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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:

An Expanding Repertoire of Protein Acylations
Yuxuan Xu, Zhenyu Shi, Li Bao
Molecular & Cellular Proteomics (2022) Vol. 21, Iss. 3, pp. 100193-100193
Open Access | Times Cited: 52

Showing 26-50 of 52 citing articles:

The Brain Protein Acylation System Responds to Seizures in the Rat Model of PTZ-Induced Epilepsy
Lev Zavileyskiy, Vasily A. Aleshin, Thilo Kaehne, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 20, pp. 12302-12302
Open Access | Times Cited: 9
In‐depth analysis of the Sirtuin 5‐regulated mouse brain malonylome and succinylome using library‐free data‐independent acquisitions
Joanna Bons, Jacob Rose, Ran Zhang, et al.
PROTEOMICS (2022) Vol. 23, Iss. 3-4
Open Access | Times Cited: 8
Germline status and micronutrient availability regulate a somatic mitochondrial quality control pathway via short-chain fatty acid metabolism
James P Held, Nadir H Dbouk, Adrianna M. Strozak, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Multi-step HPLC fractionation enabled in-depth and unbiased characterization of histone marks
Wensi Zhao, Kaifeng Chen, Jun Zhang, et al.
Journal of Chromatography A (2024) Vol. 1736, pp. 465368-465368
Closed Access | Times Cited: 1
Biological functions and therapeutic potential of acylation by histone acetyltransferases
Nan Li, Clark Hamor, Yahang An, et al.
Acta Materia Medica (2023) Vol. 2, Iss. 2
Open Access | Times Cited: 4
Global proteomic analyses of lysine acetylation, malonylation, succinylation, and crotonylation in human sperm reveal their involvement in male fertility
Yan Tian, Hao Wang, Tingting Pan, et al.
Journal of Proteomics (2024) Vol. 303, pp. 105213-105213
Closed Access | Times Cited: 1
Lipid switches in the immunological synapse
Gillian M. Griffiths, Britta Brügger, Christian Freund
Journal of Biological Chemistry (2024) Vol. 300, Iss. 7, pp. 107428-107428
Open Access | Times Cited: 1
Acetylation, ADP-ribosylation and methylation of malate dehydrogenase
Misty L. Kuhn, John F. Rakus, Delphine Quénet
Essays in Biochemistry (2024) Vol. 68, Iss. 2, pp. 199-212
Closed Access | Times Cited: 1
Global isonicotinylome analysis identified SMAD3 isonicotinylation promotes liver cancer cell epithelial–mesenchymal transition and invasion
Yixiao Li, Yuhan Jiang, Haoyi Yan, et al.
iScience (2024) Vol. 27, Iss. 9, pp. 110775-110775
Open Access | Times Cited: 1
Functions of Coenzyme A and Acyl-CoA in Post-Translational Modification and Human Disease
Jumin Xie, Yu Zhang, Ying Zhu, et al.
Frontiers in Bioscience-Landmark (2024) Vol. 29, Iss. 9
Open Access | Times Cited: 1
Studying Reversible Protein Post‐translational Modification through Co‐translational Modification
Dan Wu, Tao Liu
ChemBioChem (2023) Vol. 24, Iss. 7
Closed Access | Times Cited: 2
Post-crotonylation oxidation by a monooxygenase promotes acetyl-CoA synthetase degradation in Streptomyces roseosporus
Bingbing Ma, Chen‐Fan Sun, Jingyi Zhou, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 2
Dynamic acylome reveals metabolite driven modifications in Syntrophomonas wolfei
Janine Y. Fu, John M. Muroski, Mark A. Arbing, et al.
Frontiers in Microbiology (2022) Vol. 13
Open Access | Times Cited: 3
Propargylamine Amino Acids as Constrained Nε-Substituted Lysine Mimetics
Kevin Van holsbeeck, Mathias Elsocht, Steven Ballet
Organic Letters (2022) Vol. 25, Iss. 1, pp. 130-133
Closed Access | Times Cited: 3
Identification and Functional Analysis of Lysine 2-Hydroxyisobutyrylation in Cyanobacteria
Qiaoya Li, Jian Lin, Haiyan Ma, et al.
Journal of Proteome Research (2024) Vol. 23, Iss. 5, pp. 1689-1701
Closed Access
Perspective: Pathological transdifferentiation—a novel therapeutic target for cardiovascular diseases and chronic inflammation
William Y. Yang, Melissa Mahgoub, Fatma Saaoud, et al.
Frontiers in Cardiovascular Medicine (2024) Vol. 11
Open Access
Regulation of ovarian cancer by protein post-translational modifications
Qiugang Zhu, Huimin Zhou, Feiting Xie
Frontiers in Oncology (2024) Vol. 14
Open Access
Non-enzymatic posttranslational protein modifications in protein aggregation and neurodegenerative diseases
Tim Baldensperger, Miriam Preissler, Christian F. W. Becker
RSC Chemical Biology (2024)
Open Access
Acylation of the Rat Brain Proteins is Affected by the Inhibition of Pyruvate Dehydrogenase in vivo
Vasily A. Aleshin, Daria A. Sibiryakina, A. V. KAZANTSEV, et al.
Biochemistry (Moscow) (2023) Vol. 88, Iss. 1, pp. 105-118
Closed Access | Times Cited: 1
Editorial: Experts' opinion in medicine 2022
Victoria I. Bunik
Frontiers in Medicine (2023) Vol. 10
Open Access | Times Cited: 1
Effects of Crotonylation on Reprogramming of Cashmere Goat Somatic Cells with Different Differentiation Degrees
Wennan Li, Wei Yan, Hao Fei, et al.
Animals (2022) Vol. 12, Iss. 20, pp. 2848-2848
Open Access | Times Cited: 2
In-depth Analysis of the Sirtuin 5-regulated Mouse Brain Acylome using Library-free Data-Independent Acquisitions
Joanna Bons, Jacob Rose, Ran Zhang, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 1
Succinyl-CoA Synthetase Deficiency in Mouse Forebrain Results in Hyper-Succinylation With Perturbed Neuronal Transcriptional Regulation and Metabolism
Makayla Suzanne Anderson, Emma H. Doud, Hongyu Gao, et al.
SSRN Electronic Journal (2022)
Closed Access | Times Cited: 1
Acylation of the rat brain proteins is affected by the inhibition of pyruvate dehydrogenase <i>in vivo</i>
Vasily A. Aleshin, Daria A. Sibiryakina, A. V Kazantsev, et al.
Биохимия (2023) Vol. 88, Iss. 1, pp. 147-163
Closed Access
Localization and Quantification of Post-Translational Modifications of Proteins Using Electron Activated Dissociation Fragmentation on a Fast-Acquisition Time-of-Flight Mass Spectrometer
Joanna Bons, Christie L. Hunter, Rita Chupalov, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access

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