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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:

Investigation of the impact of PTMs on the protein backbone conformation
Pierrick Craveur, Tarun Narwani, Joseph Rebehmed, et al.
Amino Acids (2019) Vol. 51, Iss. 7, pp. 1065-1079
Open Access | Times Cited: 20

Showing 20 citing articles:

Mini-review: Recent advances in post-translational modification site prediction based on deep learning
Lingkuan Meng, Wai‐Sum Chan, Lei Huang, et al.
Computational and Structural Biotechnology Journal (2022) Vol. 20, pp. 3522-3532
Open Access | Times Cited: 31
Protein diversification through post-translational modifications, alternative splicing, and gene duplication
Yonathan Goldtzvik, Neeladri Sen, Su Datt Lam, et al.
Current Opinion in Structural Biology (2023) Vol. 81, pp. 102640-102640
Open Access | Times Cited: 19
FuncPhos-STR: An integrated deep neural network for functional phosphosite prediction based on AlphaFold protein structure and dynamics
Guangyu Zhang, Cai Zhang, Mingyue Cai, et al.
International Journal of Biological Macromolecules (2024) Vol. 266, pp. 131180-131180
Closed Access | Times Cited: 6
Drug design targeting active posttranslational modification protein isoforms
Fanwang Meng, Zhongjie Liang, Kehao Zhao, et al.
Medicinal Research Reviews (2020) Vol. 41, Iss. 3, pp. 1701-1750
Closed Access | Times Cited: 42
Citrullination of TDP-43 is a key post-translation modification associated with structural and functional changes and progressive pathology in TDP-43 mouse models and human proteinopathies
Christopher P. Saunders, Patricia Rocha-Rangel, Rohan Desai, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Closed Access
Protein phosphorylation database and prediction tools
Mingxiao Zhao, Qiang Chen, Fulai Li, et al.
Briefings in Bioinformatics (2023) Vol. 24, Iss. 2
Closed Access | Times Cited: 12
Current status of PTMs structural databases: applications, limitations and prospects
Alexandre G. de Brevern, Joseph Rebehmed
Amino Acids (2022) Vol. 54, Iss. 4, pp. 575-590
Closed Access | Times Cited: 17
A structural entropy index to analyse local conformations in intrinsically disordered proteins
Akhila Melarkode Vattekatte, Tarun Narwani, Aline Floch, et al.
Journal of Structural Biology (2020) Vol. 210, Iss. 1, pp. 107464-107464
Open Access | Times Cited: 18
Catalytic activity regulation through post-translational modification: the expanding universe of protein diversity
Michael Kokkinidis, Nicholas M. Glykos, Vasiliki E. Fadouloglou
Advances in protein chemistry and structural biology (2020), pp. 97-125
Open Access | Times Cited: 18
Dynamics of Post-Translational Modification Inspires Drug Design in the Kinase Family
Huimin Zhang, Jixiao He, Guang Hu, et al.
Journal of Medicinal Chemistry (2021) Vol. 64, Iss. 20, pp. 15111-15125
Closed Access | Times Cited: 17
Significance of Type II Collagen Posttranslational Modifications: From Autoantigenesis to Improved Diagnosis and Treatment of Rheumatoid Arthritis
Tsvetelina Batsalova, Balik Dzhambazov
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 12, pp. 9884-9884
Open Access | Times Cited: 6
Ammonia stress affects the structure and function of hemocyanin in Penaeus vannamei
Mingming Zhao, Jude Juventus Aweya, Qian Feng, et al.
Ecotoxicology and Environmental Safety (2022) Vol. 241, pp. 113827-113827
Open Access | Times Cited: 10
Pyranose Ring Puckering Thermodynamics for Glycan Monosaccharides Associated with Vertebrate Proteins
Olgun Guvench, Devon Martin, Megan Greene
International Journal of Molecular Sciences (2021) Vol. 23, Iss. 1, pp. 473-473
Open Access | Times Cited: 14
The pattern of apolipoprotein A-I lysine carbamylation reflects its lipidation state and the chemical environment within human atherosclerotic aorta
Shawna Battle, Valentin Gogonea, Belinda Willard, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 4, pp. 101832-101832
Open Access | Times Cited: 9
PPICT: an integrated deep neural network for predicting inter-protein PTM cross-talk
Fei Zhu, Lei Deng, Yuhao Dai, et al.
Briefings in Bioinformatics (2023) Vol. 24, Iss. 2
Open Access | Times Cited: 5
Machine Learning for Prediction of Drug Targets in Microbe Associated Cardiovascular Diseases by Incorporating Host‐pathogen Interaction Network Parameters
N. L. Singh, Sonika Bhatnagar
Molecular Informatics (2021) Vol. 41, Iss. 3
Closed Access | Times Cited: 12
Analysis of Protein Disorder Predictions in the Light of a Protein Structural Alphabet
Alexandre G. de Brevern
Biomolecules (2020) Vol. 10, Iss. 7, pp. 1080-1080
Open Access | Times Cited: 11
Analysis of Structural Changes in the Protein near the Phosphorylation Site
Kirill S. Nikolsky, Liudmila I. Kulikova, Denis V. Petrovskiy, et al.
Biomolecules (2023) Vol. 13, Iss. 11, pp. 1564-1564
Open Access | Times Cited: 3
Imidazole-amino acids. Conformational switch under tautomer and pH change
Monika Staś, Piotr Najgebauer, Dawid Siodłak
Research Square (Research Square) (2022)
Open Access
Imidazole-amino acids. Conformational switch under tautomer and pH change
Monika Staś, Piotr Najgebauer, Dawid Siodłak
Amino Acids (2022) Vol. 55, Iss. 1, pp. 33-49
Open Access
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