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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:

Structural and Functional Insights to Ubiquitin-Like Protein Conjugation
Frederick C. Streich, Christopher D. Lima
Annual Review of Biophysics (2014) Vol. 43, Iss. 1, pp. 357-379
Open Access | Times Cited: 147

Showing 1-25 of 147 citing articles:

Ubiquitin modifications
Kirby N. Swatek, David Komander
Cell Research (2016) Vol. 26, Iss. 4, pp. 399-422
Open Access | Times Cited: 1676
Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism
Laurent Cappadocia, Christopher D. Lima
Chemical Reviews (2017) Vol. 118, Iss. 3, pp. 889-918
Open Access | Times Cited: 468
Drugging the undruggables: exploring the ubiquitin system for drug development
Xiaodong Huang, Vishva M. Dixit
Cell Research (2016) Vol. 26, Iss. 4, pp. 484-498
Open Access | Times Cited: 399
The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery
Elena Papaleo, Giorgio Saladino, Matteo Lambrughi, et al.
Chemical Reviews (2016) Vol. 116, Iss. 11, pp. 6391-6423
Open Access | Times Cited: 376
The demographics of the ubiquitin system
Michael J. Clague, Claire Heride, Sylvie Urbé
Trends in Cell Biology (2015) Vol. 25, Iss. 7, pp. 417-426
Closed Access | Times Cited: 324
E3 ubiquitin ligases: styles, structures and functions
Quan Yang, Jinyao Zhao, Dan Chen, et al.
Molecular Biomedicine (2021) Vol. 2, Iss. 1
Open Access | Times Cited: 220
Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
Daniel C. Scott, David Y. Rhee, David M. Duda, et al.
Cell (2016) Vol. 166, Iss. 5, pp. 1198-1214.e24
Open Access | Times Cited: 202
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
Molecular basis of resistance to proteasome inhibitors in hematological malignancies
Denise Niewerth, Gerrit Jansen, Yehuda G. Assaraf, et al.
Drug Resistance Updates (2014) Vol. 18, pp. 18-35
Closed Access | Times Cited: 169
Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C
Nicholas G. Brown, Ryan T. VanderLinden, Edmond R. Watson, et al.
Cell (2016) Vol. 165, Iss. 6, pp. 1440-1453
Open Access | Times Cited: 149
SUMOylation: re-wiring the plant nucleus during stress and development
Robert C. Augustine, Richard D. Vierstra
Current Opinion in Plant Biology (2018) Vol. 45, pp. 143-154
Open Access | Times Cited: 142
p62-mediated phase separation at the intersection of the ubiquitin-proteasome system and autophagy
Alberto Danieli, Sascha Martens
Journal of Cell Science (2018) Vol. 131, Iss. 19
Open Access | Times Cited: 129
Positioning of proteasome inhibitors in therapy of solid malignancies
Margot S. F. Roeten, Jacqueline Cloos, Gerrit Jansen
Cancer Chemotherapy and Pharmacology (2017) Vol. 81, Iss. 2, pp. 227-243
Open Access | Times Cited: 128
Degrons in cancer
Bálint Mészáros, Manjeet Kumar, Toby J. Gibson, et al.
Science Signaling (2017) Vol. 10, Iss. 470
Open Access | Times Cited: 124
Layers of DUB regulation
Danny D. Sahtoe, Titia K. Sixma
Trends in Biochemical Sciences (2015) Vol. 40, Iss. 8, pp. 456-467
Closed Access | Times Cited: 120
Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase
Laurent Cappadocia, Andrea Pichler, Christopher D. Lima
Nature Structural & Molecular Biology (2015) Vol. 22, Iss. 12, pp. 968-975
Open Access | Times Cited: 119
Emerging Paradigm of Crosstalk between Autophagy and the Ubiquitin-Proteasome System.
Taewook Nam, Jong Hyun Han, Sushil Devkota, et al.
PubMed (2017) Vol. 40, Iss. 12, pp. 897-905
Closed Access | Times Cited: 104
Capturing a substrate in an activated RING E3/E2–SUMO complex
Frederick C. Streich, Christopher D. Lima
Nature (2016) Vol. 536, Iss. 7616, pp. 304-308
Open Access | Times Cited: 99
Resistance to proteasome inhibitors and other targeted therapies in myeloma
Craig T. Wallington‐Beddoe, Magdalena Sobieraj‐Teague, Bryone J. Kuss, et al.
British Journal of Haematology (2018) Vol. 182, Iss. 1, pp. 11-28
Open Access | Times Cited: 99
The ubiquitin‐conjugating enzyme UBE 2 QL 1 coordinates lysophagy in response to endolysosomal damage
Lisa Koerver, Chrisovalantis Papadopoulos, Bin Liu, et al.
EMBO Reports (2019) Vol. 20, Iss. 10
Open Access | Times Cited: 94
Delineating Crosstalk Mechanisms of the Ubiquitin Proteasome System That Regulate Apoptosis
Ishita Gupta, Kanika Singh, N. Varshney, et al.
Frontiers in Cell and Developmental Biology (2018) Vol. 6
Open Access | Times Cited: 87
E1 Enzymes as Therapeutic Targets in Cancer
Samir H. Barghout, Aaron D. Schimmer
Pharmacological Reviews (2020) Vol. 73, Iss. 1, pp. 1-56
Open Access | Times Cited: 81
Proteotoxic stress and the ubiquitin proteasome system
Rachel Kandel, Jasmine Jung, Sonya E. Neal
Seminars in Cell and Developmental Biology (2023) Vol. 156, pp. 107-120
Open Access | Times Cited: 36
Development and crystal structures of a potent second-generation dual degrader of BCL-2 and BCL-xL
Digant Nayak, Dongwen Lv, Yaxia Yuan, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 12
Mechanism and disease association of E2-conjugating enzymes: lessons from UBE2T and UBE2L3
Arno F. Alpi, Viduth K. Chaugule, Helen Walden
Biochemical Journal (2016) Vol. 473, Iss. 20, pp. 3401-3419
Open Access | Times Cited: 73
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