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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:

Post-translational modifications in proteins: resources, tools and prediction methods
Shahin Ramazi, Javad Zahiri
Database (2021) Vol. 2021
Open Access | Times Cited: 532

Showing 51-75 of 532 citing articles:

Post-translational modifications in kidney diseases and associated cardiovascular risk
Heidi Noels, Vera Jankowski, Stefan Schunk, et al.
Nature Reviews Nephrology (2024) Vol. 20, Iss. 8, pp. 495-512
Closed Access | Times Cited: 10
Nanopore: Emerging for detecting protein post-translational modifications
Xinjia Zhao, Haijuan Qin, Mingliang Tang, et al.
TrAC Trends in Analytical Chemistry (2024) Vol. 173, pp. 117658-117658
Closed Access | Times Cited: 9
Citric Acid: A Nexus Between Cellular Mechanisms and Biomaterial Innovations
Hui Xu, Yan Su, Ethan Gerhard, et al.
Advanced Materials (2024) Vol. 36, Iss. 32
Open Access | Times Cited: 8
Bacterial protein acetylation: mechanisms, functions, and methods for study
Jocelin Rizo, Sergio Encarnación
Frontiers in Cellular and Infection Microbiology (2024) Vol. 14
Open Access | Times Cited: 8
Towards highly sensitive deep learning-based end-to-end database search for tandem mass spectrometry
Yonghan Yu, Ming Li
Nature Machine Intelligence (2025)
Closed Access | Times Cited: 1
A review on omics-based biomarkers discovery for Alzheimer's disease from the bioinformatics perspectives: Statistical approach vs machine learning approach
Mei Sze Tan, Phaik‐Leng Cheah, Ai‐Vyrn Chin, et al.
Computers in Biology and Medicine (2021) Vol. 139, pp. 104947-104947
Closed Access | Times Cited: 48
Biomarkers in Neurodegenerative Diseases: Proteomics Spotlight on ALS and Parkinson’s Disease
Rekha Raghunathan, Kathleen Turajane, Li Chin Wong
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 16, pp. 9299-9299
Open Access | Times Cited: 36
Characterisation of NLRP3 pathway-related neuroinflammation in temporal lobe epilepsy
Malin S. Pohlentz, Philipp Müller, Silvia Cases‐Cunillera, et al.
PLoS ONE (2022) Vol. 17, Iss. 8, pp. e0271995-e0271995
Open Access | Times Cited: 31
LMPhosSite: A Deep Learning-Based Approach for General Protein Phosphorylation Site Prediction Using Embeddings from the Local Window Sequence and Pretrained Protein Language Model
Subash C. Pakhrin, Suresh Pokharel, Pawel Pratyush, et al.
Journal of Proteome Research (2023) Vol. 22, Iss. 8, pp. 2548-2557
Closed Access | Times Cited: 20
Proteome‐wide lysine acetylation profiling to investigate the involvement of histone deacetylase HDA5 in the salt stress response of Arabidopsis leaves
Priyadarshini Tilak, Florian Kotnik, Guillaume Née, et al.
The Plant Journal (2023) Vol. 115, Iss. 1, pp. 275-292
Open Access | Times Cited: 19
S-Palmitoylation of Synaptic Proteins in Neuronal Plasticity in Normal and Pathological Brains
Anna Buszka, Agata Pytyś, Domnic Colvin, et al.
Cells (2023) Vol. 12, Iss. 3, pp. 387-387
Open Access | Times Cited: 18
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
Sequence-based prediction of the intrinsic solubility of peptides containing non-natural amino acids
Marc Oeller, Ryan Kang, Hannah L. Bolt, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 17
How aberrant N-glycosylation can alter protein functionality and ligand binding: An atomistic view
Matteo Castelli, Pengrong Yan, Anna Rodina, et al.
Structure (2023) Vol. 31, Iss. 8, pp. 987-1004.e8
Open Access | Times Cited: 16
Proximity-inducing modalities: the past, present, and future
Sameek Singh, Wenzhi Tian, Zachary C. Severance, et al.
Chemical Society Reviews (2023) Vol. 52, Iss. 16, pp. 5485-5515
Closed Access | Times Cited: 16
Lectins as potential tools for cancer biomarker discovery from extracellular vesicles
Md. Khirul Islam, Misba Khan, Kamlesh Gidwani, et al.
Biomarker Research (2023) Vol. 11, Iss. 1
Open Access | Times Cited: 16
The logic of protein post‐translational modifications (PTMs): Chemistry, mechanisms and evolution of protein regulation through covalent attachments
Marcin J. Suskiewicz
BioEssays (2024) Vol. 46, Iss. 3
Open Access | Times Cited: 7
Advance computational tools for multiomics data learning
Sheikh Mansoor, Saira Hamid, Thai Thanh Tuan, et al.
Biotechnology Advances (2024) Vol. 77, pp. 108447-108447
Closed Access | Times Cited: 7
Lectin-Mimicking Aptamer as a Generic Glycan Receptor for Sensitive Detection of Glycoproteins Associated with Cancer
Inés Díaz-Martínez, Rebeca Miranda‐Castro, Noemı́ de-los-Santos-Álvarez, et al.
Analytical Chemistry (2024)
Open Access | Times Cited: 6
Genetic Encoding of Phosphorylated Amino Acids into Proteins
Michael Allen, P. Andrew Karplus, Ryan A. Mehl, et al.
Chemical Reviews (2024) Vol. 124, Iss. 10, pp. 6592-6642
Closed Access | Times Cited: 6
TRIM28 in cancer and cancer therapy
Kailang Li, Haifeng Wang, Bitao Jiang, et al.
Frontiers in Genetics (2024) Vol. 15
Open Access | Times Cited: 6
Post-translational modification prediction via prompt-based fine-tuning of a GPT-2 model
Palistha Shrestha, Jeevan Kandel, Hilal Tayara, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
Cellular Site-Specific Incorporation of Noncanonical Amino Acids in Synthetic Biology
Wei Niu, Jiantao Guo
Chemical Reviews (2024) Vol. 124, Iss. 18, pp. 10577-10617
Closed Access | Times Cited: 6
Epigenetic Effects of Resveratrol on Oncogenic Signaling in Breast Cancer
Lucinda Kurzava Kendall, Yuexi Ma, T.Y. Yang, et al.
Nutrients (2024) Vol. 16, Iss. 5, pp. 699-699
Open Access | Times Cited: 5
A review of factors affecting the structure, compositions, and the techno-functionalities of bovine milk fat globule and membrane
Yanjun Sun, Yrjö H. Roos, Song Miao
Trends in Food Science & Technology (2024) Vol. 150, pp. 104570-104570
Closed Access | Times Cited: 5

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