Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

The Role of Post-Translational Modifications on the Structure and Function of Tau Protein
Haiqiong Ye, Yue Han, Ping Li, et al.
Journal of Molecular Neuroscience (2022) Vol. 72, Iss. 8, pp. 1557-1571
Closed Access | Times Cited: 41

Showing 1-25 of 41 citing articles:

Intrinsically Disordered Proteins: An Overview
Rakesh Trivedi, Hampapathalu Adimurthy Nagarajaram
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 22, pp. 14050-14050
Open Access | Times Cited: 98
Inflammatory aspects of Alzheimer’s disease
Pablo Botella Lucena, Michael T. Heneka
Acta Neuropathologica (2024) Vol. 148, Iss. 1
Closed Access | Times Cited: 13
Temperature-Dependent Aggregation of Tau Protein Is Attenuated by Native PLGA Nanoparticles Under in vitro Conditions
Pallabi Sil Paul, Mallesh Rathnam, Aria Khalili, et al.
International Journal of Nanomedicine (2025) Vol. Volume 20, pp. 1999-2019
Open Access | Times Cited: 1
Specific post-translational modifications of soluble tau protein distinguishes Alzheimer’s disease and primary tauopathies
Nathalie Kyalu Ngoie Zola, Clémence Balty, Sébastien Pyr dit Ruys, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 38
Alzheimer's disease: The role of proteins in formation, mechanisms, and new therapeutic approaches
Amirreza Gholami
Neuroscience Letters (2023) Vol. 817, pp. 137532-137532
Closed Access | Times Cited: 21
The multiple facets of acetyl-CoA metabolism: Energetics, biosynthesis, regulation, acylation and inborn errors
Youlin Wang, Hao Yang, Chloé Geerts, et al.
Molecular Genetics and Metabolism (2022) Vol. 138, Iss. 1, pp. 106966-106966
Closed Access | Times Cited: 28
Nature's toolbox against tau aggregation: An updated review of current research
Sumaiya Khan, Md. Imtaiyaz Hassan, Mohammad Shahid, et al.
Ageing Research Reviews (2023) Vol. 87, pp. 101924-101924
Closed Access | Times Cited: 17
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: 17
Post-Translational Modifications in Tau and Their Roles in Alzheimer's Pathology
Subha Kalyaanamoorthy, Stanley Opare, Xiaoxiao Xu, et al.
Current Alzheimer Research (2024) Vol. 21, Iss. 1, pp. 24-49
Closed Access | Times Cited: 5
Impact of Phosphorylation and O-GlcNAcylation on the Binding Affinity of R4 Tau Peptide to Microtubule and Its Conformational Preference upon Dissociation
Sathish Dasari, Subha Kalyaanamoorthy
Journal of Chemical Information and Modeling (2025)
Closed Access
O-GlcNAc modification differentially regulates microtubule binding and pathological conformations of tau isoforms in vitro
Mohammed M. Alhadidy, Paul M. Stemmer, Nicholas M. Kanaan
Journal of Biological Chemistry (2025) Vol. 301, Iss. 3, pp. 108263-108263
Closed Access
Tau biomarkers for Neurodegenerative Diseases: current state and perspectives
Elena Vacchi, Iñigo Ruiz‐Barrio, Giorgia Melli
Parkinsonism & Related Disorders (2025), pp. 107772-107772
Closed Access
Impaired mitochondrial dynamics and removal of the damaged mitochondria in diabetic retinopathy
Kumari Alka, J. Kumar, Renu A. Kowluru
Frontiers in Endocrinology (2023) Vol. 14
Open Access | Times Cited: 14
Anti-amyloid-β Antibodies and Anti-tau Therapies for Alzheimer’s Disease: Recent Advances and Perspectives
Naoyuki Suzuki, T. Hatta, Mana Ito, et al.
Chemical and Pharmaceutical Bulletin (2024) Vol. 72, Iss. 7, pp. 602-609
Open Access | Times Cited: 4
Liquid − liquid phase separation of tau: Driving forces, regulation, and biological implications
Ping Li, Jingxin Chen, Xi Wang, et al.
Neurobiology of Disease (2023) Vol. 183, pp. 106167-106167
Open Access | Times Cited: 11
Modulation of Tau Pathology in Alzheimer’s Disease by Dietary Bioactive Compounds
Huahua Shi, Yan Zhao
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 2, pp. 831-831
Open Access | Times Cited: 3
Liquid–liquid phase separation in diseases
Xinyue Zhang, Yuan Lin, Wanlu Zhang, et al.
MedComm (2024) Vol. 5, Iss. 7
Open Access | Times Cited: 3
The effect of Tau K677 lactylation on ferritinophagy and ferroptosis in Alzheimer's disease
Xiaoqiong An, Jun He, Peng Xie, et al.
Free Radical Biology and Medicine (2024) Vol. 224, pp. 685-706
Open Access | Times Cited: 3
Gut-brain axis and Alzheimer's disease: Therapeutic interventions and strategies
Hetender Singh, Chirag Chopra, Hemender Singh, et al.
Journal of Functional Foods (2023) Vol. 112, pp. 105915-105915
Open Access | Times Cited: 8
Biochemical approaches to assess the impact of post-translational modifications on pathogenic tau conformations using recombinant protein
Mohammed M. Alhadidy, Nicholas M. Kanaan
Biochemical Society Transactions (2024) Vol. 52, Iss. 1, pp. 301-318
Open Access | Times Cited: 2
Tannic acid as a biphasic modulator of tau protein liquid–liquid phase separation
Jiani Xiang, Jingxin Chen, Yanqing Liu, et al.
International Journal of Biological Macromolecules (2024) Vol. 275, pp. 133578-133578
Closed Access | Times Cited: 2
Untangling Tau: Molecular Insights into Neuroinflammation, Pathophysiology, and Emerging Immunotherapies
Ryder Davidson, Reese I. Krider, Philip Borsellino, et al.
Current Issues in Molecular Biology (2023) Vol. 45, Iss. 11, pp. 8816-8839
Open Access | Times Cited: 7
Heparan Sulfate Proteoglycans in Tauopathy
Yanan Zhu, Lauren Gandy, Fuming Zhang, et al.
Biomolecules (2022) Vol. 12, Iss. 12, pp. 1792-1792
Open Access | Times Cited: 11
Drug Target to Alleviate Mitochondrial Dysfunctions in Alzheimer’s Disease: Recent Advances and Therapeutic Implications
Md. Ataur Rahman, MD. Hasanur Rahman, Hyewhon Rhim, et al.
Current Neuropharmacology (2024) Vol. 22, Iss. 12, pp. 1942-1959
Closed Access | Times Cited: 1
The role and mechanism of SUMO modification in liver disease
Mengxue Li, Jingrong Zhang, Zihao Li, et al.
Biomedicine & Pharmacotherapy (2024) Vol. 177, pp. 116898-116898
Open Access | Times Cited: 1
Page 1 - Next Page

Scroll to top