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:

Mechanistic roles for altered O-GlcNAcylation in neurodegenerative disorders
Aaron T. Balana, Matthew R. Pratt
Biochemical Journal (2021) Vol. 478, Iss. 14, pp. 2733-2758
Open Access | Times Cited: 42

Showing 1-25 of 42 citing articles:

Altered glucose metabolism in Alzheimer's disease: Role of mitochondrial dysfunction and oxidative stress
Saikat Dewanjee, Pratik Chakraborty, Hiranmoy Bhattacharya, et al.
Free Radical Biology and Medicine (2022) Vol. 193, pp. 134-157
Closed Access | Times Cited: 108

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

Emerging roles of O-glycosylation in regulating protein aggregation, phase separation, and functions
Xiang Li, Pinou Lv, Yifei Du, et al.
Current Opinion in Chemical Biology (2023) Vol. 75, pp. 102314-102314
Closed Access | Times Cited: 21

Integration of O-GlcNAc into Stress Response Pathways
Kamau Fahie, Kyriakos N. Papanicolaou, Natasha E. Zachara
Cells (2022) Vol. 11, Iss. 21, pp. 3509-3509
Open Access | Times Cited: 32

Glycosidase-targeting small molecules for biological and therapeutic applications
Yujun Kim, Hui Li, JooHee Choi, et al.
Chemical Society Reviews (2023) Vol. 52, Iss. 20, pp. 7036-7070
Closed Access | Times Cited: 15

Understanding and exploiting the roles of O-GlcNAc in neurodegenerative diseases
Matthew R. Pratt, David J. Vocadlo
Journal of Biological Chemistry (2023) Vol. 299, Iss. 12, pp. 105411-105411
Open Access | Times Cited: 15

The Misfolding Mystery: α-syn and the Pathogenesis of Parkinson's Disease
Samir Negi, Navneet Khurana, Navneet Duggal
Neurochemistry International (2024) Vol. 177, pp. 105760-105760
Closed Access | Times Cited: 5

Neuronal activity-driven O-GlcNAcylation promotes mitochondrial plasticity
Seungyoon B. Yu, Haoming Wang, Richard G. Sánchez, et al.
Developmental Cell (2024) Vol. 59, Iss. 16, pp. 2143-2157.e9
Open Access | Times Cited: 5

Low glucose induced Alzheimer's disease‐like biochemical changes in human induced pluripotent stem cell‐derived neurons is due to dysregulated O‐GlcNAcylation
Chia‐Wei Huang, Nicholas C. Rust, Hsueh‐Fu Wu, et al.
Alzheimer s & Dementia (2023) Vol. 19, Iss. 11, pp. 4872-4885
Open Access | Times Cited: 11

Protein glycosylation and glycoinformatics for novel biomarker discovery in neurodegenerative diseases
Júlia Costa, Catherine Hayes, Frédérique Lisacek
Ageing Research Reviews (2023) Vol. 89, pp. 101991-101991
Open Access | Times Cited: 11

Targeting protein aggregation for the treatment of neurodegenerative diseases
Qingchao Li, Wei Pan, Jun Zhou, et al.
Medicine Plus (2024) Vol. 1, Iss. 1, pp. 100005-100005
Open Access | Times Cited: 3

Neurodevelopmental defects in a mouse model of O-GlcNAc transferase intellectual disability
Florence Authier, Nina Ondrušková, Andrew T. Ferenbach, et al.
Disease Models & Mechanisms (2024) Vol. 17, Iss. 4
Open Access | Times Cited: 3

Organization of a functional glycolytic metabolon on mitochondria for metabolic efficiency
Haoming Wang, John Vant, Andrew Zhang, et al.
Nature Metabolism (2024) Vol. 6, Iss. 9, pp. 1712-1735
Closed Access | Times Cited: 3

Phage display uncovers a sequence motif that drives polypeptide binding to a conserved regulatory exosite of O-GlcNAc transferase
Matthew G. Alteen, Richard W. Meek, Subramania Kolappan, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 42
Open Access | Times Cited: 10

Altered O-GlcNAcylation and mitochondrial dysfunction, a molecular link between brain glucose dysregulation and sporadic Alzheimer’s disease
Gerald W. Hart, Chia‐Wei Huang, NicholasC Rust, et al.
Neural Regeneration Research (2022) Vol. 18, Iss. 4, pp. 779-779
Open Access | Times Cited: 15

O-GlcNAc modification forces the formation of an α-Synuclein amyloid-strain with notably diminished seeding activity and pathology
Aaron T. Balana, Anne‐Laure Mahul‐Mellier, Binh A. Nguyen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 8

Discovery of 4-(Arylethynyl)piperidine Derivatives as Potent Nonsaccharide O-GlcNAcase Inhibitors for the Treatment of Alzheimer’s Disease
Zihan Cheng, Nianying Shang, Xiaoyu Wang, et al.
Journal of Medicinal Chemistry (2024) Vol. 67, Iss. 16, pp. 14292-14312
Closed Access | Times Cited: 2

O‐GlcNAc modification of HSP27 alters its protein interactions and promotes refolding of proteins through the BAG3/HSP70 co‐chaperone
Afraah Javed, Oleta T. Johnson, Aaron T. Balana, et al.
Protein Science (2024) Vol. 33, Iss. 10
Open Access | Times Cited: 2

O-GlcNAcylation is crucial for sympathetic neuron development, maintenance, functionality and contributes to peripheral neuropathy
Hsueh‐Fu Wu, Chia‐Wei Huang, Jennifer Art, et al.
Frontiers in Neuroscience (2023) Vol. 17
Open Access | Times Cited: 6

Acute inhibition of OGA sex-dependently alters the networks associated with bioenergetics, autophagy, and neurodegeneration
Nha Van Huynh, Gloria A. Benavides, Michelle S. Johnson, et al.
Molecular Brain (2022) Vol. 15, Iss. 1
Open Access | Times Cited: 9

Neuronal activity-driven O-GlcNAcylation promotes mitochondrial plasticity
Seungyoon B. Yu, Richard G. Sánchez, Zachary D. Papich, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 5

The Cerebrospinal Fluid Free-Glycans Hex1 and HexNAc1Hex1Neu5Ac1 as Potential Biomarkers of Alzheimer’s Disease
Lynn Krüger, Karina Biskup, Carola G. Schipke, et al.
Biomolecules (2024) Vol. 14, Iss. 5, pp. 512-512
Open 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

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