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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:

Getting to know the neighborhood: using proximity-dependent biotinylation to characterize protein complexes and map organelles
Anne‐Claude Gingras, Kento T. Abe, Brian Raught
Current Opinion in Chemical Biology (2018) Vol. 48, pp. 44-54
Closed Access | Times Cited: 278

Showing 1-25 of 278 citing articles:

Deciphering molecular interactions by proximity labeling
Wei Qin, Kelvin F. Cho, P. Cavanagh, et al.
Nature Methods (2021) Vol. 18, Iss. 2, pp. 133-143
Open Access | Times Cited: 436
A proximity-dependent biotinylation map of a human cell
Christopher D. Go, James D.R. Knight, Archita Rajasekharan, et al.
Nature (2021) Vol. 595, Iss. 7865, pp. 120-124
Open Access | Times Cited: 375
Properties of Stress Granule and P-Body Proteomes
Ji‐Young Youn, Boris J.A. Dyakov, Jianping Zhang, et al.
Molecular Cell (2019) Vol. 76, Iss. 2, pp. 286-294
Open Access | Times Cited: 364
Proximity labeling in mammalian cells with TurboID and split-TurboID
Kelvin F. Cho, Tess C. Branon, Namrata D. Udeshi, et al.
Nature Protocols (2020) Vol. 15, Iss. 12, pp. 3971-3999
Closed Access | Times Cited: 313
Recent advances in mass spectrometry based clinical proteomics: applications to cancer research
Andrew Macklin, Shahbaz Khan, Thomas Kislinger
Clinical Proteomics (2020) Vol. 17, Iss. 1
Open Access | Times Cited: 248
Modulating biomolecular condensates: a novel approach to drug discovery
Diana M. Mitrea, Matthäus Mittasch, Beatriz Ferreira Gomes, et al.
Nature Reviews Drug Discovery (2022) Vol. 21, Iss. 11, pp. 841-862
Open Access | Times Cited: 236
The emerging role of mass spectrometry-based proteomics in drug discovery
Felix Meissner, Jennifer Geddes‐McAlister, Matthias Mann, et al.
Nature Reviews Drug Discovery (2022) Vol. 21, Iss. 9, pp. 637-654
Closed Access | Times Cited: 234
Proximity labeling of protein complexes and cell-type-specific organellar proteomes in Arabidopsis enabled by TurboID
Andrea Mair, Shou‐Ling Xu, Tess C. Branon, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 217
Proteomic and interactomic insights into the molecular basis of cell functional diversity
Isabell Bludau, Ruedi Aebersold
Nature Reviews Molecular Cell Biology (2020) Vol. 21, Iss. 6, pp. 327-340
Closed Access | Times Cited: 215
A high-stringency blueprint of the human proteome
Subash Adhikari, Edouard C. Nice, Eric W. Deutsch, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 199
Proximity Dependent Biotinylation: Key Enzymes and Adaptation to Proteomics Approaches
Payman Samavarchi‐Tehrani, Reuben Samson, Anne‐Claude Gingras
Molecular & Cellular Proteomics (2020) Vol. 19, Iss. 5, pp. 757-773
Open Access | Times Cited: 174
Understudied proteins: opportunities and challenges for functional proteomics
Georg Kustatscher, Tom Collins, Anne‐Claude Gingras, et al.
Nature Methods (2022) Vol. 19, Iss. 7, pp. 774-779
Open Access | Times Cited: 164
A High-Density Human Mitochondrial Proximity Interaction Network
Hana Antonická, Zhen‐Yuan Lin, Alexandre Janer, et al.
Cell Metabolism (2020) Vol. 32, Iss. 3, pp. 479-497.e9
Open Access | Times Cited: 163
The Human Protein Atlas—Spatial localization of the human proteome in health and disease
Andreas Digre, Cecilia Lindskog
Protein Science (2020) Vol. 30, Iss. 1, pp. 218-233
Open Access | Times Cited: 158
Mapping the proximity interaction network of the Rho-family GTPases reveals signalling pathways and regulatory mechanisms
Halil Bagci, Neera Sriskandarajah, Amélie Robert, et al.
Nature Cell Biology (2019) Vol. 22, Iss. 1, pp. 120-134
Closed Access | Times Cited: 156
Engineering of ultraID, a compact and hyperactive enzyme for proximity-dependent biotinylation in living cells
Lea Kubitz, Sebastian Bitsch, Xiyan Zhao, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 75
Mapping the signaling network of BIN2 kinase using TurboID-mediated biotin labeling and phosphoproteomics
Tae‐Wuk Kim, Chan Ho Park, Chuan‐Chih Hsu, et al.
The Plant Cell (2023) Vol. 35, Iss. 3, pp. 975-993
Open Access | Times Cited: 57
Recruitment of FBXO22 for targeted degradation of NSD2
Yan Nie, John R. Tabor, Jianping Li, et al.
Nature Chemical Biology (2024) Vol. 20, Iss. 12, pp. 1597-1607
Closed Access | Times Cited: 19
Proteomics: An In‐Depth Review on Recent Technical Advances and Their Applications in Biomedicine
Jing Liang, Jun Tian, Huadong Zhang, et al.
Medicinal Research Reviews (2025)
Closed Access | Times Cited: 2
Turn and Face the Strange: A New View on Phosphatases
Maja Köhn
ACS Central Science (2020) Vol. 6, Iss. 4, pp. 467-477
Open Access | Times Cited: 109
A SARS-CoV-2 – host proximity interactome
Payman Samavarchi‐Tehrani, Hala Abdouni, James D.R. Knight, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 108
Proximity‐dependent labeling methods for proteomic profiling in living cells: An update
Justin A. Bosch, Chiao‐Lin Chen, Norbert Perrimon
Wiley Interdisciplinary Reviews Developmental Biology (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 98
Subcellular proteomics
Josie A. Christopher, Charlotte Stadler, Claire E. Martin, et al.
Nature Reviews Methods Primers (2021) Vol. 1, Iss. 1
Open Access | Times Cited: 94
Recent progress in mass spectrometry-based strategies for elucidating protein–protein interactions
Teck Yew Low, Saiful Effendi Syafruddin, M. Aiman Mohtar, et al.
Cellular and Molecular Life Sciences (2021) Vol. 78, Iss. 13, pp. 5325-5339
Open Access | Times Cited: 89
Global BioID-based SARS-CoV-2 proteins proximal interactome unveils novel ties between viral polypeptides and host factors involved in multiple COVID19-associated mechanisms
Estelle Laurent, Yorgos Sofianatos, Anastassia V. Komarova, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 83
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