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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:

Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding
Edward C. Twomey, Zhejian Ji, Thomas E. Wales, et al.
Science (2019) Vol. 365, Iss. 6452
Open Access | Times Cited: 268

Showing 1-25 of 268 citing articles:

Protein quality control in the secretory pathway
Zhihao Sun, Jeffrey L. Brodsky
The Journal of Cell Biology (2019) Vol. 218, Iss. 10, pp. 3171-3187
Open Access | Times Cited: 330
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
The molecular principles governing the activity and functional diversity of AAA+ proteins
Cristina Puchades, Colby R. Sandate, Gabriel C. Lander
Nature Reviews Molecular Cell Biology (2019) Vol. 21, Iss. 1, pp. 43-58
Open Access | Times Cited: 221
The Overlapping Genetics of Amyotrophic Lateral Sclerosis and Frontotemporal Dementia
Yevgeniya Abramzon, Pietro Fratta, Bryan J. Traynor, et al.
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 202
The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag
Indrajit Sahu, Sachitanand M. Mali, Prasad Sulkshane, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 109
Order through destruction: how ER‐associated protein degradation contributes to organelle homeostasis
John C. Christianson, Pedro Carvalho
The EMBO Journal (2022) Vol. 41, Iss. 6
Open Access | Times Cited: 94
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
The AAA+ chaperone VCP disaggregates Tau fibrils and generates aggregate seeds in a cellular system
Itika Saha, Patricia Yuste‐Checa, Miguel da Silva Padilha, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 47
Cellular functions and molecular mechanisms of non-lysine ubiquitination
Amie J. McClellan, Sophie Heiden Laugesen, Lars Ellgaard
Open Biology (2019) Vol. 9, Iss. 9, pp. 190147-190147
Open Access | Times Cited: 138
Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate
Fei X, Tristan A. Bell, Simon Jenni, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 134
Autosomal dominant VCP hypomorph mutation impairs disaggregation of PHF-tau
Nabil F. Darwich, Jessica M. Phan, Boram Kim, et al.
Science (2020) Vol. 370, Iss. 6519
Open Access | Times Cited: 114
Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP‐dependent substrate translocation
Stephanie N. Gates, Andreas Martin
Protein Science (2019) Vol. 29, Iss. 2, pp. 407-419
Open Access | Times Cited: 113
Structure, Dynamics and Function of the 26S Proteasome
Youdong Mao
Sub-cellular biochemistry/Subcellular biochemistry (2020), pp. 1-151
Open Access | Times Cited: 95
Maintenance of organellar protein homeostasis by ER-associated degradation and related mechanisms
Marius K. Lemberg, Kvido Střı́šovský
Molecular Cell (2021) Vol. 81, Iss. 12, pp. 2507-2519
Open Access | Times Cited: 90
The AAA+ superfamily: a review of the structural and mechanistic principles of these molecular machines
Yousuf A. Khan, K. Ian White, Axel T. Brünger
Critical Reviews in Biochemistry and Molecular Biology (2021) Vol. 57, Iss. 2, pp. 156-187
Open Access | Times Cited: 87
Mechanism of membrane-curvature generation by ER-tubule shaping proteins
Ning Wang, Lindsay Clark, Yuan Gao, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 75
TRIP12 promotes small-molecule-induced degradation through K29/K48-branched ubiquitin chains
Ai Kaiho-Soma, Yoshino Akizuki, Katsuhide Igarashi, et al.
Molecular Cell (2021) Vol. 81, Iss. 7, pp. 1411-1424.e7
Open Access | Times Cited: 75
Mechanistic insight into substrate processing and allosteric inhibition of human p97
Man Pan, Yuanyuan Yu, Huasong Ai, et al.
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 7, pp. 614-625
Open Access | Times Cited: 75
Hrd1 forms the retrotranslocation pore regulated by auto-ubiquitination and binding of misfolded proteins
Vedran Vasic, Niels Denkert, Claudia Schmidt, et al.
Nature Cell Biology (2020) Vol. 22, Iss. 3, pp. 274-281
Open Access | Times Cited: 72
Seesaw conformations of Npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative
Man Pan, Qingyun Zheng, Yuanyuan Yu, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 72
Assembly and function of branched ubiquitin chains
SriDurgaDevi Kolla, Mengchen Ye, Kevin G. Mark, et al.
Trends in Biochemical Sciences (2022) Vol. 47, Iss. 9, pp. 759-771
Open Access | Times Cited: 63
Structures of the human LONP1 protease reveal regulatory steps involved in protease activation
Mia Shin, Edmond R. Watson, Albert S. Song, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 59
Translocation of polyubiquitinated protein substrates by the hexameric Cdc48 ATPase
Zhejian Ji, Hao Li, Daniele Peterle, et al.
Molecular Cell (2021) Vol. 82, Iss. 3, pp. 570-584.e8
Open Access | Times Cited: 57
The CDC48 complex mediates ubiquitin-dependent degradation of intra-chloroplast proteins in plants
Jialong Li, Jiarui Yuan, Yuhong Li, et al.
Cell Reports (2022) Vol. 39, Iss. 2, pp. 110664-110664
Open Access | Times Cited: 52
Inhibitors of the ATPase p97/VCP: From basic research to clinical applications
Susan Kilgas, Kristijan Ramadan
Cell chemical biology (2023) Vol. 30, Iss. 1, pp. 3-21
Open Access | Times Cited: 32
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