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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 pathway for biological methane production using bacterial iron-only nitrogenase
Yanning Zheng, Derek F. Harris, Yu Zheng, et al.
Nature Microbiology (2018) Vol. 3, Iss. 3, pp. 281-286
Closed Access | Times Cited: 150

Showing 1-25 of 150 citing articles:

Reduction of Substrates by Nitrogenases
Lance C. Seefeldt, Zhi‐Yong Yang, Dmitriy Lukoyanov, et al.
Chemical Reviews (2020) Vol. 120, Iss. 12, pp. 5082-5106
Open Access | Times Cited: 320
Global Nitrogen Cycle: Critical Enzymes, Organisms, and Processes for Nitrogen Budgets and Dynamics
Xinning Zhang, Bess B. Ward, Daniel M. Sigman
Chemical Reviews (2020) Vol. 120, Iss. 12, pp. 5308-5351
Closed Access | Times Cited: 320
Aquatic and terrestrial cyanobacteria produce methane
Mina Bižić, Thomas Klintzsch, Danny Ionescu, et al.
Science Advances (2020) Vol. 6, Iss. 3
Open Access | Times Cited: 305
MOF-based materials for photo- and electrocatalytic CO2 reduction
Xiaofang Li, Qi‐Long Zhu
EnergyChem (2020) Vol. 2, Iss. 3, pp. 100033-100033
Closed Access | Times Cited: 305
The Spectroscopy of Nitrogenases
Casey Van Stappen, Laure Decamps, George E. Cutsail, et al.
Chemical Reviews (2020) Vol. 120, Iss. 12, pp. 5005-5081
Open Access | Times Cited: 178
Reactivity, Mechanism, and Assembly of the Alternative Nitrogenases
Andrew J. Jasniewski, Chi Chung Lee, Markus W. Ribbe, et al.
Chemical Reviews (2020) Vol. 120, Iss. 12, pp. 5107-5157
Open Access | Times Cited: 167
2022 roadmap on low temperature electrochemical CO2 reduction
Ifan E. L. Stephens, Karen Chan, Alexander Bagger, et al.
Journal of Physics Energy (2022) Vol. 4, Iss. 4, pp. 042003-042003
Open Access | Times Cited: 156
Metal–Sulfur Compounds in N2 Reduction and Nitrogenase-Related Chemistry
Kazuki Tanifuji, Yasuhiro Ohki
Chemical Reviews (2020) Vol. 120, Iss. 12, pp. 5194-5251
Closed Access | Times Cited: 152
Methane formation driven by reactive oxygen species across all living organisms
Leonard Ernst, Benedikt Steinfeld, Uladzimir Barayeu, et al.
Nature (2022) Vol. 603, Iss. 7901, pp. 482-487
Open Access | Times Cited: 138
Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase
Sven T. Stripp, Benjamin R. Duffus, Vincent Fourmond, et al.
Chemical Reviews (2022) Vol. 122, Iss. 14, pp. 11900-11973
Open Access | Times Cited: 128
Light-driven CO2 sequestration in Escherichia coli to achieve theoretical yield of chemicals
Guipeng Hu, Zehong Li, Danlei Ma, et al.
Nature Catalysis (2021) Vol. 4, Iss. 5, pp. 395-406
Closed Access | Times Cited: 121
Iron-only Fe-nitrogenase underscores common catalytic principles in biological nitrogen fixation
Christian Trncik, Franka Detemple, Oliver Einsle
Nature Catalysis (2023) Vol. 6, Iss. 5, pp. 415-424
Closed Access | Times Cited: 43
Recent advances in metal–organic framework-derived materials for electrocatalytic and photocatalytic CO2 reduction
Yu‐Tao Zheng, Shumin Li, Ning‐Yu Huang, et al.
Coordination Chemistry Reviews (2024) Vol. 510, pp. 215858-215858
Closed Access | Times Cited: 31
Exploring the alternatives of biological nitrogen fixation
Florence Mus, Alexander B. Alleman, Natasha Pence, et al.
Metallomics (2018) Vol. 10, Iss. 4, pp. 523-538
Closed Access | Times Cited: 154
Insights into the ecological roles and evolution of methyl-coenzyme M reductase-containing hot spring Archaea
Zheng‐Shuang Hua, Yulin Wang, Paul N. Evans, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 135
Biological nitrogen fixation by alternative nitrogenases in terrestrial ecosystems: a review
Jean‐Philippe Bellenger, Romain Darnajoux, Xinning Zhang, et al.
Biogeochemistry (2020) Vol. 149, Iss. 1, pp. 53-73
Closed Access | Times Cited: 119
Metabolism of hydrogen gases and bile acids in the gut microbiome
Phillip B. Hylemon, Spencer Harris, Jason M. Ridlon
FEBS Letters (2018) Vol. 592, Iss. 12, pp. 2070-2082
Open Access | Times Cited: 105
Electron Transfer to Nitrogenase in Different Genomic and Metabolic Backgrounds
Saroj Poudel, Daniel R. Colman, Kathryn R. Fixen, et al.
Journal of Bacteriology (2018) Vol. 200, Iss. 10
Open Access | Times Cited: 104
Reconstructing the evolutionary history of nitrogenases: Evidence for ancestral molybdenum‐cofactor utilization
Amanda K. Garcia, Hanon McShea, Bryan Kolaczkowski, et al.
Geobiology (2020) Vol. 18, Iss. 3, pp. 394-411
Open Access | Times Cited: 96
Extracellular Metabolism Sets the Table for Microbial Cross-Feeding
Ryan K. Fritts, Alexandra L. McCully, James B. McKinlay
Microbiology and Molecular Biology Reviews (2021) Vol. 85, Iss. 1
Open Access | Times Cited: 94
Photosynthesis‐driven methane production in oxic lake water as an important contributor to methane emission
Marco Günthel, Isabell Klawonn, Jason Woodhouse, et al.
Limnology and Oceanography (2020) Vol. 65, Iss. 12, pp. 2853-2865
Open Access | Times Cited: 76
Identification of Complex Rumen Microbiome Interaction Within Diverse Functional Niches as Mechanisms Affecting the Variation of Methane Emissions in Bovine
Marina Martínez-Álvaro, Marc Auffret, Robert D. Stewart, et al.
Frontiers in Microbiology (2020) Vol. 11
Open Access | Times Cited: 73
Iron-Only and Vanadium Nitrogenases: Fail-Safe Enzymes or Something More?
Caroline S. Harwood
Annual Review of Microbiology (2020) Vol. 74, Iss. 1, pp. 247-266
Open Access | Times Cited: 73
Light-driven carbon dioxide reduction to methane by Methanosarcina barkeri in an electric syntrophic coculture
Lingyan Huang, Xing Liu, Zhishuai Zhang, et al.
The ISME Journal (2021) Vol. 16, Iss. 2, pp. 370-377
Open Access | Times Cited: 56
Characteristics and Application of Rhodopseudomonas palustris as a Microbial Cell Factory
Meijie Li, Peng Ning, Yi Sun, et al.
Frontiers in Bioengineering and Biotechnology (2022) Vol. 10
Open Access | Times Cited: 39
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