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:

Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them
Justin M. Westerfield, Francisco N. Barrera
Journal of Biological Chemistry (2019) Vol. 295, Iss. 7, pp. 1792-1814
Open Access | Times Cited: 58

Showing 1-25 of 58 citing articles:

Modulation of FGF pathway signaling and vascular differentiation using designed oligomeric assemblies
Natasha I. Edman, Ashish Phal, Rachel L. Redler, et al.
Cell (2024) Vol. 187, Iss. 14, pp. 3726-3740.e43
Open Access | Times Cited: 20

Scaling Protein–Water Interactions in the Martini 3 Coarse-Grained Force Field to Simulate Transmembrane Helix Dimers in Different Lipid Environments
Ainara Claveras Cabezudo, Christina Athanasiou, Alexandros Tsengenes, et al.
Journal of Chemical Theory and Computation (2023) Vol. 19, Iss. 7, pp. 2109-2119
Open Access | Times Cited: 33

Importance of integrin transmembrane helical interactions for antagonistic versus agonistic ligand behavior: Consequences for medical applications
Ute Reuning, Vincenzo Maria D’Amore, Kairbaan Hodivala‐Dilke, et al.
Bioorganic Chemistry (2025) Vol. 156, pp. 108193-108193
Closed Access | Times Cited: 1

Notch in mechanotransduction – from molecular mechanosensitivity to tissue mechanostasis
Oscar M. J. A. Stassen, Tommaso Ristori, Cecilia Sahlgren
Journal of Cell Science (2020) Vol. 133, Iss. 24
Open Access | Times Cited: 55

Membranes on the move: The functional role of the extracellular vesicle membrane for contact‐dependent cellular signalling
Kevin Jahnke, Oskar Staufer
Journal of Extracellular Vesicles (2024) Vol. 13, Iss. 4
Open Access | Times Cited: 8

AlphaFold2 enables accurate deorphanization of ligands to single-pass receptors
Niels Banhos Danneskiold‐Samsøe, Deniz Kavi, Kevin M. Jude, et al.
Cell Systems (2024) Vol. 15, Iss. 11, pp. 1046-1060.e3
Closed Access | Times Cited: 8

ASGR1 and Its Enigmatic Relative, CLEC10A
J. Kenneth Hoober
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 14, pp. 4818-4818
Open Access | Times Cited: 43

Spatially modulated ephrinA1:EphA2 signaling increases local contractility and global focal adhesion dynamics to promote cell motility
Zhongwen Chen, Dongmyung Oh, Kabir H. Biswas, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 25
Open Access | Times Cited: 43

Elucidation and refinement of synthetic receptor mechanisms
Hailey I. Edelstein, Patrick S. Donahue, Joseph J. Muldoon, et al.
Synthetic Biology (2020) Vol. 5, Iss. 1
Open Access | Times Cited: 33

AlphaFold2 enables accurate deorphanization of ligands to single-pass receptors
Niels Banhos Danneskiold‐Samsøe, Deniz Kavi, Kevin M. Jude, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 11

Conversion of natural cytokine receptors into orthogonal synthetic biosensors
Hailey I. Edelstein, Amparo Cosio, M Ezekiel, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4

PIP2 promotes conformation-specific dimerization of the EphA2 membrane region
Katherine M. Stefanski, C. Russell, Justin M. Westerfield, et al.
Journal of Biological Chemistry (2020) Vol. 296, pp. 100149-100149
Open Access | Times Cited: 32

Cryo-electron Microscopic Analysis of Single-Pass Transmembrane Receptors
Kai Cai, Xuewu Zhang, Xiao‐chen Bai
Chemical Reviews (2022) Vol. 122, Iss. 17, pp. 13952-13988
Open Access | Times Cited: 17

De novo-designed transmembrane proteins bind and regulate a cytokine receptor
Marco Mravic, Li He, Huong T. Kratochvil, et al.
Nature Chemical Biology (2024) Vol. 20, Iss. 6, pp. 751-760
Open Access | Times Cited: 3

Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells?
Camille Albrecht, Aline Appert-Collin, Dominique Bagnard, et al.
Frontiers in Oncology (2020) Vol. 10
Open Access | Times Cited: 26

Strategies for Site‐Specific Labeling of Receptor Proteins on the Surfaces of Living Cells by Using Genetically Encoded Peptide Tags
Philipp Wolf, Georgina C. Gavins, Annette G. Beck‐Sickinger, et al.
ChemBioChem (2021) Vol. 22, Iss. 10, pp. 1717-1732
Open Access | Times Cited: 21

Recent Advances in Functional Nanomaterials for Diagnostic and Sensing Using Self-Assembled Monolayers
Caroline R. Basso, Bruno P. Crulhas, Gustavo R. Castro, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 13, pp. 10819-10819
Open Access | Times Cited: 9

Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors
Amita R. Sahoo, Matthias Buck
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 16, pp. 8593-8593
Open Access | Times Cited: 18

Conformational Clamping by a Membrane Ligand Activates the EphA2 Receptor
Justin M. Westerfield, Amita R. Sahoo, Daiane S. Alves, et al.
Journal of Molecular Biology (2021) Vol. 433, Iss. 18, pp. 167144-167144
Open Access | Times Cited: 17

Transmembrane Peptides as a New Strategy to Inhibit Neuraminidase-1 Activation
Camille Albrecht, Andrey S. Kuznetsov, Aline Appert-Collin, et al.
Frontiers in Cell and Developmental Biology (2020) Vol. 8
Open Access | Times Cited: 17

Modulation of FGF pathway signaling and vascular differentiation using designed oligomeric assemblies
Natasha I. Edman, Rachel L. Redler, Ashish Phal, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 6

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