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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 and Function of the 26S Proteasome
Jared A.M. Bard, Ellen A. Goodall, Eric R. Greene, et al.
Annual Review of Biochemistry (2018) Vol. 87, Iss. 1, pp. 697-724
Open Access | Times Cited: 677

Showing 1-25 of 677 citing articles:

N-degron and C-degron pathways of protein degradation
Alexander Varshavsky
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 2, pp. 358-366
Open Access | Times Cited: 480
A guide to antigen processing and presentation
Novalia Pishesha, Thibault J. Harmand, Hidde L. Ploegh
Nature reviews. Immunology (2022) Vol. 22, Iss. 12, pp. 751-764
Closed Access | Times Cited: 435
Advancing targeted protein degradation for cancer therapy
Brandon Dale, Meng Cheng, Kwang‐Su Park, et al.
Nature reviews. Cancer (2021) Vol. 21, Iss. 10, pp. 638-654
Open Access | Times Cited: 433
High-Resolution Native Mass Spectrometry
Sem Tamara, Maurits A. den Boer, Albert J. R. Heck
Chemical Reviews (2021) Vol. 122, Iss. 8, pp. 7269-7326
Open Access | Times Cited: 336
Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome
Yuanchen Dong, Shuwen Zhang, Zhaolong Wu, et al.
Nature (2018) Vol. 565, Iss. 7737, pp. 49-55
Open Access | Times Cited: 298
Substrate-engaged 26S proteasome structures reveal mechanisms for ATP-hydrolysis–driven translocation
Andres H. de la Peña, Ellen A. Goodall, Stephanie N. Gates, et al.
Science (2018) Vol. 362, Iss. 6418
Open Access | Times Cited: 282
Ubiquitin signalling in neurodegeneration: mechanisms and therapeutic opportunities
Marlene F. Schmidt, Zhong Yan Gan, David Komander, et al.
Cell Death and Differentiation (2021) Vol. 28, Iss. 2, pp. 570-590
Open Access | Times Cited: 282
The immunoproteasome and thymoproteasome: functions, evolution and human disease
Shigeo Murata, Yousuke Takahama, Masanori Kasahara, et al.
Nature Immunology (2018) Vol. 19, Iss. 9, pp. 923-931
Closed Access | Times Cited: 260
An expanded lexicon for the ubiquitin code
Ivan Đikić, Brenda A. Schulman
Nature Reviews Molecular Cell Biology (2022) Vol. 24, Iss. 4, pp. 273-287
Open Access | Times Cited: 225
Deubiquitinases: From mechanisms to their inhibition by small molecules
Sven M. Lange, Lee A. Armstrong, Yogesh Kulathu
Molecular Cell (2021) Vol. 82, Iss. 1, pp. 15-29
Open Access | Times Cited: 190
Proteolysis-targeting chimeras (PROTACs) in cancer therapy
Xinyi Li, Wenchen Pu, Qingquan Zheng, et al.
Molecular Cancer (2022) Vol. 21, Iss. 1
Open Access | Times Cited: 188
Harnessing the Power of Proteolysis for Targeted Protein Inactivation
Rati Verma, Dane Mohl, Raymond J. Deshaies
Molecular Cell (2020) Vol. 77, Iss. 3, pp. 446-460
Open Access | Times Cited: 171
The Ubiquitin–Proteasome System in Immune Cells
Gonca Çetin, Sandro Klafack, Maja Studencka‐Turski, et al.
Biomolecules (2021) Vol. 11, Iss. 1, pp. 60-60
Open Access | Times Cited: 118
Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies
Jakub Šinský, Karoline Pichlerová, Jozef Hanes
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 17, pp. 9207-9207
Open Access | Times Cited: 113
Mechanisms of substrate processing during ER-associated protein degradation
John C. Christianson, Ernst Jarosch, Thomas Sommer
Nature Reviews Molecular Cell Biology (2023) Vol. 24, Iss. 11, pp. 777-796
Closed Access | Times Cited: 80
Disorders of ubiquitylation: unchained inflammation
David B. Beck, Achim Werner, Daniel L. Kastner, et al.
Nature Reviews Rheumatology (2022) Vol. 18, Iss. 8, pp. 435-447
Open Access | Times Cited: 76
Reduced secretion of LCN2 (lipocalin 2) from reactive astrocytes through autophagic and proteasomal regulation alleviates inflammatory stress and neuronal damage
Byung-Kwon Jung, Yujin Park, Boran Yoon, et al.
Autophagy (2023) Vol. 19, Iss. 8, pp. 2296-2317
Closed Access | Times Cited: 43
Journey of PROTAC: From Bench to Clinical Trial and Beyond
Kyli Berkley, Julian Zalejski, Nidhi Sharma, et al.
Biochemistry (2025)
Closed Access | Times Cited: 3
The proteasome 19S cap and its ubiquitin receptors provide a versatile recognition platform for substrates
Kirby Martinez‐Fonts, Caroline Davis, Takuya Tomita, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 136
The 26S Proteasome Utilizes a Kinetic Gateway to Prioritize Substrate Degradation
Jared A.M. Bard, Charlene Bashore, Ken C. Dong, et al.
Cell (2019) Vol. 177, Iss. 2, pp. 286-298.e15
Open Access | Times Cited: 128
The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome
Michal M. Olszewski, Cameron B. Williams, Ken C. Dong, et al.
Communications Biology (2019) Vol. 2, Iss. 1
Open Access | Times Cited: 122
Chaperoning Endoplasmic Reticulum–Associated Degradation (ERAD) and Protein Conformational Diseases
Patrick G. Needham, Christopher J. Guerriero, Jeffrey L. Brodsky
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 8, pp. a033928-a033928
Open Access | Times Cited: 122
Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating
Markus R. Eisele, Randi G. Reed, Till Rudack, et al.
Cell Reports (2018) Vol. 24, Iss. 5, pp. 1301-1315.e5
Open Access | Times Cited: 120
An orphan protein of Fusarium graminearum modulates host immunity by mediating proteasomal degradation of TaSnRK1α
Cong Jiang, Ruonan Hei, Yang Yang, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 117
A conserved SUMO pathway repairs topoisomerase DNA-protein cross-links by engaging ubiquitin-mediated proteasomal degradation
Yilun Sun, Lisa M. Jenkins, Yijun Su, et al.
Science Advances (2020) Vol. 6, Iss. 46
Open Access | Times Cited: 111
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