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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:

PARPs and PAR as novel pharmacological targets for the treatment of stress granule-associated disorders
Giovanna Grimaldi, Giuliana Catara, Luca Palazzo, et al.
Biochemical Pharmacology (2019) Vol. 167, pp. 64-75
Closed Access | Times Cited: 23

Showing 23 citing articles:

(ADP-ribosyl)hydrolases: structure, function, and biology
J.G.M. Rack, Luca Palazzo, Ivan Ahel
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 263-284
Open Access | Times Cited: 159
The Role of PARPs in Inflammation—And Metabolic—Related Diseases: Molecular Mechanisms and Beyond
Yueshuang Ke, Chenxin Wang, Jiaqi Zhang, et al.
Cells (2019) Vol. 8, Iss. 9, pp. 1047-1047
Open Access | Times Cited: 100
The involvement of stress granules in aging and aging‐associated diseases
Xiuling Cao, Xuejiao Jin, Beidong Liu
Aging Cell (2020) Vol. 19, Iss. 4
Open Access | Times Cited: 92
Post-translational modifications: Regulators of neurodegenerative proteinopathies
Rohan Gupta, Mehar Sahu, Devesh Srivastava, et al.
Ageing Research Reviews (2021) Vol. 68, pp. 101336-101336
Closed Access | Times Cited: 76
Targeting the Ubiquitin–Proteasome System and Recent Advances in Cancer Therapy
Daniela Spano, Giuliana Catara
Cells (2023) Vol. 13, Iss. 1, pp. 29-29
Open Access | Times Cited: 27
Targeting the NEDP1 enzyme to ameliorate ALS phenotypes through stress granule disassembly
Toufic Kassouf, Rohit Shrivastava, Igor Meszka, et al.
Science Advances (2023) Vol. 9, Iss. 13
Open Access | Times Cited: 17
Cancer cell adaptability: turning ribonucleoprotein granules into targets
Margot Lavalée, Nicolas Curdy, Camille Laurent, et al.
Trends in cancer (2021) Vol. 7, Iss. 10, pp. 902-915
Open Access | Times Cited: 41
Mono(ADP-ribosyl)ation Enzymes and NAD+ Metabolism: A Focus on Diseases and Therapeutic Perspectives
Palmiro Poltronieri, Angela Celetti, Luca Palazzo
Cells (2021) Vol. 10, Iss. 1, pp. 128-128
Open Access | Times Cited: 24
Intracellular mono-ADP-ribosyltransferases at the host–virus interphase
Bernhard Lüscher, Maud Verheirstraeten, Sarah Krieg, et al.
Cellular and Molecular Life Sciences (2022) Vol. 79, Iss. 6
Open Access | Times Cited: 18
PKD-dependent PARP12-catalyzed mono-ADP-ribosylation of Golgin-97 is required for E-cadherin transport from Golgi to plasma membrane
Giovanna Grimaldi, Angela Filograna, Laura Schembri, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 119, Iss. 1
Open Access | Times Cited: 22
Targeting ADP-ribosylation as an antimicrobial strategy
Giuliana Catara, Annunziata Corteggio, Carmen Valente, et al.
Biochemical Pharmacology (2019) Vol. 167, pp. 13-26
Open Access | Times Cited: 21
Neddylation of protein, a new strategy of protein post-translational modification for targeted treatment of central nervous system diseases
Qian Wu, Ziang Geng, Lu Jun, et al.
Frontiers in Neuroscience (2024) Vol. 18
Open Access | Times Cited: 2
Response to stress in biological disorders: Implications of stress granule assembly and function
Lingjuan Wang, Weina Yang, Bin Li, et al.
Cell Proliferation (2021) Vol. 54, Iss. 8
Open Access | Times Cited: 15
Functional Roles of Poly(ADP-Ribose) in Stress Granule Formation and Dynamics
Xuejiao Jin, Xiuling Cao, Shenkui Liu, et al.
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 13
Oxidative Stress in Neurology and in Neurodegenerative Processes
Gaurav Gupta, Sacchidanand Pathak, Sarita Rawat, et al.
Springer eBooks (2020), pp. 49-65
Closed Access | Times Cited: 11
Poly(ADP-Ribosyl) Code Functions
Natalya Maluchenko, Darya O. Koshkina, Alexey V. Feofanov, et al.
Acta Naturae (2021) Vol. 13, Iss. 2, pp. 58-69
Open Access | Times Cited: 8
Chemical synthesis of linear ADP-ribose oligomers up to pentamer and their binding to the oncogenic helicase ALC1
Qiang Liu, G. Knobloch, Jim Voorneveld, et al.
Chemical Science (2021) Vol. 12, Iss. 37, pp. 12468-12475
Open Access | Times Cited: 5
PARP12-catalyzed mono-ADP-ribosylation of Golgin-97 controls the transport of E-cadherin
Giovanna Grimaldi, Laura Schembri, Matteo Lo Monte, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 4
ADP-ribosylation inhibitors in treatment of diseases
Péter Bai, Palmiro Poltronieri, Mariella Di Girolamo
Biochemical Pharmacology (2019) Vol. 167, pp. 1-2
Closed Access | Times Cited: 3
A global analysis of low-complexity regions in the Trypanosoma brucei proteome reveals enrichment in the C-terminus of nucleic acid binding proteins providing potential targets of phosphorylation
Mathieu Cayla, Keith R. Matthews, Alasdair Ivens
Wellcome Open Research (2020) Vol. 5, pp. 219-219
Open Access | Times Cited: 3
A global analysis of low-complexity regions in the Trypanosoma brucei proteome reveals enrichment in the C-terminus of nucleic acid binding proteins providing potential targets of phosphorylation
Mathieu Cayla, Keith R. Matthews, Alasdair Ivens
Wellcome Open Research (2020) Vol. 5, pp. 219-219
Open Access | Times Cited: 2
Targeting the deNEDDylating enzyme NEDP1 to ameliorate ALS phenotypes through Stress Granules dissolution
Toufic Kassouf, Rohit Shrivastava, Igor Meszka, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
The Role of Stress in the Progression of Motor Neuron Disease: Mechanisms and Implications for Treatment
Chenyang Lu, Xingshun Xu
Stress and Brain (2023) Vol. 3, Iss. 4, pp. 159-178
Open Access
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