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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:

PCprophet: a framework for protein complex prediction and differential analysis using proteomic data
Andrea Fossati, Chen Li, Federico Uliana, et al.
Nature Methods (2021) Vol. 18, Iss. 5, pp. 520-527
Closed Access | Times Cited: 52

Showing 1-25 of 52 citing articles:

Analysis of DIA proteomics data using MSFragger-DIA and FragPipe computational platform
Fengchao Yu, Guo Ci Teo, Andy T. Kong, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 121
Protein interaction landscapes revealed by advanced in vivo cross-linking–mass spectrometry
Andrew Wheat, Clinton Yu, Xiaorong Wang, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 32
Open Access | Times Cited: 118
Protein complexes in cells by AI‐assisted structural proteomics
Francis J. O’Reilly, Andrea Graziadei, Christian Forbrig, et al.
Molecular Systems Biology (2023) Vol. 19, Iss. 4
Open Access | Times Cited: 97
Spatial multi-omics: deciphering technological landscape of integration of multi-omics and its applications
Xiaojie Liu, Ting Peng, Miaochun Xu, et al.
Journal of Hematology & Oncology (2024) Vol. 17, Iss. 1
Open Access | Times Cited: 18
Positive-unlabeled learning in bioinformatics and computational biology: a brief review
Fuyi Li, Shuangyu Dong, André Leier, et al.
Briefings in Bioinformatics (2021) Vol. 23, Iss. 1
Closed Access | Times Cited: 57
DIP-MS: ultra-deep interaction proteomics for the deconvolution of protein complexes
Fabian Frommelt, Andrea Fossati, Federico Uliana, et al.
Nature Methods (2024) Vol. 21, Iss. 4, pp. 635-647
Open Access | Times Cited: 14
Tapioca: a platform for predicting de novo protein–protein interactions in dynamic contexts
Tavis. J. Reed, Matthew D. Tyl, Alicja Tadych, et al.
Nature Methods (2024) Vol. 21, Iss. 3, pp. 488-500
Closed Access | Times Cited: 11
Systematic identification of structure-specific protein–protein interactions
Aleš Holfeld, Dina Schuster, Fabian Sesterhenn, et al.
Molecular Systems Biology (2024) Vol. 20, Iss. 6, pp. 651-675
Open Access | Times Cited: 11
Mapping protein–protein interactions by mass spectrometry
Xiaonan Liu, Lawrence Abad, Lopamudra Chatterjee, et al.
Mass Spectrometry Reviews (2024)
Open Access | Times Cited: 10
Meta-analysis defines principles for the design and analysis of co-fractionation mass spectrometry experiments
Michael A. Skinnider, Leonard J. Foster
Nature Methods (2021) Vol. 18, Iss. 7, pp. 806-815
Closed Access | Times Cited: 55
Next-generation proteomics for quantitative Jumbophage-bacteria interaction mapping
Andrea Fossati, Deepto Mozumdar, Claire Kokontis, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 20
Advances in spatial proteomics: Mapping proteome architecture from protein complexes to subcellular localizations
Lisa M. Breckels, Charlotte Hutchings, Kishor D. Ingole, et al.
Cell chemical biology (2024) Vol. 31, Iss. 9, pp. 1665-1687
Open Access | Times Cited: 7
The complex machinery of human cobalamin metabolism
Thomas J. McCorvie, Douglas Ferreira, Wyatt W. Yue, et al.
Journal of Inherited Metabolic Disease (2023) Vol. 46, Iss. 3, pp. 406-420
Open Access | Times Cited: 15
Rapid Profiling of Protein Complex Reorganization in Perturbed Systems
Isabell Bludau, Charlotte Nicod, Claudia Martelli, et al.
Journal of Proteome Research (2023) Vol. 22, Iss. 5, pp. 1520-1536
Open Access | Times Cited: 15
State of the interactomes: an evaluation of molecular networks for generating biological insights
Sarah N. Wright, Scott Colton, Leah V. Schaffer, et al.
Molecular Systems Biology (2024)
Closed Access | Times Cited: 5
Phosphorylation‐linked complex profiling identifies assemblies required for Hippo signal integration
Federico Uliana, Rodolfo Ciuffa, Ranjan Mishra, et al.
Molecular Systems Biology (2023) Vol. 19, Iss. 4
Open Access | Times Cited: 13
Mapping the Multiscale Proteomic Organization of Cellular and Disease Phenotypes
Anthony J. Cesnik, Leah V. Schaffer, Ishan Gaur, et al.
Annual Review of Biomedical Data Science (2024) Vol. 7, Iss. 1, pp. 369-389
Open Access | Times Cited: 4
Protein complexes in cells by AI-assisted structural proteomics
Francis J. O’Reilly, Andrea Graziadei, Christian Forbrig, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 17
SEC-MX: an approach to systematically study the interplay between protein assembly states and phosphorylation
Ella Doron‐Mandel, Benjamin J. Bokor, Yanzhe Ma, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
EndoMAPV1, a Structural Protein Complex Landscape of Human Endosomes
Miguel A. Gonzalez‐Lozano, E. Schmid, Enya Miguel Whelan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Mass Spectrometry‐Based Proteomics Technologies to Define Endogenous Protein‐Protein Interactions and Their Applications to Cancer and Viral Infectious Diseases
Clinton Yu, Rithika Adavikolanu, Robyn M. Kaake, et al.
Mass Spectrometry Reviews (2025)
Closed Access
Progress toward a comprehensive brain protein interactome
Vy Dang, Brittney Voigt, Edward M. Marcotte
Biochemical Society Transactions (2025) Vol. 53, Iss. 01
Closed Access
Integration of data‐independent acquisition (DIA) with co‐fractionation mass spectrometry (CF‐MS) to enhance interactome mapping capabilities
Brenna N. Hay, Mopelola O. Akinlaja, Teesha C Baker, et al.
PROTEOMICS (2023) Vol. 23, Iss. 21-22
Open Access | Times Cited: 9
Enabling cryo‐EM density interpretation from yeast native cell extracts by proteomics data and AlphaFold structures
Christian Tüting, Lisa Schmidt, Ioannis Skalidis, et al.
PROTEOMICS (2023) Vol. 23, Iss. 17
Open Access | Times Cited: 8
Trends in co-fractionation mass spectrometry: A new gold-standard in global protein interaction network discovery
Raghuveera Kumar Goel, Nazmin Bithi, Andrew Emili
Current Opinion in Structural Biology (2024) Vol. 88, pp. 102880-102880
Open Access | Times Cited: 3
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