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:

Promoting Vibrations and the Function of Enzymes. Emerging Theoretical and Experimental Convergence
Vern L. Schramm, Steven D. Schwartz
Biochemistry (2018) Vol. 57, Iss. 24, pp. 3299-3308
Open Access | Times Cited: 73

Showing 26-50 of 73 citing articles:

The physical origin of rate promoting vibrations in enzymes revealed by structural rigidity
Yann Chalopin
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 13

Inverse heavy enzyme isotope effects in methylthioadenosine nucleosidases
Morais Brown, Ioanna Zoi, Dimitri Antoniou, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 40
Open Access | Times Cited: 12

Exact Topology of the Dynamic Probability Surface of an Activated Process by Persistent Homology
Farid Manuchehrfar, Huiyu Li, Wei Tian, et al.
The Journal of Physical Chemistry B (2021) Vol. 125, Iss. 18, pp. 4667-4680
Open Access | Times Cited: 11

Transition Path Sampling Based Calculations of Free Energies for Enzymatic Reactions: The Case of Human Methionine Adenosyl Transferase and Plasmodium vivax Adenosine Deaminase
Sree Ganesh Balasubramani, Steven D. Schwartz
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 29, pp. 5413-5420
Open Access | Times Cited: 8

Connecting Conformational Motions to Rapid Dynamics in Human Purine Nucleoside Phosphorylase
Clara F. Frost, Sree Ganesh Balasubramani, Dimitri Antoniou, et al.
The Journal of Physical Chemistry B (2022) Vol. 127, Iss. 1, pp. 144-150
Closed Access | Times Cited: 8

REVERSIBLE INHIBITORS
Robert A. Copeland
˜The œEnzymes (2023), pp. 317-355
Closed Access | Times Cited: 3

Glycosyltransferases as targets for therapeutic intervention in cancer and inflammation: molecular modeling insights
Igor Tvaroška
Chemical Papers (2022) Vol. 76, Iss. 4, pp. 1953-1988
Closed Access | Times Cited: 6

Hydride Transfer Mechanism of Enzymatic Sugar Nucleotide C2 Epimerization Probed with a Loose-Fit CDP-Glucose Substrate
Christian Rapp, Bernd Nidetzky
ACS Catalysis (2022) Vol. 12, Iss. 12, pp. 6816-6830
Open Access | Times Cited: 6

Mechanism for the rare fluctuation that powers protein conformational change
Shanshan Wu, Ao Ma
The Journal of Chemical Physics (2022) Vol. 156, Iss. 5
Open Access | Times Cited: 5

Temperature-Dependent Low-Frequency Modes in the Active Site of Bovine Carbonic Anhydrase II Probed by 2D-IR Spectroscopy
Julian M. Schmidt-Engler, Sarah von Berg, Jens Bredenbeck
The Journal of Physical Chemistry Letters (2021) Vol. 12, Iss. 32, pp. 7777-7782
Closed Access | Times Cited: 7

Phonon-assisted electron-proton transfer in [FeFe] hydrogenases: Topological role of clusters
Yann Chalopin, Stephen P. Cramer, Simon Arragain
Biophysical Journal (2023) Vol. 122, Iss. 8, pp. 1557-1567
Open Access | Times Cited: 2

Wide Transition-State Ensemble as Key Component for Enzyme Catalysis
Gabriel Ernesto Jara, Francesco Pontiggia, Renee Otten, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2

Dynamics of Ligand Binding to a Rigid Glycosidase**
Fredj Ben Bdira, Christopher A. Waudby, Alexander N. Volkov, et al.
Angewandte Chemie International Edition (2020) Vol. 59, Iss. 46, pp. 20508-20514
Open Access | Times Cited: 6

Multiple Reaction Pathways in the Morphinone Reductase-Catalyzed Hydride Transfer Reaction
Xi Chen, Steven D. Schwartz
ACS Omega (2020) Vol. 5, Iss. 36, pp. 23468-23480
Open Access | Times Cited: 6

Titr-DMD—A Rapid, Coarse-Grained Quasi-All-Atom Constant pH Molecular Dynamics Framework
David J. Reilley, Jian Wang, Nikolay V. Dokholyan, et al.
Journal of Chemical Theory and Computation (2021) Vol. 17, Iss. 7, pp. 4538-4549
Open Access | Times Cited: 6

Energy Bilocalization Effect and the Emergence of Molecular Functions in Proteins
Yann Chalopin, Julien Sparfel
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 6

Solvent Effects on the Temperature Dependence of Hydride Kinetic Isotope Effects: Correlation to the Donor–Acceptor Distances
Pratichhya Adhikari, Meimei Song, Mingxuan Bai, et al.
The Journal of Physical Chemistry A (2022) Vol. 126, Iss. 42, pp. 7675-7686
Closed Access | Times Cited: 4

Allosteric activation unveils protein-mass modulation of ATP phosphoribosyltransferase product release
Benjamin J. Read, John B. O. Mitchell, Rafael G. da Silva
Communications Chemistry (2024) Vol. 7, Iss. 1
Open Access

Interplay of structural preorganization and conformational sampling in UDP-glucuronic acid 4-epimerase catalysis
Christian Rapp, Annika J. E. Borg, Bernd Nidetzky
Nature Communications (2024) Vol. 15, Iss. 1
Open Access

Wide Transition-State Ensemble as Key Component for Enzyme Catalysis
Gabriel Ernesto Jara, Francesco Pontiggia, Renee Otten, et al.
(2024)
Open Access

Substrate Turnover Dynamics Guide Ketol-Acid Reductoisomerase Redesign for Increased Specific Activity
Elijah Karvelis, Chloe Swanson, Bruce Tidor
ACS Catalysis (2024) Vol. 14, Iss. 14, pp. 10491-10509
Open Access

GPCR Signaling: A Study of the Interplay Between Structure, Energy, and Function
Yann Chalopin
Proteins Structure Function and Bioinformatics (2024) Vol. 92, Iss. 12, pp. 1385-1397
Closed Access

Active-Site Glu165 Activation in Triosephosphate Isomerase and Its Deprotonation Kinetics
Hua Deng, R. Brian Dyer, Robert Callender
The Journal of Physical Chemistry B (2019) Vol. 123, Iss. 19, pp. 4230-4241
Open Access | Times Cited: 5

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