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:

O-GlcNAc forces an α-synuclein amyloid strain with notably diminished seeding and pathology
Aaron T. Balana, Anne‐Laure Mahul‐Mellier, Binh A. Nguyen, et al.
Nature Chemical Biology (2024) Vol. 20, Iss. 5, pp. 646-655
Open Access | Times Cited: 24

Showing 24 citing articles:

Investigation of All Disease-Relevant Lysine Acetylation Sites in α-Synuclein Enabled by Non-canonical Amino Acid Mutagenesis
Marie Shimogawa, Minghao Li, Grace Park, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Mechanically Triggered Protein Desulfurization
Dongyang Han, Yan Cui, Xiangyu Deng, et al.
Journal of the American Chemical Society (2025)
Closed Access
Binding adaptability of chemical ligands to polymorphic α-synuclein amyloid fibrils
Kaien Liu, Youqi Tao, Qinyue Zhao, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 35
Closed Access | Times Cited: 2
A Versatile Method for Site-Specific Chemical Installation of Aromatic Posttranslational Modification Analogs into Proteins
Xiaoxi Lin, Shaswati Mandal, Raj V. Nithun, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 37, pp. 25788-25798
Open Access | Times Cited: 2
Current insights and assumptions on α-synuclein in Lewy body disease
Rehana K. Leak, Rachel N. Clark, Muslim Abbas, et al.
Acta Neuropathologica (2024) Vol. 148, Iss. 1
Open Access | Times Cited: 1
Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases
Arpine Sokratian, Zhou Ye, Meltem Tatlı, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Cryo-EM structures of pathogenic fibrils and their impact on neurodegenerative disease research
Tiffany W. Todd, Naeyma N. Islam, Casey Cook, et al.
Neuron (2024) Vol. 112, Iss. 14, pp. 2269-2288
Closed Access | Times Cited: 1
O-GlcNAc Modification of α-Synuclein Can Alter Monomer Dynamics to Control Aggregation Kinetics
Kasun Gamage, Binyou Wang, Eldon R. Hard, et al.
ACS Chemical Neuroscience (2024) Vol. 15, Iss. 16, pp. 3044-3052
Open Access | Times Cited: 1
Posttranslational Modifications ofα-Synuclein, Their Therapeutic Potential, and Crosstalk in Health and Neurodegenerative Diseases
Kambiz Hassanzadeh, Jun Liu, Santhosh Chandar Maddila, et al.
Pharmacological Reviews (2024) Vol. 76, Iss. 6, pp. 1254-1290
Closed Access | Times Cited: 1
Navigating the Neurobiology of Parkinson’s: The Impact and Potential of α-Synuclein
Erlandas Paulėkas, Tadas Vanagas, Saulius Lagunavičius, et al.
Biomedicines (2024) Vol. 12, Iss. 9, pp. 2121-2121
Open Access | Times Cited: 1
Post-translational Modification of α-Synuclein Modifies Monomer Dynamics and Aggregation Kinetics
Kasun Gamage, Binyou Wang, Eldon R. Hard, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Engineered reactivity of a bacterial E1-like enzyme enables ATP-driven modification of protein C termini
Clara L. Frazier, Debashrito Deb, Amy M. Weeks
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Effect of host and strain factors on α-synuclein prion pathogenesis
Amanda L. Woerman, Jason C. Bartz
Trends in Neurosciences (2024) Vol. 47, Iss. 7, pp. 538-550
Closed Access
1.94 Angstrom structure of synthetic alpha-synuclein fibrils seeding MSA neuropathology
Domenic Burger, Marianna Kashyrina, Amanda J. Lewis, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access
Solid-state NMR assignment of α-synuclein polymorph prepared from helical intermediate
Sahil Ahlawat, Surabhi Mehra, Chandrakala M. Gowda, et al.
Biomolecular NMR Assignments (2024) Vol. 18, Iss. 2, pp. 193-200
Open Access
Selective detection of alpha synuclein amyloid fibrils by faradaic and non-faradaic electrochemical impedance spectroscopic approaches
Hussaini Adam, Subash C. B. Gopinath, Hemavathi Krishnan, et al.
Bioelectrochemistry (2024) Vol. 161, pp. 108800-108800
Closed Access
From Fringe to the Mainstream: How ETD MS brought O-GlcNAc to the masses
Namrata D. Udeshi, Gerald W. Hart, Chad Slawson
Molecular & Cellular Proteomics (2024), pp. 100859-100859
Open Access
Liquid–liquid phase separation and conformational strains of α-Synuclein: implications for Parkinson’s disease pathogenesis
Eva D. Ruiz-Ortega, Anna Wilkaniec, Agata Adamczyk
Frontiers in Molecular Neuroscience (2024) Vol. 17
Open Access
The post-translational modification O-GlcNAc is a sensor and regulator of metabolism
Murielle M. Morales, Matthew R. Pratt
Open Biology (2024) Vol. 14, Iss. 10
Open Access
Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases
Arpine Sokratian, Ye Zhou, Meltem Tatlı, et al.
Science Advances (2024) Vol. 10, Iss. 44
Open Access
Opportunities for Therapeutic Modulation of O-GlcNAc
Steven S. Cheng, Alison Mody, Christina M. Woo
Chemical Reviews (2024) Vol. 124, Iss. 22, pp. 12918-13019
Closed Access
Protein aggregation in health and disease: A looking glass of two faces
Guilherme C. de Andrade, Michelle F. Mota, Dinarte N. Moreira-Ferreira, et al.
Advances in protein chemistry and structural biology (2024)
Closed Access
Uncovering the intricacies of O-GlcNAc modification in cognitive impairment: New insights from regulation to therapeutic targeting
Jianhui Wang, Ning Jiang, Feng Liu, et al.
Pharmacology & Therapeutics (2024), pp. 108761-108761
Closed Access
From onset to advancement: the temporal spectrum of α-synuclein in synucleinopathies
James A. Wiseman, Kreesan Reddy, Birger Victor Dieriks
Ageing Research Reviews (2024), pp. 102640-102640
Open Access
How is the Amyloid Fold Built? Polymorphism and the Microscopic Mechanisms of Fibril Assembly
Liam D. Aubrey, Sheena E. Radford
(2024)
Closed Access
Page 1

Scroll to top