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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:

OGT (O-GlcNAc Transferase) Selectively Modifies Multiple Residues Unique to Lamin A
Dan N. Simon, Amanda Wriston, Qiong Fan, et al.
Cells (2018) Vol. 7, Iss. 5, pp. 44-44
Open Access | Times Cited: 20

Showing 20 citing articles:

Lamina-associated domains: peripheral matters and internal affairs
Nolwenn Briand, Philippe Collas
Genome biology (2020) Vol. 21, Iss. 1
Open Access | Times Cited: 215
Analytical and Biochemical Perspectives of Protein O-GlcNAcylation
Junfeng Ma, Ci Wu, Gerald W. Hart
Chemical Reviews (2021) Vol. 121, Iss. 3, pp. 1513-1581
Closed Access | Times Cited: 132
Lamins: The backbone of the nucleocytoskeleton interface
Joan M. Sobo, Nicholas S. Alagna, Sean X. Sun, et al.
Current Opinion in Cell Biology (2024) Vol. 86, pp. 102313-102313
Open Access | Times Cited: 20
Functional mechanisms and abnormalities of the nuclear lamina
Adam Karoutas, Asifa Akhtar
Nature Cell Biology (2021) Vol. 23, Iss. 2, pp. 116-126
Closed Access | Times Cited: 71
Post-Translational Modification of Lamins: Mechanisms and Functions
Mingyue Zheng, Guoxiang Jin, Zhongjun Zhou
Frontiers in Cell and Developmental Biology (2022) Vol. 10
Open Access | Times Cited: 29
Lamin post-translational modifications: emerging toggles of nuclear organization and function
Laura A. Murray‐Nerger, Ileana M. Cristea
Trends in Biochemical Sciences (2021) Vol. 46, Iss. 10, pp. 832-847
Open Access | Times Cited: 24
The Hunt lab weighs in on mass spectrometry-based analysis of protein post-translational modifications
Joshua J. Coon, Jarrod A. Marto, John E. P. Syka, et al.
Molecular & Cellular Proteomics (2025), pp. 100943-100943
Open Access
O-GlcNAc modifications regulate lamin A tail processing
Katherine Augspurger, Elizabeth I. Martin, Jason C. Maynard, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Ultradeep O-GlcNAc proteomics reveals widespread O-GlcNAcylation on tyrosine residues of proteins
Chunyan Hou, Jun Deng, Ci Wu, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 47
Open Access | Times Cited: 3
Genotype‐phenotype analysis ofLMNA‐related diseases predicts phenotype‐selective alterations in lamin phosphorylation
Eric W. Lin, Graham F. Brady, Raymond Kwan, et al.
The FASEB Journal (2020) Vol. 34, Iss. 7, pp. 9051-9073
Open Access | Times Cited: 22
Emerin Is Required for Proper Nucleus Reassembly after Mitosis: Implications for New Pathogenetic Mechanisms for Laminopathies Detected in EDMD1 Patients
Magda Dubińska–Magiera, Katarzyna Kozioł, Magdalena Machowska, et al.
Cells (2019) Vol. 8, Iss. 3, pp. 240-240
Open Access | Times Cited: 20
O-GlcNAc Transferase (OGT) Protects Cerebral Neurons from Death During Ischemia/Reperfusion (I/R) Injury by Modulating Drp1 in Mice
Jingru Zhao, Lipeng Dong, Tiantian Huo, et al.
NeuroMolecular Medicine (2021) Vol. 24, Iss. 3, pp. 299-310
Closed Access | Times Cited: 18
Methods for Studying Site-Specific O-GlcNAc Modifications: Successes, Limitations, and Important Future Goals
Stuart P. Moon, Afraah Javed, Eldon R. Hard, et al.
JACS Au (2021) Vol. 2, Iss. 1, pp. 74-83
Open Access | Times Cited: 17
Exploration of O-GlcNAc transferase glycosylation sites reveals a target sequence compositional bias
P. Andrew Chong, Michael L. Nosella, Manasvi Vanama, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 5, pp. 104629-104629
Open Access | Times Cited: 6
Native lamin A/C proteomes and novel partners from heart and skeletal muscle in a mouse chronic inflammation model of human frailty
Fatima D. Elzamzami, Arushi Samal, Adith S. Arun, et al.
Frontiers in Cell and Developmental Biology (2023) Vol. 11
Open Access | Times Cited: 5
Regulation of Lipid Metabolism by Lamin in Mutation-Related Diseases
Yue Peng, Qianyu Tang, Fan Xiao, et al.
Frontiers in Pharmacology (2022) Vol. 13
Open Access | Times Cited: 7
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 | Times Cited: 1
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 | Times Cited: 1
Exploration of O-GlcNAc-transferase (OGT) glycosylation sites reveals a target sequence compositional bias
P. Andrew Chong, Michael L. Nosella, Manasvi Vanama, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 1
Glycan analysis of Lamin A/C protein at G2/M and S phases of the cell cycle
Ecem Şener Uslupehlivan, Remziye Deveci, Umut Şahar, et al.
Cell Biochemistry and Biophysics (2022) Vol. 80, Iss. 4, pp. 689-698
Closed Access | Times Cited: 1
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