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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.

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Showing 1-25 of 43 citing articles:

ROS Generation and Antioxidant Defense Systems in Normal and Malignant Cells
Anastasiya V. Snezhkina, Anna V. Kudryavtseva, Olga Kardymon, et al.
Oxidative Medicine and Cellular Longevity (2019) Vol. 2019, pp. 1-17
Open Access | Times Cited: 735
Role of the ERO1-PDI interaction in oxidative protein folding and disease
Andrea Shergalis, Shuai Hu, Armand Bankhead, et al.
Pharmacology & Therapeutics (2020) Vol. 210, pp. 107525-107525
Open Access | Times Cited: 122
Endoplasmic Reticulum stress-dependent expression of ERO1L promotes aerobic glycolysis in Pancreatic Cancer
Junfeng Zhang, Jian‐Yu Yang, Chaoyi Lin, et al.
Theranostics (2020) Vol. 10, Iss. 18, pp. 8400-8414
Open Access | Times Cited: 74
Heat stress-induced endoplasmic reticulum stress promotes liver apoptosis in largemouth bass (Micropterus salmoides)
Xuqian Zhao, Lingling Li, Caijuan Li, et al.
Aquaculture (2021) Vol. 546, pp. 737401-737401
Closed Access | Times Cited: 73
Regulation of redox signaling in HIF‐1‐dependent tumor angiogenesis
Valeria Manuelli, Chiara Pecorari, Giuseppe Filomeni, et al.
FEBS Journal (2021) Vol. 289, Iss. 18, pp. 5413-5425
Open Access | Times Cited: 64
Oxidative protein folding fidelity and redoxtasis in the endoplasmic reticulum
Lei Wang, Chih-chen Wang
Trends in Biochemical Sciences (2022) Vol. 48, Iss. 1, pp. 40-52
Closed Access | Times Cited: 50
SEPN1-related myopathy depends on the oxidoreductase ERO1A and is druggable with the chemical chaperone TUDCA
Serena Germani, Andrew Tri Van Ho, Alessandro Cherubini, et al.
Cell Reports Medicine (2024) Vol. 5, Iss. 3, pp. 101439-101439
Open Access | Times Cited: 13
Crosstalk between endoplasmic reticulum stress and oxidative stress: Focus on protein disulfide isomerase and endoplasmic reticulum oxidase 1
Paul Victor, D. V. L. Sarada, Kunka Mohanram Ramkumar
European Journal of Pharmacology (2020) Vol. 892, pp. 173749-173749
Closed Access | Times Cited: 62
The ER stress response mediator ERO1 triggers cancer metastasis by favoring the angiogenic switch in hypoxic conditions
Ersilia Varone, Alessandra Decio, Alexander Chernorudskiy, et al.
Oncogene (2021) Vol. 40, Iss. 9, pp. 1721-1736
Open Access | Times Cited: 49
Reducing oxidative protein folding alleviates senescence by minimizing ER‐to‐nucleus H2O2 release
Cheng Fang, Qianzhao Ji, Lu Wang, et al.
EMBO Reports (2023) Vol. 24, Iss. 8
Open Access | Times Cited: 17
Reductive Stress-Induced Mitochondrial Dysfunction and Cardiomyopathy
WEI-XING MA, Chunyan Li, Ran Tao, et al.
Oxidative Medicine and Cellular Longevity (2020) Vol. 2020, pp. 1-11
Open Access | Times Cited: 46
Protein disulfide isomerase blocks the interaction of LC3II-PHB2 and promotes mTOR signaling to regulate autophagy and radio/chemo-sensitivity
Ruru Wang, Yajing Shang, Bin Chen, et al.
Cell Death and Disease (2022) Vol. 13, Iss. 10
Open Access | Times Cited: 26
Integration of transcriptome and proteome analyses reveals the regulation mechanisms of Larimichthys polyactis liver exposed to heat stress
Feng Liu, Tianle Zhang, Yu He, et al.
Fish & Shellfish Immunology (2023) Vol. 135, pp. 108704-108704
Closed Access | Times Cited: 14
SIRT6 deficiency in endothelial cells exacerbates oxidative stress by enhancing HIF1α accumulation and H3K9 acetylation at the Ero1α promoter
Zhenyang Guo, Xueting Yu, Shuang Zhao, et al.
Clinical and Translational Medicine (2023) Vol. 13, Iss. 8
Open Access | Times Cited: 13
Thioredoxin Domain Containing 5 (TXNDC5): Friend or Foe?
Seyed Hesamoddin Bidooki, María Á. Navarro, Susana C. M. Fernandes, et al.
Current Issues in Molecular Biology (2024) Vol. 46, Iss. 4, pp. 3134-3163
Open Access | Times Cited: 5
Targeting ER stress/ER stress response in myopathies
Ester Zito
Redox Biology (2019) Vol. 26, pp. 101232-101232
Open Access | Times Cited: 36
ER reductive stress caused by Ero1α S-nitrosation accelerates senescence
Xinhua Qiao, Yingmin Zhang, Aojun Ye, et al.
Free Radical Biology and Medicine (2022) Vol. 180, pp. 165-178
Closed Access | Times Cited: 22
Distinct Roles of Nrf1 and Nrf2 in Monitoring the Reductive Stress Response to Dithiothreitol (DTT)
Reziyamu Wufuer, Zhuo Fan, Jianxin Yuan, et al.
Antioxidants (2022) Vol. 11, Iss. 8, pp. 1535-1535
Open Access | Times Cited: 19
Small molecule-mediated inhibition of the oxidoreductase ERO1A restrains aggressive breast cancer by impairing VEGF and PD-L1 in the tumor microenvironment
Ersilia Varone, Michele Retini, Alessandro Cherubini, et al.
Cell Death and Disease (2025) Vol. 16, Iss. 1
Open Access
Ero1α, the Most Significantly Upregulated Hypoxia-Induced Protein in Pasmcs, Promotes the Development of Hypoxia and Mct Induced Pulmonary Hypertension
Hongxia Jiang, Xiaojun Hao, Zhenshun Cheng, et al.
(2025)
Closed Access
Protein disulfide isomerase is regulated in multiple ways: Consequences for conformation, activities, and pathophysiological functions
Lei Wang, Jiaojiao Yu, Chih‐Chen Wang
BioEssays (2020) Vol. 43, Iss. 3
Closed Access | Times Cited: 30
Biological mechanisms and clinical significance of endoplasmic reticulum oxidoreductase 1 alpha (ERO1α) in human cancer
Peng Chen, Amit Sharma, Hans Weiher, et al.
Journal of Experimental & Clinical Cancer Research (2024) Vol. 43, Iss. 1
Open Access | Times Cited: 3
ERO1-PDI Redox Signaling in Health and Disease
Vishwanath Jha, Tripti Kumari, Vijayprakash Manickam, et al.
Antioxidants and Redox Signaling (2021) Vol. 35, Iss. 13, pp. 1093-1115
Open Access | Times Cited: 21
The extracellular Ero1α/PDI electron transport system regulates platelet function by increasing glutathione reduction potential
Lu Wang, Xi Wang, Xiying Lv, et al.
Redox Biology (2022) Vol. 50, pp. 102244-102244
Open Access | Times Cited: 14
Nano-bioengineered sensing technologies for real-time monitoring of reactive oxygen species in in vitro and in vivo models
Rohini Kumari, Daphika S. Dkhar, Supratim Mahapatra, et al.
Microchemical Journal (2022) Vol. 180, pp. 107615-107615
Closed Access | Times Cited: 14
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