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:

Overview of the mammalian ADP-ribosyl-transferases clostridia toxin-like (ARTCs) family
Maria Di Girolamo, Gaia Fabrizio
Biochemical Pharmacology (2019) Vol. 167, pp. 86-96
Closed Access | Times Cited: 32

Showing 1-25 of 32 citing articles:

ADP‐ribosyltransferases, an update on function and nomenclature
Bernhard Lüscher, Ivan Ahel, Matthias Altmeyer, et al.
FEBS Journal (2021) Vol. 289, Iss. 23, pp. 7399-7410
Open Access | Times Cited: 238

ADP-ribosylation from molecular mechanisms to therapeutic implications
Marcin J. Suskiewicz, Evgeniia Prokhorova, J.G.M. Rack, et al.
Cell (2023) Vol. 186, Iss. 21, pp. 4475-4495
Open Access | Times Cited: 75

Parps in immune response: Potential targets for cancer immunotherapy
S Wang, Jingling Huang, T. X. Zeng, et al.
Biochemical Pharmacology (2025) Vol. 234, pp. 116803-116803
Closed Access | Times Cited: 2

Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation
Ann-Katrin Hopp, Patrick Grüter, Michael O. Hottiger
Cells (2019) Vol. 8, Iss. 8, pp. 890-890
Open Access | Times Cited: 90

Nucleotide Sugars in Chemistry and Biology
Satu Mikkola
Molecules (2020) Vol. 25, Iss. 23, pp. 5755-5755
Open Access | Times Cited: 63

CYB5R3 functions as a tumor suppressor by inducing ER stress-mediated apoptosis in lung cancer cells via the PERK-ATF4 and IRE1α-JNK pathways
Joo‐Young Im, Soo Jin Kim, Jong‐Lyul Park, et al.
Experimental & Molecular Medicine (2024) Vol. 56, Iss. 1, pp. 235-249
Open Access | Times Cited: 6

Enzymology of extracellular NAD metabolism
Massimiliano Gasparrini, Leonardo Sorci, Nadia Raffaelli
Cellular and Molecular Life Sciences (2021) Vol. 78, Iss. 7, pp. 3317-3331
Open Access | Times Cited: 32

ADP-Ribosylation Post-Translational Modification: An Overview with a Focus on RNA Biology and New Pharmacological Perspectives
Giuseppe Manco, Giuseppina Lacerra, Elena Porzio, et al.
Biomolecules (2022) Vol. 12, Iss. 3, pp. 443-443
Open Access | Times Cited: 21

Kinetic Mechanism of the Emergent Anticancer Target, Human ADP-ribosyltransferase 1
D. Groom, Amanda Lopacinski, S. Garforth, et al.
Biochemistry (2025)
Closed Access

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

ART1 knockdown decreases the IL-6-induced proliferation of colorectal cancer cells
Ting Lin, Shuxian Zhang, Yi Tang, et al.
BMC Cancer (2024) Vol. 24, Iss. 1
Open Access | Times Cited: 3

ADP-ribosylation, a multifaceted modification: Functions and mechanisms in aging and aging-related diseases
Wu Hao, Zhao Jialong, Yuan Jiuzhi, et al.
Ageing Research Reviews (2024) Vol. 98, pp. 102347-102347
Open Access | Times Cited: 3

NAD+ Degrading Enzymes, Evidence for Roles During Infection
Arnold Tan, Craig Doig
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 18

Profound inhibition of CD73-dependent formation of anti-inflammatory adenosine in B cells of SLE patients
Julia Hesse, M. Siekierka-Harreis, Bodo Steckel, et al.
EBioMedicine (2021) Vol. 73, pp. 103616-103616
Open Access | Times Cited: 18

Functional roles of ADP-ribosylation writers, readers and erasers
Ping Li, Yushuang Lei, Qi Jia, et al.
Frontiers in Cell and Developmental Biology (2022) Vol. 10
Open Access | Times Cited: 12

Mono-ADP-ribosylation, a MARylationmultifaced modification of protein, DNA and RNA: characterizations, functions and mechanisms
Hao Wu, Anqi Lu, Jiuzhi Yuan, et al.
Cell Death Discovery (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 2

The ART of tumor immune escape
Erik Wennerberg, Sumit Mukherjee, Ricardo M. Sainz, et al.
OncoImmunology (2022) Vol. 11, Iss. 1
Open Access | Times Cited: 10

Selective Pharmaceutical Inhibition of PARP14 Mitigates Allergen-Induced IgE and Mucus Overproduction in a Mouse Model of Pulmonary Allergic Response
Alex M. Eddie, Kevin W. Chen, Laurie B. Schenkel, et al.
ImmunoHorizons (2022) Vol. 6, Iss. 7, pp. 432-446
Open Access | Times Cited: 10

ADP-Ribosylation as Post-Translational Modification of Proteins: Use of Inhibitors in Cancer Control
Palmiro Poltronieri, Masanao Miwa, Mitsuko Masutani
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 19, pp. 10829-10829
Open Access | Times Cited: 11

Role of APD-Ribosylation in Bone Health and Disease
Chun Wang, Gabriel Mbalaviele
Cells (2019) Vol. 8, Iss. 10, pp. 1201-1201
Open Access | Times Cited: 7

Mono-ADP-ribosylation sites of human CD73 inhibit its adenosine-generating enzymatic activity
Julia Hesse, Mona K. Rosse, Bodo Steckel, et al.
Purinergic Signalling (2021) Vol. 18, Iss. 1, pp. 115-121
Open Access | Times Cited: 7

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

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