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 basis and regulation of the reductive stress response
Andrew G. Manford, Elijah L. Mena, Karen Y. Shih, et al.
Cell (2021) Vol. 184, Iss. 21, pp. 5375-5390.e16
Open Access | Times Cited: 100

Showing 1-25 of 100 citing articles:

Discovery of a Covalent FEM1B Recruiter for Targeted Protein Degradation Applications
Nathaniel J. Henning, Andrew G. Manford, Jessica N. Spradlin, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 2, pp. 701-708
Open Access | Times Cited: 157

Induction of lysosomal and mitochondrial biogenesis by AMPK phosphorylation of FNIP1
Nazma Malik, Bibiana I. Ferreira, Pablo E. Hollstein, et al.
Science (2023) Vol. 380, Iss. 6642
Open Access | Times Cited: 114

Chasing molecular glue degraders: screening approaches
Ana Domostegui, Luis Nieto‐Barrado, Carles Perez‐Lopez, et al.
Chemical Society Reviews (2022) Vol. 51, Iss. 13, pp. 5498-5517
Open Access | Times Cited: 103

Targeted protein degradation: from mechanisms to clinic
Jonathan M. Tsai, Radosław P. Nowak, Benjamin L. Ebert, et al.
Nature Reviews Molecular Cell Biology (2024) Vol. 25, Iss. 9, pp. 740-757
Closed Access | Times Cited: 95

E3 ligase ligand chemistries: from building blocks to protein degraders
Izidor Sosič, Aleša Bricelj, Christian Steinebach
Chemical Society Reviews (2022) Vol. 51, Iss. 9, pp. 3487-3534
Closed Access | Times Cited: 92

NRF2 activation induces NADH-reductive stress, providing a metabolic vulnerability in lung cancer
Tommy Weiss‐Sadan, Maolin Ge, Makiko Hayashi, et al.
Cell Metabolism (2023) Vol. 35, Iss. 3, pp. 487-503.e7
Open Access | Times Cited: 76

Regulation of antioxidants in cancer
Fábio Hecht, Marco Zocchi, Fatemeh Alimohammadi, et al.
Molecular Cell (2023) Vol. 84, Iss. 1, pp. 23-33
Open Access | Times Cited: 46

Nanomaterials‐Induced Redox Imbalance: Challenged and Opportunities for Nanomaterials in Cancer Therapy
Xumeng Wu, Ziqi Zhou, Kai Li, et al.
Advanced Science (2024) Vol. 11, Iss. 16
Open Access | Times Cited: 27

Converging mechanism of UM171 and KBTBD4 neomorphic cancer mutations
Xiaowen Xie, Olivia Zhang, Megan J. R. Yeo, et al.
Nature (2025)
Open Access | Times Cited: 7

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: 69

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

Current advances of small molecule E3 ligands for proteolysis-targeting chimeras design
Dazhao Mi, Yuzhan Li, Haijun Gu, et al.
European Journal of Medicinal Chemistry (2023) Vol. 256, pp. 115444-115444
Closed Access | Times Cited: 27

E3 ligase autoinhibition by C-degron mimicry maintains C-degron substrate fidelity
Daniel C. Scott, Moeko T. King, Kheewoong Baek, et al.
Molecular Cell (2023) Vol. 83, Iss. 5, pp. 770-786.e9
Open Access | Times Cited: 26

Potential Benefits of Antioxidant Phytochemicals in Type 2 Diabetes
Arman Arabshomali, Shadi Bazzazzadehgan, Fakhri Mahdi, et al.
Molecules (2023) Vol. 28, Iss. 20, pp. 7209-7209
Open Access | Times Cited: 23

Reductive stress in cancer: coming out of the shadows
Maolin Ge, Thales Papagiannakopoulos, Liron Bar‐Peled
Trends in cancer (2023) Vol. 10, Iss. 2, pp. 103-112
Closed Access | Times Cited: 23

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: 15

A RAB7A phosphoswitch coordinates Rubicon Homology protein regulation of Parkin-dependent mitophagy
Dan Tudorica, Bishal Basak, Alexia S. Puerta Cordova, et al.
The Journal of Cell Biology (2024) Vol. 223, Iss. 7
Open Access | Times Cited: 10

Non-canonical substrate recognition by the human WDR26-CTLH E3 ligase regulates prodrug metabolism
Karthik V Gottemukkala, Jakub Chrustowicz, Dawafuti Sherpa, et al.
Molecular Cell (2024) Vol. 84, Iss. 10, pp. 1948-1963.e11
Open Access | Times Cited: 9

Reductive stress: The key pathway in metabolic disorders induced by overnutrition
Shiyi Zhang, Na Wang, Zhichao Gao, et al.
Journal of Advanced Research (2025)
Open Access | Times Cited: 1

Distinct Stress Regulators in the CRL Family: Emerging Roles of F‐Box Proteins
Jiwon Hwang, Linda Lauinger, Peter Kaiser
BioEssays (2025)
Closed Access | Times Cited: 1

Quality control of protein complex composition
Chris Padovani, Predrag Jevtić, Michael Rapé
Molecular Cell (2022) Vol. 82, Iss. 8, pp. 1439-1450
Open Access | Times Cited: 29

Defining E3 ligase–substrate relationships through multiplex CRISPR screening
Richard T. Timms, Elijah L. Mena, Yumei Leng, et al.
Nature Cell Biology (2023) Vol. 25, Iss. 10, pp. 1535-1545
Open Access | Times Cited: 22

Elucidation of E3 ubiquitin ligase specificity through proteome-wide internal degron mapping
Zhiqian Zhang, Brandon Sie, Aiquan Chang, et al.
Molecular Cell (2023) Vol. 83, Iss. 18, pp. 3377-3392.e6
Open Access | Times Cited: 21

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