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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:

Analytical Guidelines for co-fractionation Mass Spectrometry Obtained through Global Profiling of Gold Standard Saccharomyces cerevisiae Protein Complexes
Chi Nam Ignatius Pang, Sara Ballouz, Daniel Weissberger, et al.
Molecular & Cellular Proteomics (2020) Vol. 19, Iss. 11, pp. 1876-1895
Open Access | Times Cited: 18

Showing 18 citing articles:

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
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
CEDAR, an online resource for the reporting and exploration of complexome profiling data
Joeri van Strien, Alexander Haupt, Uwe Schulte, et al.
Biochimica et Biophysica Acta (BBA) - Bioenergetics (2021) Vol. 1862, Iss. 7, pp. 148411-148411
Open Access | Times Cited: 38
Alternative proteoforms and proteoform-dependent assemblies in humans and plants
Claire D. McWhite, Wisath Sae-Lee, Yaning Yuan, et al.
Molecular Systems Biology (2024) Vol. 20, Iss. 8, pp. 933-951
Open Access | Times Cited: 5
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
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
Closing the protein gap in plant chronobiology
Devang Mehta, Johanna Krahmer, R. Glen Uhrig
The Plant Journal (2021) Vol. 106, Iss. 6, pp. 1509-1522
Open Access | Times Cited: 13
Co-fractionation–mass spectrometry to characterize native mitochondrial protein assemblies in mammalian neurons and brain
Mara Zilocchi, Matineh Rahmatbakhsh, Mohamed Taha Moutaoufik, et al.
Nature Protocols (2023) Vol. 18, Iss. 12, pp. 3918-3973
Closed Access | Times Cited: 5
Don't let go: co‐fractionation mass spectrometry for untargeted mapping of protein–metabolite interactomes
Dennis Schlossarek, Youjun Zhang, Ewelina Sokołowska, et al.
The Plant Journal (2022) Vol. 113, Iss. 5, pp. 904-914
Open Access | Times Cited: 6
CEDAR, an online resource for the reporting and exploration of complexome profiling data
Joeri van Strien, Alexander Haupt, Uwe Schulte, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 6
Expanding interactome analyses beyond model eukaryotes
Katherine James, Anil Wipat, Simon Cockell
Briefings in Functional Genomics (2022) Vol. 21, Iss. 4, pp. 243-269
Open Access | Times Cited: 4
Native Size-Exclusion Chromatography–Based Mass Spectrometry Reveals New Components of the Early Heat Shock Protein 90 Inhibition Response Among Limited Global Changes
Rahul S. Samant, Sílvia Batista, Mark Larance, et al.
Molecular & Cellular Proteomics (2022) Vol. 22, Iss. 2, pp. 100485-100485
Open Access | Times Cited: 4
Proteomic applications in identifying protein-protein interactions
Benjamin T. Veenstra, Timothy D. Veenstra
Advances in protein chemistry and structural biology (2023)
Closed Access | Times Cited: 1
Alternative proteoforms and proteoform-dependent assemblies in humans and plants
Claire D. McWhite, Wisath Sae-Lee, Yaning Yuan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 2
Native size exclusion chromatography-based mass spectrometry (SEC-MS) identifies novel components of the Heat Shock Protein 90-dependent proteome
Rahul S. Samant, Sílvia Batista, Mark Larance, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Closed Access | Times Cited: 1
A machine learning-based approach to identify reliable gold standards for protein complex composition prediction
Pengcheng Yang, Youngwoo Lee, Daniel B. Szymanski, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Expanding Interactome Analyses beyond Model Eukaryotes
Katherine James, Anil Wipat, Simon Cockell
(2021)
Open Access
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