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:

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

Showing 1-25 of 131 citing articles:

Cancer metabolism: looking forward
Inmaculada Martínez‐Reyes, Navdeep S. Chandel
Nature reviews. Cancer (2021) Vol. 21, Iss. 10, pp. 669-680
Closed Access | Times Cited: 1223

Defining roles of specific reactive oxygen species (ROS) in cell biology and physiology
Helmut Sies, Vsevolod V. Belousov, Navdeep S. Chandel, et al.
Nature Reviews Molecular Cell Biology (2022) Vol. 23, Iss. 7, pp. 499-515
Closed Access | Times Cited: 992

Reactive oxygen species-based nanomaterials for the treatment of myocardial ischemia reperfusion injuries
Tianjiao Zhao, Wei Wu, Sui Li-hua, et al.
Bioactive Materials (2021) Vol. 7, pp. 47-72
Open Access | Times Cited: 216

E3 Ligase Ligands in Successful PROTACs: An Overview of Syntheses and Linker Attachment Points
Aleša Bricelj, Christian Steinebach, Robert D. Kuchta, et al.
Frontiers in Chemistry (2021) Vol. 9
Open Access | Times Cited: 158

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

Fundamentals of redox regulation in biology
Helmut Sies, Ryan J. Mailloux, Ursula Jakob
Nature Reviews Molecular Cell Biology (2024) Vol. 25, Iss. 9, pp. 701-719
Closed Access | Times Cited: 111

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

Typhaneoside-Tetrahedral Framework Nucleic Acids System: Mitochondrial Recovery and Antioxidation for Acute Kidney Injury treatment
Ran Yan, Weitong Cui, Wenjuan Ma, et al.
ACS Nano (2023) Vol. 17, Iss. 9, pp. 8767-8781
Closed Access | Times Cited: 81

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

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: 72

The pleiotropic functions of reactive oxygen species in cancer
Katherine Wu, Ahmed E. El Zowalaty, Volkan I. Sayin, et al.
Nature Cancer (2024) Vol. 5, Iss. 3, pp. 384-399
Closed Access | Times Cited: 58

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

Stress response silencing by an E3 ligase mutated in neurodegeneration
Diane L. Haakonsen, Michael Heider, Andrew J. Ingersoll, et al.
Nature (2024) Vol. 626, Iss. 8000, pp. 874-880
Open Access | Times Cited: 37

Effects of Lactobacillus plantarum and Bacillus subtilis on growth, immunity and intestinal flora of largemouth bass(Micropterus salmoides)
Wangyang Jin, Lihua Jiang, Siling Hu, et al.
Aquaculture (2024) Vol. 583, pp. 740581-740581
Closed Access | Times Cited: 18

Intracellular dehydrogenation catalysis leads to reductive stress and immunosuppression
Jie Jiang, Huizhen Zheng, Zhenzhen Wang, et al.
Nature Nanotechnology (2025)
Closed Access | Times Cited: 3

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

An E3 ligase guide to the galaxy of small-molecule-induced protein degradation
Predrag Jevtić, Diane L. Haakonsen, Michael Rapé
Cell chemical biology (2021) Vol. 28, Iss. 7, pp. 1000-1013
Open Access | Times Cited: 99

Ligandability of E3 Ligases for Targeted Protein Degradation Applications
Bridget P. Belcher, Carl C. Ward, Daniel K. Nomura
Biochemistry (2021) Vol. 62, Iss. 3, pp. 588-600
Open Access | Times Cited: 94

The KEAP1-NRF2 System in Healthy Aging and Longevity
Daisuke Matsumaru, Hozumi Motohashi
Antioxidants (2021) Vol. 10, Iss. 12, pp. 1929-1929
Open Access | Times Cited: 69

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

New anti-cancer explorations based on metal ions
Han Hu, Qi Xu, Zhimin Mo, et al.
Journal of Nanobiotechnology (2022) Vol. 20, Iss. 1
Open Access | Times Cited: 66

Folliculin: A Regulator of Transcription Through AMPK and mTOR Signaling Pathways
Josué M. J. Ramirez Reyes, Rafael Cuesta, Arnim Pause
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 65

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

The NLRP1 and CARD8 inflammasomes detect reductive stress
Qinghui Wang, Jeffrey C. Hsiao, Noah Yardeny, et al.
Cell Reports (2023) Vol. 42, Iss. 1, pp. 111966-111966
Open Access | Times Cited: 30

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