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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:

Cryo‐EM structure of the chain‐elongating E3 ubiquitin ligase UBR5
Zuzana Hodáková, Irina Grishkovskaya, Hanna L. Brunner, et al.
The EMBO Journal (2023) Vol. 42, Iss. 16
Open Access | Times Cited: 23

Showing 23 citing articles:

Structural snapshots along K48-linked ubiquitin chain formation by the HECT E3 UBR5
Laura A. Hehl, Daniel Horn‐Ghetko, J. Rajan Prabu, et al.
Nature Chemical Biology (2023) Vol. 20, Iss. 2, pp. 190-200
Open Access | Times Cited: 35
Orphan quality control shapes network dynamics and gene expression
Kevin G. Mark, SriDurgaDevi Kolla, Jacob D. Aguirre, et al.
Cell (2023) Vol. 186, Iss. 16, pp. 3460-3475.e23
Open Access | Times Cited: 33
Structural mechanisms of autoinhibition and substrate recognition by the ubiquitin ligase HACE1
Jonas Düring, M. Wolter, Julia J. Toplak, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 2, pp. 364-377
Open Access | Times Cited: 7
UBR5 in Tumor Biology: Exploring Mechanisms of Immune Regulation and Possible Therapeutic Implications in MPNST
Diana Odhiambo, Shuangyi Fan, Angela C. Hirbe
Cancers (2025) Vol. 17, Iss. 2, pp. 161-161
Open Access
Convergence of orphan quality control pathways at a ubiquitin chain-elongating ligase
Sara Carrillo Roas, Yuichi Yagita, Paul V. Murphy, et al.
Molecular Cell (2025)
Open Access
Revisiting the structure of UBR box from human UBR6
Bokyung Kim, Sang Hyun Lee, Bong Heon Kim, et al.
Protein Science (2025) Vol. 34, Iss. 4
Closed Access
The role of UBR5 in tumor proliferation and oncotherapy
Bin Hu, Shiyuan Chen
Gene (2024) Vol. 906, pp. 148258-148258
Closed Access | Times Cited: 3
Noncanonical assembly, neddylation and chimeric cullin–RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex
Daniel Horn‐Ghetko, Linus V. M. Hopf, Ishita Tripathi‐Giesgen, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 7, pp. 1083-1094
Open Access | Times Cited: 3
Harnessing UBR5 for targeted protein degradation of key transcriptional regulators
Asad M. Taherbhoy, Danette L. Daniels
Trends in Pharmacological Sciences (2023) Vol. 44, Iss. 11, pp. 758-761
Open Access | Times Cited: 9
The G1/S transition is promoted by Rb degradation via the E3 ligase UBR5
Shuyuan Zhang, Lucas Fuentes Valenzuela, Evgeny Zatulovskiy, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 5
A review: targeting UBR5 domains to mediate emerging roles and mechanisms: chance or necessity?
Yizhu Wang, Kaiyi Niu, Yanlong Shi, et al.
International Journal of Surgery (2024)
Open Access | Times Cited: 1
The G 1 -S transition is promoted by Rb degradation via the E3 ligase UBR5
Shuyuan Zhang, Lucas Fuentes Valenzuela, Evgeny Zatulovskiy, et al.
Science Advances (2024) Vol. 10, Iss. 43
Open Access | Times Cited: 1
Deciphering the RNA-binding protein network during endosomal mRNA transport
Senthil-Kumar Devan, Sainath Shanmugasundaram, Kira Müntjes, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 46
Open Access | Times Cited: 1
The molecular basis of integrated stress response silencing
Zhi Yang, Diane L. Haakonsen, Michael Heider, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Friend or foe? Reciprocal regulation between E3 ubiquitin ligases and deubiquitinases
Derek L. Bolhuis, Michael J. Emanuele, Nicholas G. Brown
Biochemical Society Transactions (2024) Vol. 52, Iss. 1, pp. 241-267
Open Access
Deciphering the RNA-binding protein network during endosomal mRNA transport
Senthil-Kumar Devan, Sainath Shanmugasundaram, Kira Müntjes, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Research advancements on the involvement of E3 ubiquitin ligase UBR5 in gastrointestinal cancers
Rong Qin, Xirui Fan, Rui Ding, et al.
Heliyon (2024) Vol. 10, Iss. 9, pp. e30284-e30284
Open Access
Guardian ubiquitin E3 ligases target cancer-associated APOBEC3 deaminases for degradation to promote human genome integrity
Irene Schwartz, Valentina Budroni, Mathilde Meyenberg, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
UBR-5 and UBE2D mediate timely exit from stem fate via destabilization of poly(A)-binding protein PABP-2 in cell state transition
J. F. Moreno, G. Abreu Jose, Yi M. Weaver, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 43
Open Access
A multivalent adaptor mechanism drives the nuclear import of proteasomes
Hanna L. Brunner, Robert Kalis, Lorenz Grundmann, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
To be (in a transcriptional complex) or not to be (promoting UBR5 ubiquitylation): That is an answer to how degradation controls gene expression
Laura A. Hehl, Brenda A. Schulman
Molecular Cell (2023) Vol. 83, Iss. 15, pp. 2616-2618
Open Access | Times Cited: 1
Structural mechanisms of autoinhibition and substrate recognition by the ubiquitin ligase HACE1
Jonas Duering, M. Wolter, Julia J. Toplak, et al.
Research Square (Research Square) (2023)
Open Access
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