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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:

Role of protein dynamics in transmembrane receptor signalling
Yong Wang, Katrine Bugge, Birthe B. Kragelund, et al.
Current Opinion in Structural Biology (2017) Vol. 48, pp. 74-82
Closed Access | Times Cited: 30

Showing 1-25 of 30 citing articles:

New Binding Sites, New Opportunities for GPCR Drug Discovery
H. C. Stephen Chan, Yi Li, Thamani Dahoun, et al.
Trends in Biochemical Sciences (2019) Vol. 44, Iss. 4, pp. 312-330
Open Access | Times Cited: 124
Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding
Jing Yang, Meng Gao, J. Xiong, et al.
Protein Science (2019) Vol. 28, Iss. 11, pp. 1952-1965
Open Access | Times Cited: 76
Kinetic Solvent Viscosity Effects as Probes for Studying the Mechanisms of Enzyme Action
Giovanni Gadda, Pablo Sobrado
Biochemistry (2018) Vol. 57, Iss. 25, pp. 3445-3453
Closed Access | Times Cited: 62
TNF receptors: Structure-function relationships and therapeutic targeting strategies
Chih Hung Lo
Biochimica et Biophysica Acta (BBA) - Biomembranes (2024), pp. 184394-184394
Closed Access | Times Cited: 8
Noncompetitive inhibitors of TNFR1 probe conformational activation states
Chih Hung Lo, Tory Schaaf, Benjamin D. Grant, et al.
Science Signaling (2019) Vol. 12, Iss. 592
Open Access | Times Cited: 50
CD95 Structure, Aggregation and Cell Signaling
Nicolas Levoin, Mickaël Jean, Patrick Legembre
Frontiers in Cell and Developmental Biology (2020) Vol. 8
Open Access | Times Cited: 40
In Situ Monitoring of Membrane Protein Dynamics Using High-Throughput Red-Light-Activated Single-Molecule Tracking
Jinyang Liu, Xuebo Zhang, Bingjie Zhao, et al.
ACS Nano (2025)
Closed Access
Multiply Perturbed Response to Disclose Allosteric Control of Conformational Change: Application to Fluorescent Biosensor Design
Melike Berksöz, Ali Rana Atılgan, Burak Kocuk, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Closed Access
Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR
Cecilia de Agrela Pinto, Deni Mance, Tessa Sinnige, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 30
Dynamics and mechanistic underpinnings to pharmacology of class A GPCRs: an NMR perspective
Shuya Kate Huang, R. Scott Prosser
AJP Cell Physiology (2022) Vol. 322, Iss. 4, pp. C739-C753
Closed Access | Times Cited: 15
Evolutionary shifts in pheromone receptors contribute to speciation in four Helicoverpa species
Song Cao, C. H. Shi, Bing Wang, et al.
Cellular and Molecular Life Sciences (2023) Vol. 80, Iss. 8
Open Access | Times Cited: 9
Fluorescence-Based TNFR1 Biosensor for Monitoring Receptor Structural and Conformational Dynamics and Discovery of Small Molecule Modulators
Chih Hung Lo, Tory Schaaf, David D. Thomas, et al.
Methods in molecular biology (2020), pp. 121-137
Closed Access | Times Cited: 18
All-Atom Simulations Reveal the Intricacies of Signal Transduction upon Binding of the HLA-E Ligand to the Transmembrane Inhibitory CD94/NKG2A Receptor
Martin Ljubič, Eva Prašnikar, Andrej Perdih, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 11, pp. 3486-3499
Open Access | Times Cited: 6
The intracellular lipid-binding domain of human Na+/H+ exchanger 1 forms a lipid-protein co-structure essential for activity
Ruth Hendus‐Altenburger, Jens Vogensen, Emilie S Pedersen, et al.
Communications Biology (2020) Vol. 3, Iss. 1
Open Access | Times Cited: 15
Single-Molecule Fluorescence Techniques for Membrane Protein Dynamics Analysis
Wenlong Yang, Haiqi Xu, Jiayu Wang, et al.
Applied Spectroscopy (2021) Vol. 75, Iss. 5, pp. 491-505
Open Access | Times Cited: 13
Double Monoubiquitination Modifies the Molecular Recognition Properties of p15PAF Promoting Binding to the Reader Module of Dnmt1
Amaia González‐Magaña, Alain Ibáñez de Opakua, Nekane Merino, et al.
ACS Chemical Biology (2019)
Open Access | Times Cited: 14
Dawn of a New Era for Membrane Protein Design
Shahin Sowlati‐Hashjin, Aanshi Gandhi, Michael Garton
BioDesign Research (2022) Vol. 2022
Open Access | Times Cited: 7
Generating Multistate Conformations of P-type ATPases with a Conditional Diffusion Model
Jingtian Xu, Yong Wang
Journal of Chemical Information and Modeling (2024)
Closed Access | Times Cited: 1
Identification of key sites controlling protein functional motions by using elastic network model combined with internal coordinates
Pengfei Zhang, Ji Guo Su
The Journal of Chemical Physics (2019) Vol. 151, Iss. 4
Closed Access | Times Cited: 9
Correction to: A process ontology approach in biochemistry: the case of GPCRs and biosignaling
Fiorela Alassia
Foundations of Chemistry (2023) Vol. 25, Iss. 1, pp. 189-206
Open Access | Times Cited: 3
CD98 regulates the phosphorylation of HER2 and a bispecific anti‐HER2/CD98 antibody inhibits the growth signal of human breast cancer cells
Akitaka Yamasaki, Kumiko Maruyama‐Takahashi, Kento Nishida, et al.
Genes to Cells (2023) Vol. 28, Iss. 5, pp. 374-382
Closed Access | Times Cited: 2
Quantifying Intramolecular Protein Conformational Dynamics Under Lipid Interaction Using smFRET and FCCS
Pei Li, Yawei Dai, Markus Seeger, et al.
Methods in molecular biology (2018), pp. 345-359
Closed Access | Times Cited: 4
Microsecond dynamics in proteins by two-dimensional ESR: Predictions
Pranav Gupta, Zhichun Liang, Jack H. Freed
The Journal of Chemical Physics (2020) Vol. 152, Iss. 21
Open Access | Times Cited: 4
¿Es posible una ontología procesual de las entidades bioquímicas? Consideraciones a partir del caso de los receptores celulares y la señalización celular
Fiorela Alassia
Estudios de Filosofía (2021)
Open Access | Times Cited: 4
A process ontology approach in biochemistry: the case of GPCRs and biosignaling
Fiorela Alassia
Foundations of Chemistry (2022) Vol. 24, Iss. 3, pp. 405-422
Closed Access | Times Cited: 3
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