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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:

Ca2+-Dependent Inactivation of GluN2A and GluN2B NMDA Receptors Occurs by a Common Kinetic Mechanism
Gary J. Iacobucci, Gabriela Popescu
Biophysical Journal (2019) Vol. 118, Iss. 4, pp. 798-812
Open Access | Times Cited: 26

Showing 1-25 of 26 citing articles:

Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels
Kasper B. Hansen, Lonnie P. Wollmuth, Derek Bowie, et al.
Pharmacological Reviews (2021) Vol. 73, Iss. 4, pp. 1469-1658
Open Access | Times Cited: 445
Impairments of Long-Term Synaptic Plasticity in the Hippocampus of Young Rats during the Latent Phase of the Lithium-Pilocarpine Model of Temporal Lobe Epilepsy
Tatyana Y. Postnikova, Georgy P. Diespirov, Dmitry V. Amakhin, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 24, pp. 13355-13355
Open Access | Times Cited: 31
Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B genes: Insights into NMDA Receptor Structure, Function, and Pathophysiology
Michal Korinek, M C Serra, Fes Abdel Rahman, et al.
Physiological Research (2024), Iss. Suppl 1, pp. S413-S434
Open Access | Times Cited: 4
Zelquistinel acts at an extracellular binding domain to modulate intracellular calcium inactivation of N-methyl-d-aspartate receptors
Xiaolei Zhang, Yong‐Xin Li, Nils Berglund, et al.
Neuropharmacology (2024) Vol. 259, pp. 110100-110100
Open Access | Times Cited: 4
Lithium partially rescues gene expression and enhancer activity from heterozygous knockout of AKAP11 while inducing novel differential changes
Nargess Farhangdoost, Calwing Liao, Yumin Liu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Making time and space for calcium control of neuron activity
Joanna Jędrzejewska‐Szmek, Daniel B. Dormán, Kim T. Blackwell
Current Opinion in Neurobiology (2023) Vol. 83, pp. 102804-102804
Open Access | Times Cited: 10
Selective inhibitor of sodium-calcium exchanger, SEA0400, affects NMDA receptor currents and abolishes their calcium-dependent block by tricyclic antidepressants
Sergei I. Boikov, Т. В. Карелина, Д. А. Сибаров, et al.
Frontiers in Pharmacology (2024) Vol. 15
Open Access | Times Cited: 3
Tricyclic Antidepressant Structure-Related Alterations in Calcium-Dependent Inhibition and Open-Channel Block of NMDA Receptors
Yulia D. Stepanenko, Д. А. Сибаров, Natalia N. Shestakova, et al.
Frontiers in Pharmacology (2022) Vol. 12
Open Access | Times Cited: 13
Calcium- and calmodulin-dependent inhibition of NMDA receptor currents
Gary J. Iacobucci, Gabriela Popescu
Biophysical Journal (2023) Vol. 123, Iss. 3, pp. 277-293
Closed Access | Times Cited: 7
Familial Alzheimer’s disease mutations in amyloid precursor protein impair calcineurin signaling to NMDA receptors
Steven J. Tavalin
Journal of Biological Chemistry (2024) Vol. 301, Iss. 2, pp. 108147-108147
Open Access | Times Cited: 2
Palmitoylation Controls NMDA Receptor Function and Steroid Sensitivity
Pavla Hubálková, Marek Ladislav, Vojtěch Vyklický, et al.
Journal of Neuroscience (2021) Vol. 41, Iss. 10, pp. 2119-2134
Open Access | Times Cited: 16
Allosteric Changes in the NMDA Receptor Associated with Calcium-Dependent Inactivation
Nidhi Kaur Bhatia, Elisa Carrillo, Ryan J. Durham, et al.
Biophysical Journal (2020) Vol. 119, Iss. 11, pp. 2349-2359
Open Access | Times Cited: 16
Regulation of the NMDA receptor by its cytoplasmic domains: (How) is the tail wagging the dog?
Yevheniia Ishchenko, Melissa G Carrizales, Anthony J. Koleske
Neuropharmacology (2021) Vol. 195, pp. 108634-108634
Open Access | Times Cited: 14
Ethanol inhibition of NMDA receptors in calcium-dependent and –independent modes
Sergei I. Boikov, Д. А. Сибаров, С. М. Антонов
Biochemical and Biophysical Research Communications (2019) Vol. 522, Iss. 4, pp. 1046-1051
Open Access | Times Cited: 11
Chemical shift assignments of calmodulin bound to the GluN1 C0 domain (residues 841–865) of the NMDA receptor
Aritra Bej, James B. Ames
Biomolecular NMR Assignments (2023) Vol. 17, Iss. 1, pp. 61-65
Open Access | Times Cited: 3
Altered Calcium Permeability of AMPA Receptor Drives NMDA Receptor Inhibition in the Hippocampus of Murine Obesity Models
Yasuyo Miyagi, Kyoko Fujiwara, Keigo Hikishima, et al.
Molecular Neurobiology (2022) Vol. 59, Iss. 8, pp. 4902-4925
Closed Access | Times Cited: 3
Nutritional and Metabolic Factors, Ethanol and Cholesterol, Interact With Calcium-Dependent N-Methyl-D-Aspartate Receptor Inhibition by Tricyclic Antidepressants
Sergei I. Boikov, Д. А. Сибаров, С. М. Антонов
Frontiers in Cellular Neuroscience (2022) Vol. 16
Open Access | Times Cited: 3
State-specific inhibition of NMDA receptors by memantine depends on intracellular calcium and provides insights into NMDAR channel blocker tolerability
Matthew B. Phillips, Nadya Povysheva, Karen A. Harnett-Scott, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Chemical shift assignments of the α-actinin C-terminal EF-hand domain bound to a cytosolic C0 domain of GluN1 (residues 841–865) from the NMDA receptor
Aritra Bej, Johannes Hell, James B. Ames
Biomolecular NMR Assignments (2024) Vol. 18, Iss. 2, pp. 239-244
Open Access
Research Highlights: Biophysics of Calcium
Henry M. Colecraft
Biophysical Journal (2020) Vol. 119, Iss. 8, pp. 1472-1473
Open Access | Times Cited: 1
Function of Excitatory Periaqueductal Gray Synapses in the Ventral Tegmental Area following Inflammatory Injury
Claire Manning, Michael Fritz, Julie A. Kauer
eNeuro (2022) Vol. 9, Iss. 6, pp. ENEURO.0324-22.2022
Open Access | Times Cited: 1
Chemical shift assignments of calmodulin bound to a cytosolic domain of GluN2A (residues 1004–1024) from the NMDA receptor
Aritra Bej, James B. Ames
Biomolecular NMR Assignments (2023) Vol. 17, Iss. 1, pp. 89-93
Closed Access
FRET-ting over Inactivation
Gabriela Popescu
Biophysical Journal (2020) Vol. 119, Iss. 11, pp. 2139-2140
Open Access
GluN2A Mediated PS-Induced Depressive-Like Behavior Through Ca <sup>2+</sup> Overload Inhibited Myelinization
Huimei Huang, Wei He, Hongli Sun, et al.
SSRN Electronic Journal (2022)
Closed Access
Lab-NMDAR: simuladores de la electrofisiología básica del receptor NMDA
Marleni Reyes Monreal, María Eugenia Pérez Bonilla, Jessica Quintero Pérez, et al.
Acta Universitaria (2022) Vol. 32, pp. 1-23
Open Access
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