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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:

The increasing complexity of the ubiquitin code
Richard G. Yau, Michael Rapé
Nature Cell Biology (2016) Vol. 18, Iss. 6, pp. 579-586
Closed Access | Times Cited: 923

Showing 1-25 of 923 citing articles:

PROTAC targeted protein degraders: the past is prologue
Miklós Békés, David R. Langley, Craig M. Crews
Nature Reviews Drug Discovery (2022) Vol. 21, Iss. 3, pp. 181-200
Open Access | Times Cited: 1824
Proteolysis-Targeting Chimeras as Therapeutics and Tools for Biological Discovery
George M. Burslem, Craig M. Crews
Cell (2020) Vol. 181, Iss. 1, pp. 102-114
Open Access | Times Cited: 776
The role of JAK-STAT signaling pathway and its regulators in the fate of T helper cells
Farhad Seif, Majid Khoshmirsafa, Hossein Aazami, et al.
Cell Communication and Signaling (2017) Vol. 15, Iss. 1
Open Access | Times Cited: 689
Breaking the chains: deubiquitylating enzyme specificity begets function
Michael J. Clague, Sylvie Urbé, David Komander
Nature Reviews Molecular Cell Biology (2019) Vol. 20, Iss. 6, pp. 338-352
Closed Access | Times Cited: 677
The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy
Yong Tae Kwon, Aaron Ciechanover
Trends in Biochemical Sciences (2017) Vol. 42, Iss. 11, pp. 873-886
Closed Access | Times Cited: 667
The role of ubiquitination in tumorigenesis and targeted drug discovery
Lu Deng, Tong Meng, Lei Chen, et al.
Signal Transduction and Targeted Therapy (2020) Vol. 5, Iss. 1
Open Access | Times Cited: 529
Ubiquitylation at the crossroads of development and disease
Michael Rapé
Nature Reviews Molecular Cell Biology (2017) Vol. 19, Iss. 1, pp. 59-70
Closed Access | Times Cited: 515
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: 467
Mechanism and inhibition of the papain‐like protease, PLpro, of SARS‐CoV‐2
Theresa Klemm, Gregor Ebert, Dale J. Calleja, et al.
The EMBO Journal (2020) Vol. 39, Iss. 18
Open Access | Times Cited: 436
Ubiquitin ligases in oncogenic transformation and cancer therapy
Daniela Senft, Jianfei Qi, Ze’ev A. Ronai
Nature reviews. Cancer (2017) Vol. 18, Iss. 2, pp. 69-88
Open Access | Times Cited: 402
Targeted Protein Degradation: from Chemical Biology to Drug Discovery
Philipp M. Cromm, Craig M. Crews
Cell chemical biology (2017) Vol. 24, Iss. 9, pp. 1181-1190
Open Access | Times Cited: 351
The Ubiquitin System, Autophagy, and Regulated Protein Degradation
Alexander Varshavsky
Annual Review of Biochemistry (2017) Vol. 86, Iss. 1, pp. 123-128
Closed Access | Times Cited: 351
A small-molecule inhibitor of the ubiquitin activating enzyme for cancer treatment
Marc L. Hyer, Michael A. Milhollen, J. Ciavarri, et al.
Nature Medicine (2018) Vol. 24, Iss. 2, pp. 186-193
Closed Access | Times Cited: 346
Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation
Ivo A. Hendriks, David Lyon, Clifford Young, et al.
Nature Structural & Molecular Biology (2017) Vol. 24, Iss. 3, pp. 325-336
Closed Access | Times Cited: 331
p62 filaments capture and present ubiquitinated cargos for autophagy
Gabriele Zaffagnini, Adriana Savova, Alberto Danieli, et al.
The EMBO Journal (2018) Vol. 37, Iss. 5
Open Access | Times Cited: 312
Principles of Ubiquitin-Dependent Signaling
Eugene Oh, David Akopian, Michael Rapé
Annual Review of Cell and Developmental Biology (2018) Vol. 34, Iss. 1, pp. 137-162
Closed Access | Times Cited: 295
Assembly and Function of Heterotypic Ubiquitin Chains in Cell-Cycle and Protein Quality Control
Richard G. Yau, Kerstin Doerner, Erick R. Castellanos, et al.
Cell (2017) Vol. 171, Iss. 4, pp. 918-933.e20
Open Access | Times Cited: 286
Collided ribosomes form a unique structural interface to induce Hel2‐driven quality control pathways
Ken Ikeuchi, Petr Těšina, Yoshitaka Matsuo, et al.
The EMBO Journal (2019) Vol. 38, Iss. 5
Open Access | Times Cited: 281
Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination
Sagar Bhogaraju, Sissy Kalayil, Yaobin Liu, et al.
Cell (2016) Vol. 167, Iss. 6, pp. 1636-1649.e13
Open Access | Times Cited: 279
Post-translational regulation of ubiquitin signaling
Lei Song, Zhao‐Qing Luo
The Journal of Cell Biology (2019) Vol. 218, Iss. 6, pp. 1776-1786
Open Access | Times Cited: 272
Crosstalk and Interplay between the Ubiquitin-Proteasome System and Autophagy
Chang Hoon Ji, Yong Tae Kwon
Molecules and Cells (2017) Vol. 40, Iss. 7, pp. 441-449
Open Access | Times Cited: 268
Small-Molecule Modulation of Protein Homeostasis
George M. Burslem, Craig M. Crews
Chemical Reviews (2017) Vol. 117, Iss. 17, pp. 11269-11301
Closed Access | Times Cited: 255
K63 ubiquitylation triggers proteasomal degradation by seeding branched ubiquitin chains
Fumiaki Ohtake, Hikaru Tsuchiya, Yasushi Saeki, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 7
Open Access | Times Cited: 255
Ubiquitin-mediated regulation of autophagy
Ruey‐Hwa Chen, Yu-Hsuan Chen, Tzu-Yu Huang
Journal of Biomedical Science (2019) Vol. 26, Iss. 1
Open Access | Times Cited: 254
Legionella and Coxiella effectors: strength in diversity and activity
Jiazhang Qiu, Zhao‐Qing Luo
Nature Reviews Microbiology (2017) Vol. 15, Iss. 10, pp. 591-605
Closed Access | Times Cited: 247
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