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 Eukaryotic Proteome Is Shaped by E3 Ubiquitin Ligases Targeting C-Terminal Degrons
Itay Koren, Richard T. Timms, Tomasz Kula, et al.
Cell (2018) Vol. 173, Iss. 7, pp. 1622-1635.e14
Open Access | Times Cited: 267

Showing 1-25 of 267 citing articles:

Targeted protein degradation: expanding the toolbox
Matthieu Schapira, Matthew F. Calabrese, Alex N. Bullock, et al.
Nature Reviews Drug Discovery (2019) Vol. 18, Iss. 12, pp. 949-963
Closed Access | Times Cited: 718

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

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

Targeted protein degradation: elements of PROTAC design
Stacey-Lynn Paiva, Craig M. Crews
Current Opinion in Chemical Biology (2019) Vol. 50, pp. 111-119
Open Access | Times Cited: 478

T-Scan: A Genome-wide Method for the Systematic Discovery of T Cell Epitopes
Tomasz Kula, M Dezfulian, Charlotte I. Wang, et al.
Cell (2019) Vol. 178, Iss. 4, pp. 1016-1028.e13
Open Access | Times Cited: 202

A glycine-specific N-degron pathway mediates the quality control of protein N -myristoylation
Richard T. Timms, Zhiqian Zhang, David Y. Rhee, et al.
Science (2019) Vol. 365, Iss. 6448
Open Access | Times Cited: 184

Cullin-RING Ubiquitin Ligase Regulatory Circuits: A Quarter Century Beyond the F-Box Hypothesis
J. Wade Harper, Brenda A. Schulman
Annual Review of Biochemistry (2021) Vol. 90, Iss. 1, pp. 403-429
Open Access | Times Cited: 181

Quality Control of Orphaned Proteins
Szymon Juszkiewicz, Ramanujan S. Hegde
Molecular Cell (2018) Vol. 71, Iss. 3, pp. 443-457
Open Access | Times Cited: 166

Conformational ensembles of the human intrinsically disordered proteome
Giulio Tesei, Anna Ida Trolle, Nicolas Jonsson, et al.
Nature (2024) Vol. 626, Iss. 8000, pp. 897-904
Closed Access | Times Cited: 126

Ribosome-associated quality-control mechanisms from bacteria to humans
Sebastian Filbeck, Federico Cerullo, Stefan Pfeffer, et al.
Molecular Cell (2022) Vol. 82, Iss. 8, pp. 1451-1466
Open Access | Times Cited: 120

The E3 ligase adapter cereblon targets the C-terminal cyclic imide degron
Saki Ichikawa, Hope A. Flaxman, Wenqing Xu, et al.
Nature (2022) Vol. 610, Iss. 7933, pp. 775-782
Open Access | Times Cited: 112

Driving E3 Ligase Substrate Specificity for Targeted Protein Degradation: Lessons from Nature and the Laboratory
Angus D. Cowan, Alessio Ciulli
Annual Review of Biochemistry (2022) Vol. 91, Iss. 1, pp. 295-319
Open Access | Times Cited: 83

Post-translational control of beige fat biogenesis by PRDM16 stabilization
Qiang Wang, Huixia Li, Kazuki Tajima, et al.
Nature (2022) Vol. 609, Iss. 7925, pp. 151-158
Open Access | Times Cited: 73

How the ends signal the end: Regulation by E3 ubiquitin ligases recognizing protein termini
Dawafuti Sherpa, Jakub Chrustowicz, Brenda A. Schulman
Molecular Cell (2022) Vol. 82, Iss. 8, pp. 1424-1438
Open Access | Times Cited: 72

The midnolin-proteasome pathway catches proteins for ubiquitination-independent degradation
Xin Gu, Christopher Nardone, Nolan Kamitaki, et al.
Science (2023) Vol. 381, Iss. 6660
Open Access | Times Cited: 62

Noncoding translation mitigation
Jordan S. Kesner, Ziheng Chen, Peiguo Shi, et al.
Nature (2023) Vol. 617, Iss. 7960, pp. 395-402
Open Access | Times Cited: 57

ELM—the Eukaryotic Linear Motif resource—2024 update
Manjeet Kumar, Sushama Michael, Jesús Alvarado-Valverde, et al.
Nucleic Acids Research (2023) Vol. 52, Iss. D1, pp. D442-D455
Open Access | Times Cited: 52

CRISPR/Cas9-based split homing gene drive targeting doublesex for population suppression of the global fruit pest Drosophila suzukii
Amarish Kumar Yadav, Cole Butler, Akihiko Yamamoto, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 25
Open Access | Times Cited: 48

Co-opting the E3 ligase KLHDC2 for targeted protein degradation by small molecules
Christopher M. Hickey, Katherine M. Digianantonio, Kurt Zimmermann, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 2, pp. 311-322
Closed Access | Times Cited: 25

A mutational atlas for Parkin proteostasis
Lene Clausen, Vasileios Voutsinos, Matteo Cagiada, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 20

Cullin-RING ligases employ geometrically optimized catalytic partners for substrate targeting
Jerry Li, Nicholas Purser, Joanna Liwocha, et al.
Molecular Cell (2024) Vol. 84, Iss. 7, pp. 1304-1320.e16
Open Access | Times Cited: 17

C-terminal amides mark proteins for degradation via SCF–FBXO31
Matthias Muhar, Jakob Farnung, Martina Cernakova, et al.
Nature (2025)
Open Access | Times Cited: 5

C-Terminal End-Directed Protein Elimination by CRL2 Ubiquitin Ligases
Hsiu‐Chuan Lin, Chi‐Wei Yeh, Yen‐Fu Chen, et al.
Molecular Cell (2018) Vol. 70, Iss. 4, pp. 602-613.e3
Open Access | Times Cited: 150

A Cellular Mechanism to Detect and Alleviate Reductive Stress
Andrew G. Manford, Fernando Rodríguez-Pérez, Karen Y. Shih, et al.
Cell (2020) Vol. 183, Iss. 1, pp. 46-61.e21
Open Access | Times Cited: 131

Affinity and specificity of motif-based protein–protein interactions
Ylva Ivarsson, Per Jemth
Current Opinion in Structural Biology (2018) Vol. 54, pp. 26-33
Open Access | Times Cited: 111

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