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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:

Accurate Identification of Deamidation and Citrullination from Global Shotgun Proteomics Data Using a Dual-Search Delta Score Strategy
Xi Wang, Adam Swensen, Tong Zhang, et al.
Journal of Proteome Research (2020) Vol. 19, Iss. 4, pp. 1863-1872
Open Access | Times Cited: 21

Showing 21 citing articles:

Interferon-α promotes HLA-B-restricted presentation of conventional and alternative antigens in human pancreatic β-cells
Alexia Carré, Fatoumata Samassa, Zhicheng Zhou, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Deep Learning Enhances Precision of Citrullination Identification in Human and Plant Tissue Proteomes
Wassim Gabriel, Roxana González, Sophia Laposchan, et al.
Molecular & Cellular Proteomics (2025), pp. 100924-100924
Open Access
Citrullination and PAD Enzyme Biology in Type 1 Diabetes – Regulators of Inflammation, Autoimmunity, and Pathology
Meiling Yang, Fernanda Marques Câmara Sodré, Mark J. Mamula, et al.
Frontiers in Immunology (2021) Vol. 12
Open Access | Times Cited: 33
Mass Spectrometry-Based Precise Identification of Citrullinated Histones via Limited Digestion and Biotin Derivative Tag Enrichment
Bin Wang, Zihui Li, Yatao Shi, et al.
Analytical Chemistry (2024) Vol. 96, Iss. 6, pp. 2309-2317
Closed Access | Times Cited: 2
Characterization of Citrullination Sites in Neutrophils and Mast Cells Activated by Ionomycin via Integration of Mass Spectrometry and Machine Learning
Raghothama Chaerkady, Yebin Zhou, Jared A. Delmar, et al.
Journal of Proteome Research (2021) Vol. 20, Iss. 6, pp. 3150-3164
Closed Access | Times Cited: 13
A Streamlined Data Analysis Pipeline for the Identification of Sites of Citrullination
Aaron Maurais, Ari J. Salinger, Micaela Tobin, et al.
Biochemistry (2021) Vol. 60, Iss. 38, pp. 2902-2914
Open Access | Times Cited: 11
Characterizing citrullination by mass spectrometry-based proteomics
Alexandra K.L.F.S. Rebak, Ivo A. Hendriks, Michael L. Nielsen
Philosophical Transactions of the Royal Society B Biological Sciences (2023) Vol. 378, Iss. 1890
Open Access | Times Cited: 4
Identification of Deamidated Peptides in Cytokine-Exposed MIN6 Cells through LC−MS/MS Using a Shortened Digestion Time and Inspection of MS2 Spectra
Aïsha Callebaut, Rita Derua, S Vig, et al.
Journal of Proteome Research (2020) Vol. 20, Iss. 2, pp. 1405-1414
Open Access | Times Cited: 10
Peptidylarginine deiminase enzymes and citrullinated proteins in female reproductive physiology and associated diseases
Amanda O. Christensen, Guangyuan Li, Coleman H. Young, et al.
Biology of Reproduction (2022) Vol. 107, Iss. 6, pp. 1395-1410
Open Access | Times Cited: 7
12-Plex DiLeu Isobaric Labeling Enabled High-Throughput Investigation of Citrullination Alterations in the DNA Damage Response
Zihui Li, Bin Wang, Qinying Yu, et al.
Analytical Chemistry (2022) Vol. 94, Iss. 7, pp. 3074-3081
Open Access | Times Cited: 6
Statistical Modeling for Enhancing the Discovery Power of Citrullination from Tandem Mass Spectrometry Data
Sunghyun Huh, Daehee Hwang, Min‐Sik Kim
Analytical Chemistry (2020) Vol. 92, Iss. 19, pp. 12975-12986
Closed Access | Times Cited: 7
Enabling Global Analysis of Protein Citrullination via Biotin Thiol Tag-Assisted Mass Spectrometry
Yatao Shi, Zihui Li, Bin Wang, et al.
Analytical Chemistry (2022) Vol. 94, Iss. 51, pp. 17895-17903
Open Access | Times Cited: 4
Recent advances in characterization of citrullination and its implication in human disease research: From method development to network integration
Bin Wang, Lauren Fields, Lingjun Li
PROTEOMICS (2022) Vol. 23, Iss. 21-22
Open Access | Times Cited: 4
Deep Learning Enhances Precision of Citrullination Identification in Human and Plant Tissue Proteomes
Wassim Gabriel, Roxana González, Sophia Laposchan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Pitfalls and Solutions in Mass Spectrometry-Based Identification of Protein Glycation
Wendong Ma, Irene Ang, Kate M. K. Lei, et al.
Analytical Chemistry (2023) Vol. 95, Iss. 3, pp. 1829-1837
Closed Access | Times Cited: 1
Citrullination of matrisomal proteins in health and diseases
Mohd Aslam Saifi, I‐Cheng Ho
Philosophical Transactions of the Royal Society B Biological Sciences (2023) Vol. 378, Iss. 1890
Open Access | Times Cited: 1
Human Hepatic Transporter Signature Peptides for Quantitative Targeted Absolute Proteomics: Selection, Digestion Efficiency, and Peptide Stability
Ayano Mori, Takeshi Masuda, Shingo Ito, et al.
Pharmaceutical Research (2022) Vol. 39, Iss. 11, pp. 2965-2978
Closed Access | Times Cited: 2
Characterization and use of the ECV304 autoantigenic citrullinome to understand anti-citrullinated protein/peptide autoantibodies in rheumatoid arthritis
Natália Regine de França, Henri A. Ménard, Maximilien Lora, et al.
Arthritis Research & Therapy (2022) Vol. 24, Iss. 1
Open Access | Times Cited: 1
Enabling global analysis of protein citrullination and homocitrullination via biotin thiol tag-assisted mass spectrometry
Lingjun Li, Yatao Shi, Zihui Li, et al.
Research Square (Research Square) (2022)
Open Access | Times Cited: 1
Interferon-α promotes neo-antigen formation and preferential HLA-B-restricted antigen presentation in pancreatic β-cells
Alexia Carré, Zhicheng Zhou, Javier Perez-Hernandez, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Enabling global analysis of protein citrullination and homocitrullination via biotin thiol tag-assisted mass spectrometry
Lingjun Li, Yatao Shi, Zihui Li, et al.
Research Square (Research Square) (2021)
Open Access
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