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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:

Enabling Role of Ligand-Driven Conformational Changes in Enzyme Evolution
John P. Richard
Biochemistry (2022) Vol. 61, Iss. 15, pp. 1533-1542
Open Access | Times Cited: 35

Showing 1-25 of 35 citing articles:

Perspectives on Computational Enzyme Modeling: From Mechanisms to Design and Drug Development
Kwangho Nam, Yihan Shao, Dan Thomas Major, et al.
ACS Omega (2024)
Open Access | Times Cited: 15
Dynamics of receptor activation by agonists
Anthony Auerbach
Biophysical Journal (2024) Vol. 123, Iss. 14, pp. 1915-1923
Closed Access | Times Cited: 8
Agonist efficiency links binding and gating in a nicotinic receptor
Dinesh C. Indurthi, Anthony Auerbach
eLife (2023) Vol. 12
Open Access | Times Cited: 11
Hydrophobicity-Based Force Field In Enzymes
Irena Roterman, Leszek Konieczny, Katarzyna Sta̧por, et al.
ACS Omega (2024)
Open Access | Times Cited: 3
On the Origins of Enzymes: Phosphate-Binding Polypeptides Mediate Phosphoryl Transfer to Synthesize Adenosine Triphosphate
Pratik Vyas, Sergey Malitsky, Maxim Itkin, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 15, pp. 8344-8354
Open Access | Times Cited: 7
Analyzing the Reaction of Orotidine 5′-Phosphate Decarboxylase as a Way to Examine Some Key Catalytic Proposals
Mojgan Asadi, Arieh Warshel
Journal of the American Chemical Society (2022) Vol. 145, Iss. 2, pp. 1334-1341
Open Access | Times Cited: 12
Stable monomers in the ancestral sequence reconstruction of the last opisthokont common ancestor of dimeric triosephosphate isomerase
Jorge Alejandro Pérez‐Niño, Yasel Guerra, A. Jessica Díaz‐Salazar, et al.
Protein Science (2024) Vol. 33, Iss. 9
Open Access | Times Cited: 1
Adenylate Kinase-Catalyzed Reactions of AMP in Pieces: Specificity for Catalysis at the Nucleoside Activator and Dianion Catalytic Sites
Patrick Fernandez, John P. Richard
Biochemistry (2022) Vol. 61, Iss. 23, pp. 2766-2775
Open Access | Times Cited: 10
Glycerol 3-Phosphate Dehydrogenase: Role of the Protein Conformational Change in Activation of a Readily Reversible Enzyme-Catalyzed Hydride Transfer Reaction
Judith R. Cristobal, Rania Hegazy, John P. Richard
Biochemistry (2024) Vol. 63, Iss. 8, pp. 1016-1025
Closed Access | Times Cited: 1
Four Parallel Pathways in T4 Ligase‐Catalyzed Repair of Nicked DNA with Diverse Bending Angles
Na Li, Jianbing Ma, Hang Fu, et al.
Advanced Science (2024) Vol. 11, Iss. 25
Open Access | Times Cited: 1
The Many‐Chemicals Problem of Systems Chemistry
Oliver R. Maguire
ChemSystemsChem (2024) Vol. 6, Iss. 5
Closed Access | Times Cited: 1
The Role of the Substrate Phosphodianion in Catalysis by Orotidine 5′-Monophosphate Decarboxylase
John P. Richard
Biochemistry (2023) Vol. 62, Iss. 5, pp. 969-970
Open Access | Times Cited: 4
Human 2′-Deoxynucleoside 5′-Phosphate N-Hydrolase 1: Mechanism of 2′-Deoxyuridine 5′-Monophosphate Hydrolysis
Suneeta Devi, Anna E. Carberry, Greice M. Zickuhr, et al.
Biochemistry (2023) Vol. 62, Iss. 17, pp. 2658-2668
Open Access | Times Cited: 4
The Role of Asn11 in Catalysis by Triosephosphate Isomerase
Rania Hegazy, Gabriele Cordara, Rik K. Wierenga, et al.
Biochemistry (2023) Vol. 62, Iss. 11, pp. 1794-1806
Closed Access | Times Cited: 2
Kinetics and mechanism for enzyme-catalyzed reactions of substrate pieces
Judith R. Cristobal, John P. Richard
Methods in enzymology on CD-ROM/Methods in enzymology (2023), pp. 95-126
Open Access | Times Cited: 2
Crystal structures and kinetic studies of a laboratory evolved aldehyde reductase explain the dramatic shift of its new substrate specificity
Shruthi Sridhar, Alberto Zavarise, Tiila‐Riikka Kiema, et al.
IUCrJ (2023) Vol. 10, Iss. 4, pp. 437-447
Open Access | Times Cited: 2
Dual Efficacy of a Catalytic Anti-Oligomeric Aβ42 scFv Antibody in Clearing Aβ42 Aggregates and Reducing Aβ Burden in the Brains of Alzheimer’s Disease Mice
Chuli Song, He Li, Changxin Zheng, et al.
Molecular Neurobiology (2023) Vol. 60, Iss. 10, pp. 5515-5532
Closed Access | Times Cited: 2
Enzyme dynamics—a brief review
Jeremy R. H. Tame
Biophysical Reviews (2023) Vol. 15, Iss. 3, pp. 317-320
Closed Access | Times Cited: 2
Utilization of Cofactor Binding Energy for Enzyme Catalysis: Formate Dehydrogenase-Catalyzed Reactions of the Whole NAD Cofactor and Cofactor Pieces
Judith R. Cristobal, Richard W. Nagorski, John P. Richard
Biochemistry (2023) Vol. 62, Iss. 15, pp. 2314-2324
Open Access | Times Cited: 2
Enzymes of the crotonase superfamily: Diverse assembly and diverse function
Subhadra Dalwani, Rik K. Wierenga
Current Opinion in Structural Biology (2023) Vol. 82, pp. 102671-102671
Open Access | Times Cited: 2
Triosephosphate Isomerase: The Crippling Effect of the P168A/I172A Substitution at the Heart of an Enzyme Active Site
Rania Hegazy, John P. Richard
Biochemistry (2023) Vol. 62, Iss. 20, pp. 2916-2927
Open Access | Times Cited: 2
Conformational dynamics of a nicotinic receptor neurotransmitter binding site
Mrityunjay Singh, Dinesh C. Indurthi, Lovika Mittal, et al.
eLife (2024) Vol. 13
Open Access
Conformational dynamics of a nicotinic receptor neurotransmitter binding site
Mrityunjay Singh, Dinesh C. Indurthi, Lovika Mittal, et al.
(2024)
Open Access
Redefining the Therapeutic Landscape: A Critical Analysis of Triterpenoids as Neutrophil Elastase Inhibitors
George Oche Ambrose
Natural Product Communications (2024) Vol. 19, Iss. 3
Open Access
Structural and functional effects of phosphopriming and scaffolding in the kinase GSK-3β
M.D. Enos, Maire Gavagan, Noel Jameson, et al.
Science Signaling (2024) Vol. 17, Iss. 852
Closed Access
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