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:

Anion–π interactions in active centers of superoxide dismutases
Vesna Ribić, Srđan Đ. Stojanović, Mario Zlatović
International Journal of Biological Macromolecules (2017) Vol. 106, pp. 559-568
Open Access | Times Cited: 21

Showing 21 citing articles:

Emergence of anion-π interactions: The land of opportunity in supramolecular chemistry and beyond
Ishfaq Ahmad Rather, Shafieq Ahmad Wagay, Rashid Ali
Coordination Chemistry Reviews (2020) Vol. 415, pp. 213327-213327
Closed Access | Times Cited: 102

Anion–π Catalysis Enabled by the Mechanical Bond**
John R. J. Maynard, Bartomeu Galmés, Α. Στέργιου, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 12
Open Access | Times Cited: 27

Insight into the binding behavior of N-(1,3-Dimethylbutyl)-N′-phenyl-p-phenylenediamine and its quinone-metabolite with pepsin: Multidisciplinary approaches
Yu Li, Yujuan Yao, Jianjun Qin, et al.
International Journal of Biological Macromolecules (2025), pp. 140738-140738
Closed Access

Anion-π Interactions in Computer-Aided Drug Design: Modeling the Inhibition of Malate Synthase by Phenyl-Diketo Acids
Jill F. Ellenbarger, Inna V. Krieger, Hsiao‐Ling Huang, et al.
Journal of Chemical Information and Modeling (2018) Vol. 58, Iss. 10, pp. 2085-2091
Closed Access | Times Cited: 27

Halide and hydroxide anion binding in water
Matteo Savastano, Carla Bazzicalupi, Celeste García-Gallarín, et al.
Dalton Transactions (2018) Vol. 47, Iss. 10, pp. 3329-3338
Open Access | Times Cited: 24

A green light-enhanced cytosolic protein delivery platform based on BODIPY-protein interactions
Yang Zhou, Yifan Gao, Li Pang, et al.
Nano Research (2022) Vol. 16, Iss. 1, pp. 1042-1051
Closed Access | Times Cited: 11

Anion-pi Interactions in Computer-Aided Drug Design: Modeling the Inhibition of Malate Synthase by Phenyl-Diketo Acids.
Jill F. Ellenbarger, Inna V. Krieger, Hsiao‐Ling Huang, et al.
Journal of Chemical Information and Modeling (2018) Vol. 58, Iss. 10, pp. 2085-2091
Closed Access | Times Cited: 18

Mining anion–aromatic interactions in the Protein Data Bank
Emilia Kuźniak, Michał Glanowski, Rafał Kurczab, et al.
Chemical Science (2022) Vol. 13, Iss. 14, pp. 3984-3998
Open Access | Times Cited: 9

Binding of anionic Pt(ii) complexes in a dedicated organic matrix: towards new binary crystalline composites
Emilia Kuźniak, Dorota Glosz, Grzegorz Niedzielski, et al.
Dalton Transactions (2020) Vol. 50, Iss. 1, pp. 170-185
Closed Access | Times Cited: 10

Computational Analysis of Non‐covalent Interactions in Phycocyanin Subunit Interfaces
Luka M. Breberina, Mario Zlatović, Milan Nikolić, et al.
Molecular Informatics (2019) Vol. 38, Iss. 11-12
Open Access | Times Cited: 8

Water–Tryptophan Interactions: Lone‐pair⋅⋅⋅π or O−H⋅⋅⋅π? Molecular Dynamics Simulations of β‐Galactosidase Suggest that Both Modes Can Co‐exist
Matúš Durec, Radek Marek, Jiřı́ Kozelka
Chemistry - A European Journal (2018) Vol. 24, Iss. 22, pp. 5849-5859
Closed Access | Times Cited: 7

Integrated multi-techniques to probe the binding mechanism between amlodipine and lactate dehydrogenase
Xiaolan Lv, Hao Fu, Jiawen Xie, et al.
Journal of Molecular Structure (2020) Vol. 1219, pp. 128656-128656
Closed Access | Times Cited: 6

Thyroid hormone transporters binding affinity of methoxypoly chlorinated biphenyls: Insights from molecular simulations and fluorescence competitive binding experiment
Dan Jia, Wangli Miao, Yuefan Rui, et al.
International Journal of Biological Macromolecules (2023) Vol. 231, pp. 123224-123224
Closed Access | Times Cited: 2

Amide-π interactions in active centers of superoxide dismutase
Srđan Đ. Stojanović, Zoran Z. Petrović, Mario Zlatović
Journal of the Serbian Chemical Society (2021) Vol. 86, Iss. 9, pp. 781-793
Open Access | Times Cited: 5

Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study
Luka M. Breberina, Milan Nikolić, Srđan Đ. Stojanović, et al.
Computational Biology and Chemistry (2022) Vol. 100, pp. 107752-107752
Closed Access | Times Cited: 3

Amide–π Interactions in the Structural Stability of Proteins: Role in the Oligomeric Phycocyanins
Luka M. Breberina, Mario Zlatović, Srđan Đ. Stojanović, et al.
Computation (2024) Vol. 12, Iss. 9, pp. 172-172
Open Access

On the importance of π-π interactions in the structural stability of phycocyanins
Luka M. Breberina, Milan Nikolić, Srđan Đ. Stojanović, et al.
Journal of the Serbian Chemical Society (2023) Vol. 88, Iss. 5, pp. 481-494
Open Access | Times Cited: 1

Investigations on the role of cation-π interactions in active centers of superoxide dismutase
Srđan Đ. Stojanović, Mario Zlatović
Journal of the Serbian Chemical Society (2022) Vol. 87, Iss. 4, pp. 465-477
Open Access | Times Cited: 1

π-π interactions in structural stability: Role in superoxide dismutases
Srđan Đ. Stojanović, Mario Zlatović
Journal of the Serbian Chemical Society (2022) Vol. 88, Iss. 3, pp. 223-235
Open Access | Times Cited: 1

Anion–π Catalysis Enabled by the Mechanical Bond**
John R. J. Maynard, Bartomeu Galmés, Α. Στέργιου, et al.
Angewandte Chemie (2022) Vol. 134, Iss. 12
Open Access

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