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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:

Protein post-translational modifications: In silico prediction tools and molecular modeling
Martina Audagnotto, Matteo Dal Peraro
Computational and Structural Biotechnology Journal (2017) Vol. 15, pp. 307-319
Open Access | Times Cited: 175

Showing 1-25 of 175 citing articles:

Post-translational modifications in proteins: resources, tools and prediction methods
Shahin Ramazi, Javad Zahiri
Database (2021) Vol. 2021
Open Access | Times Cited: 524
Functions of the sirtuin deacylase SIRT5 in normal physiology and pathobiology
Surinder Kumar, David B. Lombard
Critical Reviews in Biochemistry and Molecular Biology (2018) Vol. 53, Iss. 3, pp. 311-334
Open Access | Times Cited: 216
Post-translational modifications of Beclin 1 provide multiple strategies for autophagy regulation
Sandra Malmgren Hill, Lidia Wróbel, David C. Rubinsztein
Cell Death and Differentiation (2018) Vol. 26, Iss. 4, pp. 617-629
Open Access | Times Cited: 182
Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?
Joana Costa, Simona L. Bavaro, Sara Benedé, et al.
Clinical Reviews in Allergy & Immunology (2020) Vol. 62, Iss. 1, pp. 37-63
Closed Access | Times Cited: 138
Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?
Joana Costa, Caterina Villa, Kitty Verhoeckx, et al.
Clinical Reviews in Allergy & Immunology (2021) Vol. 62, Iss. 1, pp. 1-36
Open Access | Times Cited: 117
An overview of albumin and alpha-1-acid glycoprotein main characteristics: highlighting the roles of amino acids in binding kinetics and molecular interactions
Michel Bteich
Heliyon (2019) Vol. 5, Iss. 11, pp. e02879-e02879
Open Access | Times Cited: 107
Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases
Elizabeta Madzharova, Philipp Kastl, Fabio Sabino, et al.
International Journal of Molecular Sciences (2019) Vol. 20, Iss. 12, pp. 3077-3077
Open Access | Times Cited: 77
Prediction of bio-sequence modifications and the associations with diseases
Chunyan Ao, Liang Yu, Quan Zou
Briefings in Functional Genomics (2020) Vol. 20, Iss. 1, pp. 1-18
Closed Access | Times Cited: 72
A predictive coarse-grained model for position-specific effects of post-translational modifications
Theodora Myrto Perdikari, Nina Jovic, Gregory L. Dignon, et al.
Biophysical Journal (2021) Vol. 120, Iss. 7, pp. 1187-1197
Open Access | Times Cited: 68
The ubiquitylation of IL-1β limits its cleavage by caspase-1 and targets it for proteasomal degradation
Swarna Lekha Vijayaraj, Rebecca Feltham, Maryam Rashidi, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 60
Modelling Cell Metabolism: A Review on Constraint-Based Steady-State and Kinetic Approaches
Mohammadreza Yasemi, Mario Jolicœur
Processes (2021) Vol. 9, Iss. 2, pp. 322-322
Open Access | Times Cited: 56
Thiol-based Oxidative Posttranslational Modifications (OxiPTMs) of Plant Proteins
Francisco J. Corpas, Salvador González‐Gordo, Marta Rodríguez-Ruiz, et al.
Plant and Cell Physiology (2022) Vol. 63, Iss. 7, pp. 889-900
Open Access | Times Cited: 56
Advances in enrichment methods for mass spectrometry-based proteomics analysis of post-translational modifications
Jessica Brandi, Roberta Noberini, Tiziana Bonaldi, et al.
Journal of Chromatography A (2022) Vol. 1678, pp. 463352-463352
Closed Access | Times Cited: 41
Leveraging transformers‐based language models in proteome bioinformatics
Nguyen Quoc Khanh Le
PROTEOMICS (2023) Vol. 23, Iss. 23-24
Closed Access | Times Cited: 35
Emerging Roles of SIRT5 in Metabolism, Cancer, and SARS-CoV-2 Infection
Emanuele Fabbrizi, Francesco Fiorentino, Vincenzo Carafa, et al.
Cells (2023) Vol. 12, Iss. 6, pp. 852-852
Open Access | Times Cited: 34
The dawn of succinylation: a posttranslational modification
Matthew Alleyn, Mason Breitzig, Richard F. Lockey, et al.
AJP Cell Physiology (2017) Vol. 314, Iss. 2, pp. C228-C232
Open Access | Times Cited: 83
The Many Faces of Rap1 GTPase
Anna Jaśkiewicz, Beata Pająk, Arkadiusz Orzechowski
International Journal of Molecular Sciences (2018) Vol. 19, Iss. 10, pp. 2848-2848
Open Access | Times Cited: 81
Interactions between SARS coronavirus 2 papain‐like protease and immune system: A potential drug target for the treatment of COVID‐19
Shahab Mahmoudvand, Somayeh Shokri
Scandinavian Journal of Immunology (2021) Vol. 94, Iss. 4
Open Access | Times Cited: 40
A small protein coded within the mitochondrial canonical gene nd4 regulates mitochondrial bioenergetics
Laura Kienzle, Stefano Bettinazzi, Thierry Choquette, et al.
BMC Biology (2023) Vol. 21, Iss. 1
Open Access | Times Cited: 17
A Review of Machine Learning and Algorithmic Methods for Protein Phosphorylation Site Prediction
Farzaneh Esmaili, Mahdi Pourmirzaei, Shahin Ramazi, et al.
Genomics Proteomics & Bioinformatics (2023) Vol. 21, Iss. 6, pp. 1266-1285
Open Access | Times Cited: 17
Novel Ectodysplasin-A Variants: Structural and Functional Basis of Hypohidrotic Ectodermal Dysplasia
Prashant Ranjan, Chandra Devi, Rajesh Bansal, et al.
Research Square (Research Square) (2025)
Closed Access
Phosphorylation of tight junction transmembrane proteins: Many sites, much to do
Christina M. Van Itallie, James M. Anderson
Tissue Barriers (2017) Vol. 6, Iss. 1, pp. e1382671-e1382671
Open Access | Times Cited: 60
PTM-ssMP: A Web Server for Predicting Different Types of Post-translational Modification Sites Using Novel Site-specific Modification Profile
Yu Liu, Minghui Wang, Jianing Xi, et al.
International Journal of Biological Sciences (2018) Vol. 14, Iss. 8, pp. 946-956
Open Access | Times Cited: 54
A deep learning method to more accurately recall known lysine acetylation sites
Meiqi Wu, Yingxi Yang, Hui Wang, et al.
BMC Bioinformatics (2019) Vol. 20, Iss. 1
Open Access | Times Cited: 48
New approaches towards the discovery and evaluation of bioactive peptides from natural resources
Nam Joo Kang, Hyeon‐Su Jin, Sung‐Eun Lee, et al.
Critical Reviews in Environmental Science and Technology (2019) Vol. 50, Iss. 1, pp. 72-103
Closed Access | Times Cited: 43
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