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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:

The Transmembrane Domain Mediates Tetramerization of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors
Quan Gan, Jian Dai, Huan‐Xiang Zhou, et al.
Journal of Biological Chemistry (2016) Vol. 291, Iss. 12, pp. 6595-6606
Open Access | Times Cited: 25

Showing 25 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: 459
Structural and Functional Architecture of AMPA-Type Glutamate Receptors and Their Auxiliary Proteins
Ingo H. Greger, Jake F. Watson, Stuart Cull-Candy
Neuron (2017) Vol. 94, Iss. 4, pp. 713-730
Open Access | Times Cited: 336
Channel opening and gating mechanism in AMPA-subtype glutamate receptors
Edward C. Twomey, Maria V. Yelshanskaya, Robert A. Grassucci, et al.
Nature (2017) Vol. 549, Iss. 7670, pp. 60-65
Open Access | Times Cited: 213
Structural Mechanisms of Gating in Ionotropic Glutamate Receptors
Edward C. Twomey, Alexander I. Sobolevsky
Biochemistry (2017) Vol. 57, Iss. 3, pp. 267-276
Open Access | Times Cited: 93
An ER Assembly Line of AMPA-Receptors Controls Excitatory Neurotransmission and Its Plasticity
Jochen Schwenk, Sami Boudkkazi, Maciej K. Kocylowski, et al.
Neuron (2019) Vol. 104, Iss. 4, pp. 680-692.e9
Closed Access | Times Cited: 74
A conserved glycine harboring disease-associated mutations permits NMDA receptor slow deactivation and high Ca2+ permeability
Johansen Amin, Xiaoling Leng, Aaron Gochman, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 54
Divergent roles of a peripheral transmembrane segment in AMPA and NMDA receptors
Johansen Amin, Catherine L. Salussolia, Kelvin Chan, et al.
The Journal of General Physiology (2017) Vol. 149, Iss. 6, pp. 661-680
Open Access | Times Cited: 44
Novel Function of African Swine Fever Virus pE66L in Inhibition of Host Translation by the PKR/eIF2α Pathway
Zhou Shen, Chen Chen, Yilin Yang, et al.
Journal of Virology (2020) Vol. 95, Iss. 5
Open Access | Times Cited: 29
The Role of AMPARs Composition and Trafficking in Synaptic Plasticity and Diseases
Qing-lin Wu, Yan Gao, Juntong Li, et al.
Cellular and Molecular Neurobiology (2021) Vol. 42, Iss. 8, pp. 2489-2504
Closed Access | Times Cited: 27
AMPA Receptor Function in Hypothalamic Synapses
María Royo, Beatriz Aznar Escolano, M. Pilar Madrigal, et al.
Frontiers in Synaptic Neuroscience (2022) Vol. 14
Open Access | Times Cited: 17
N‐glycosylation of the AMPA‐type glutamate receptor regulates cell surface expression and tetramer formation affecting channel function
Munal Babu Kandel, Saki Yamamoto, Ryosuke Midorikawa, et al.
Journal of Neurochemistry (2018) Vol. 147, Iss. 6, pp. 730-747
Open Access | Times Cited: 30
Preferential assembly of heteromeric kainate and AMPA receptor amino terminal domains
Huaying Zhao, Suvendu Lomash, Sagar Chittori, et al.
eLife (2017) Vol. 6
Open Access | Times Cited: 29
Biology of AMPA receptor interacting proteins - From biogenesis to synaptic plasticity
Peter M. Matthews, Alexandra Pinggera, Domen Kampjut, et al.
Neuropharmacology (2021) Vol. 197, pp. 108709-108709
Closed Access | Times Cited: 21
Protein quality control of N-methyl-D-aspartate receptors
Taylor M. Benske, Ting‐Wei Mu, Yajuan Wang
Frontiers in Cellular Neuroscience (2022) Vol. 16
Open Access | Times Cited: 10
GluA1 signal peptide determines the spatial assembly of heteromeric AMPA receptors
Xue‐Yan He, Yanjun Li, Chakrapani Kalyanaraman, et al.
Proceedings of the National Academy of Sciences (2016) Vol. 113, Iss. 38
Open Access | Times Cited: 15
The Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate
O. Kristensen, Lise Baadsgaard Kristensen, Stine Møllerud, et al.
Structure (2016) Vol. 24, Iss. 9, pp. 1582-1589
Open Access | Times Cited: 10
Differential regulation of tetramerization of the AMPA receptor glutamate–gated ion channel by auxiliary subunits
Noele Certain, Quan Gan, Joseph Bennett, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 10, pp. 105227-105227
Open Access | Times Cited: 3
Quantification of AMPA receptor subunits and RNA editing-related proteins in the J20 mouse model of Alzheimer’s disease by capillary western blotting
Luke T. Milham, Gary P. Morris, Lyndsey M. Konen, et al.
Frontiers in Molecular Neuroscience (2024) Vol. 16
Open Access
Time-Dependent Transcriptional Dynamics of Contextual Fear Memory Retrieval Reveals the Function of Dipeptidyl Peptidase 9 in Reconsolidation
Wenting Guo, Wenxing Li, Yuchen Liu, et al.
Neuroscience Bulletin (2024)
Open Access
Distinct Cell Surface Expression Patterns of N-Glycosylation Site Mutants of AMPA-Type Glutamate Receptor under the Homo-Oligomeric Expression Conditions
Jyoji Morise, Saki Yamamoto, Ryosuke Midorikawa, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 14, pp. 5101-5101
Open Access | Times Cited: 2
Analysis of M4 Transmembrane Segments in NMDA Receptor Function: A Negative Allosteric Modulatory Site at the GluN1 M4 is Determining the Efficiency of Neurosteroid Modulation
Kai Langer, Adriana Müller-Längle, Jannik Wempe, et al.
Frontiers in Pharmacology (2021) Vol. 12
Open Access | Times Cited: 1
Analysis of M4 transmembrane domains in NMDA receptor function: a negative allosteric modulation site at the GluN1 M4 is determining the efficiency of neurosteroid modulation
Kai Langer, Adriana Müller-Längle, Jannik Wempe, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 1
Differential regulation of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) receptor tetramerization by auxiliary subunits
Noele Certain, Quan Gan, Joseph Bennett, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Open Practices Disclosure
Armand Chatard
(2017)
Closed Access
α-Amino-3-Hydroxy-5-Methyl-4-Isoxazolepropionic Acid and Kainate Receptors
G. Brent Dawe, Patricia M.G.E. Brown, Derek Bowie
Oxford University Press eBooks (2020), pp. 291-342
Closed Access
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