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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:

Exploring cellular biochemistry with nanobodies
Ross W. Cheloha, Thibault J. Harmand, Charlotte Wijne, et al.
Journal of Biological Chemistry (2020) Vol. 295, Iss. 45, pp. 15307-15327
Open Access | Times Cited: 82

Showing 1-25 of 82 citing articles:

A Detailed Overview of Immune Escape, Antibody Escape, Partial Vaccine Escape of SARS-CoV-2 and Their Emerging Variants With Escape Mutations
Chiranjib Chakraborty, Ashish Ranjan Sharma, Manojit Bhattacharya, et al.
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 122
Neutralization of SARS‐CoV‐2 by highly potent, hyperthermostable, and mutation‐tolerant nanobodies
Thomas Güttler, Metin Aksu, Antje Dickmanns, et al.
The EMBO Journal (2021) Vol. 40, Iss. 19
Open Access | Times Cited: 89
Proteomes Are of Proteoforms: Embracing the Complexity
Katrina Carbonara, Martin Andonovski, Jens R. Coorssen
Proteomes (2021) Vol. 9, Iss. 3, pp. 38-38
Open Access | Times Cited: 78
Single-domain near-infrared protein provides a scaffold for antigen-dependent fluorescent nanobodies
Olena S. Oliinyk, Mikhail Baloban, Charles L. Clark, et al.
Nature Methods (2022) Vol. 19, Iss. 6, pp. 740-750
Open Access | Times Cited: 42
Site-Specific Protein Labeling and Generation of Defined Ubiquitin-Protein Conjugates Using an Asparaginyl Endopeptidase
Maximilian Fottner, Johannes Heimgärtner, Maximilian Gantz, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 29, pp. 13118-13126
Open Access | Times Cited: 39
Nanobodies asin vivo, non-invasive, imaging agents
Thibault J. Harmand, Ashraful Islam, Novalia Pishesha, et al.
RSC Chemical Biology (2021) Vol. 2, Iss. 3, pp. 685-701
Open Access | Times Cited: 41
Protein visualization and manipulation in Drosophila through the use of epitope tags recognized by nanobodies
Jun Xu, Ah‐Ram Kim, Ross W. Cheloha, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 36
Nanobodies as molecular imaging probes
Sarah Barakat, Melike Berksöz, Pegah Zahedimaram, et al.
Free Radical Biology and Medicine (2022) Vol. 182, pp. 260-275
Closed Access | Times Cited: 35
Accelerating GPCR Drug Discovery With Conformation-Stabilizing VHHs
Toon Laeremans, Zara A. Sands, Pieter Claes, et al.
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 34
Application Progress of the Single Domain Antibody in Medicine
Huaping Tang, Yuan Gao, Jiangyuan Han
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 4, pp. 4176-4176
Open Access | Times Cited: 22
Highly biased agonism for GPCR ligands via nanobody tethering
Shivani Sachdev, Brendan A. Creemer, Thomas J. Gardella, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
30 years of nanobodies – an ongoing success story of small binders in biological research
Desiree I. Frecot, Theresa Froehlich, Ulrich Rothbauer
Journal of Cell Science (2023) Vol. 136, Iss. 21
Open Access | Times Cited: 14
Generation of nanobodies from transgenic ‘LamaMice’ lacking an endogenous immunoglobulin repertoire
Thomas Watts Eden, Alessa Z. Schaffrath, Janusz Wesolowski, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 5
A bifunctional protein RANbody based on nanobody facilitates dual-mode immunoassay of Staphylococcal enterotoxin B in food samples
Yao Zhang, Yuhuan Li, Min Li, et al.
Sensors and Actuators B Chemical (2024) Vol. 418, pp. 136295-136295
Closed Access | Times Cited: 5
Development of a V5-tag–directed nanobody and its implementation as an intracellular biosensor of GPCR signaling
Manel Zeghal, Kevin Matte, Angelica Venes, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 9, pp. 105107-105107
Open Access | Times Cited: 12
Functionalized Protein Binders in Developmental Biology
Sophie T. Schnider, M Viganò, Markus Affolter, et al.
Annual Review of Cell and Developmental Biology (2024) Vol. 40, Iss. 1, pp. 119-142
Closed Access | Times Cited: 4
Generation of Site‐Specifically Labeled Affinity Reagents via Use of a Self‐Labeling Single Domain Antibody
Stanley Fayn, Swarnali Roy, Chino C. Cabalteja, et al.
Advanced Science (2025)
Open Access
Computational electrostatic engineering of nanobodies for enhanced SARS−CoV−2 receptor binding domain recognition
Zafar Iqbal, Muhammad Asim, Umair Khan, et al.
Frontiers in Molecular Biosciences (2025) Vol. 12
Open Access
Asparaginyl Ligase-Catalyzed One-Step Cell Surface Modification of Red Blood Cells
Thibault J. Harmand, Novalia Pishesha, Fabian B. H. Rehm, et al.
ACS Chemical Biology (2021) Vol. 16, Iss. 7, pp. 1201-1207
Closed Access | Times Cited: 26
Protein manipulation using single copies of short peptide tags in cultured cells and in Drosophila melanogaster
M Viganò, Clara-Maria Ell, Manuela M. M. Kustermann, et al.
Development (2021) Vol. 148, Iss. 6
Open Access | Times Cited: 25
Selective Targeting of Nanobody-Modified Gold Nanoparticles to Distinct Cell Types
Yoon Ho Lee, Himadri Medhi, Xin Liu, et al.
ACS Applied Materials & Interfaces (2023) Vol. 15, Iss. 51, pp. 59258-59268
Closed Access | Times Cited: 10
A checkpoint function for Nup98 in nuclear pore formation suggested by novel inhibitory nanobodies
Mireia Solà Colom, Zhenglin Fu, Philip Gunkel, et al.
The EMBO Journal (2024) Vol. 43, Iss. 11, pp. 2198-2232
Open Access | Times Cited: 3
Characterization of a Nanobody-Epitope Tag Interaction and Its Application for Receptor Engineering
Chino C. Cabalteja, Shivani Sachdev, Ross W. Cheloha
ACS Chemical Biology (2022) Vol. 17, Iss. 8, pp. 2296-2303
Open Access | Times Cited: 15
A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure
Sarah A. Nordeen, Kasper R. Andersen, Kevin E. Knockenhauer, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 23
AAV Vector-Mediated Antibody Delivery (A-MAD) in the Central Nervous System
Marika Marino, Matthew G. Holt
Frontiers in Neurology (2022) Vol. 13
Open Access | Times Cited: 13
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