Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Glutaredoxins and iron-sulfur protein biogenesis at the interface of redox biology and iron metabolism
Ulrich Mühlenhoff, Joseph J. Braymer, Stefan Christ, et al.
Biological Chemistry (2020) Vol. 401, Iss. 12, pp. 1407-1428
Open Access | Times Cited: 40

Showing 1-25 of 40 citing articles:

Mitochondria at the crossroads of health and disease
Anu Suomalainen, Jodi Nunnari
Cell (2024) Vol. 187, Iss. 11, pp. 2601-2627
Open Access | Times Cited: 110
Understanding the role of cysteine in ferroptosis: progress & paradoxes
Carson Poltorack, Scott J. Dixon
FEBS Journal (2021) Vol. 289, Iss. 2, pp. 374-385
Open Access | Times Cited: 73
Interactions of reactive sulfur species with metalloproteins
Andrea Domán, Éva Dóka, Dorottya Garai, et al.
Redox Biology (2023) Vol. 60, pp. 102617-102617
Open Access | Times Cited: 41
The Connection Between Oxidative Stress, Mitochondrial Dysfunction, Iron Metabolism and Microglia in Multiple Sclerosis: A Narrative Review
Simonida Delic, Svetlana Miletić Drakulić, Miloš Stepović, et al.
NeuroSci (2025) Vol. 6, Iss. 1, pp. 23-23
Open Access | Times Cited: 1
Mitochondrial glutaredoxin Grx5 functions as a central hub for cellular iron-sulfur cluster assembly
Ashutosh Pandey, Jayashree Pain, Pratibha Singh, et al.
Journal of Biological Chemistry (2025), pp. 108391-108391
Open Access | Times Cited: 1
Iron in leaves: chemical forms, signalling, and in-cell distribution
Máté Sági-Kazár, Katalin Solymosi, Ádám Solti
Journal of Experimental Botany (2022) Vol. 73, Iss. 6, pp. 1717-1734
Open Access | Times Cited: 32
Regulation of Heme Synthesis by Mitochondrial Homeostasis Proteins
Yvette Y. Yien, Mark Perfetto
Frontiers in Cell and Developmental Biology (2022) Vol. 10
Open Access | Times Cited: 31
N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization
Sven‐A. Freibert, Michal T. Boniecki, Claudia Stümpfig, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 33
Homeostasis of carbohydrates and reactive oxygen species is critically changed in the brain of middle-aged mice: Molecular mechanisms and functional reasons
Maria M. Bayliak, Dmytro V. Gospodaryov, Volodymyr I. Lushchak
BBA Advances (2023) Vol. 3, pp. 100077-100077
Open Access | Times Cited: 14
The DnaJ proteins DJA6 and DJA5 are essential for chloroplast iron–sulfur cluster biogenesis
Jing Zhang, Zechen Bai, Min Ouyang, et al.
The EMBO Journal (2021) Vol. 40, Iss. 13
Open Access | Times Cited: 31
Essential Protective Role of Catalytically Active Antibodies (Abzymes) with Redox Antioxidant Functions in Animals and Humans
Anna S. Tolmacheva, Georgy A. Nevinsky
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 7, pp. 3898-3898
Open Access | Times Cited: 22
Mitochondrial [2Fe‐2S] ferredoxins: new functions for old dogs
Vinzent Schulz, Sven‐A. Freibert, Linda Boß, et al.
FEBS Letters (2022) Vol. 597, Iss. 1, pp. 102-121
Open Access | Times Cited: 21
Adaptation of the late ISC pathway in the anaerobic mitochondrial organelles of Giardia intestinalis
Alžběta Motyčková, Luboš Voleman, Vladimíra Najdrová, et al.
PLoS Pathogens (2023) Vol. 19, Iss. 10, pp. e1010773-e1010773
Open Access | Times Cited: 11
The significance of glutaredoxins for diabetes mellitus and its complications
Mengmeng Zhou, Eva-Maria Hanschmann, Axel Römer, et al.
Redox Biology (2024) Vol. 71, pp. 103043-103043
Open Access | Times Cited: 4
Requirements for the biogenesis of [2Fe-2S] proteins in the human and yeast cytosol
Joseph J. Braymer, Oliver Stehling, Martin Stümpfig, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 21
Open Access | Times Cited: 4
Glutathione and glutathione-dependent enzymes
Marcel Deponte
Elsevier eBooks (2022), pp. 241-275
Closed Access | Times Cited: 17
Control of Replication Stress Response by Cytosolic Fe-S Cluster Assembly (CIA) Machinery
Chiara Frigerio, Michela Galli, Stefano Castelli, et al.
Cells (2025) Vol. 14, Iss. 6, pp. 442-442
Open Access
The glutathione system maintains the thiol redox balance in the mitochondria of fission yeast
Laura de Cubas, Susanna Boronat, Montserrat Rojo de la Vega, et al.
Free Radical Biology and Medicine (2025)
Closed Access
Maintenance of small molecule redox homeostasis in mitochondria
Lianne H.C. Jacobs, Jan Riemer
FEBS Letters (2022) Vol. 597, Iss. 2, pp. 205-223
Open Access | Times Cited: 13
Iron homeostasis proteins Grx4 and Fra2 control activity of the Schizosaccharomyces pombe iron repressor Fep1 by facilitating [2Fe-2S] cluster removal
Debolina Hati, Ariane Brault, Malini Gupta, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 12, pp. 105419-105419
Open Access | Times Cited: 7
Mrp and SufT, Two Bacterial Homologs of Eukaryotic CIA Factors Involved in Fe-S Clusters Biogenesis
Corinne Aubert, Pierre Mandin, Béatrice Py
Inorganics (2023) Vol. 11, Iss. 11, pp. 431-431
Open Access | Times Cited: 7
Molecular pathways of generation and detoxification of reactive oxygen species and induction of apoptosis in yeasts
Sidra Gull, Chaudhry Ahmed Shabbir, Zaman Khan, et al.
Arabian Journal of Chemistry (2024) Vol. 18, Iss. 1, pp. 106069-106069
Open Access | Times Cited: 2
A pathogenic role for histone H3 copper reductase activity in a yeast model of Friedreich’s ataxia
Oscar A. Campos, Narsis Attar, Chen Cheng, et al.
Science Advances (2021) Vol. 7, Iss. 51
Open Access | Times Cited: 15
Molecular network of the oil palm root response to aluminum stress
Fernan Santiago Mejía-Alvarado, David Botero-Rozo, Leonardo Araque, et al.
BMC Plant Biology (2023) Vol. 23, Iss. 1
Open Access | Times Cited: 6
The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr (YpdA) disulfide reductase reduce S-bacillithiolated proteins
Ahmed Gaballa, Tina Tianjiao Su, John D. Helmann
Redox Biology (2021) Vol. 42, pp. 101935-101935
Open Access | Times Cited: 14
Page 1 - Next Page

Scroll to top