021) Vol. 78, Iss. 23, pp. 7257-7273
Open Access | Times Cited: 49
Protein kinase C fusion proteins are paradoxically loss of function in cancer
An‐Angela N. Van, Maya T. Kunkel, Timothy R. Baffi, et al.
Journal of Biological Chemistry (2021) Vol. 296, pp. 100445-100445
Open Access | Times Cited: 41
Advances towards Understanding the Mechanism of Action of the Hsp90 Complex
Chrisostomos Prodromou, Dennis M. Bjorklund
Biomolecules (2022) Vol. 12, Iss. 5, pp. 600-600
Open Access | Times Cited: 36
NudC guides client transfer between the Hsp40/70 and Hsp90 chaperone systems
Maximilian M. Biebl, Florent Delhommel, Ofrah Faust, et al.
Molecular Cell (2022) Vol. 82, Iss. 3, pp. 555-569.e7
Open Access | Times Cited: 32
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