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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:

Identifying Family-Member-Specific Targets of Mono-ARTDs by Using a Chemical Genetics Approach
Ian Carter-O’Connell, Haihong Jin, Rory K. Morgan, et al.
Cell Reports (2016) Vol. 14, Iss. 3, pp. 621-631
Open Access | Times Cited: 79

Showing 26-50 of 79 citing articles:

Poly(ADP-Ribose) Polymerases in Host-Pathogen Interactions, Inflammation, and Immunity
Pamlea N. Brady, Anupam Goel, Margaret A. Johnson
Microbiology and Molecular Biology Reviews (2019) Vol. 83, Iss. 1
Open Access | Times Cited: 46
Medicinal Chemistry Perspective on Targeting Mono-ADP-Ribosylating PARPs with Small Molecules
Maria Giulia Nizi, Mirko M. Maksimainen, L. Lehtiö, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 11, pp. 7532-7560
Open Access | Times Cited: 25
Characterization of TCDD-inducible poly-ADP-ribose polymerase (TIPARP/ARTD14) catalytic activity
Alvin Gomez, Christian Bindesbøll, Somisetty V. Satheesh, et al.
Biochemical Journal (2018) Vol. 475, Iss. 23, pp. 3827-3846
Open Access | Times Cited: 46
A ribose-functionalized NAD+ with unexpected high activity and selectivity for protein poly-ADP-ribosylation
Xiaonan Zhang, Qinqin Cheng, Jingwen Chen, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 36
Uncovering the Invisible: Mono-ADP-ribosylation Moved into the Spotlight
Ann-Katrin Hopp, Michael O. Hottiger
Cells (2021) Vol. 10, Iss. 3, pp. 680-680
Open Access | Times Cited: 28
On the Need to Tell Apart Fraternal Twins eEF1A1 and eEF1A2, and Their Respective Outfits
Alberto Mills, Federico Gago
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 13, pp. 6973-6973
Open Access | Times Cited: 28
mTORC1-c-Myc pathway rewires methionine metabolism for HCC progression through suppressing SIRT4 mediated ADP ribosylation of MAT2A
Liang Zhao, Huizhao Su, Xiaomeng Liu, et al.
Cell & Bioscience (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 19
Chemical proteomics reveals ADP-ribosylation of small GTPases during oxidative stress
Nathan P. Westcott, Joseph Fernandez, Henrik Molina, et al.
Nature Chemical Biology (2017) Vol. 13, Iss. 3, pp. 302-308
Open Access | Times Cited: 37
A critical review of the role of M2PYK in the Warburg effect
Robert A. Harris, Aron W. Fenton
Biochimica et Biophysica Acta (BBA) - Reviews on Cancer (2019) Vol. 1871, Iss. 2, pp. 225-239
Open Access | Times Cited: 34
Chemical Proteomics Approach for Profiling the NAD Interactome
Justina Šileikytė, Sunil K. Sundalam, Larry L. David, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 18, pp. 6787-6791
Open Access | Times Cited: 26
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
A Bifunctional NAD+ for Profiling Poly-ADP-Ribosylation-Dependent Interacting Proteins
Albert T. Lam, Xiaonan Zhang, Valentine V. Courouble, et al.
ACS Chemical Biology (2021) Vol. 16, Iss. 2, pp. 389-396
Open Access | Times Cited: 24
Profiling of the ADP‐Ribosylome in Living Cells
Maike Lehner, Sonja Rieth, Eva Höllmüller, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 18
Open Access | Times Cited: 18
Functionalised Cofactor Mimics for Interactome Discovery and Beyond
Isabel V. L. Wilkinson, Martin Pfanzelt, Stephan A. Sieber
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 29
Open Access | Times Cited: 18
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
Significance of Mitochondrial Protein Post-translational Modifications in Pathophysiology of Brain Injury
Nina Klimova, Aaron Long, Tibor Kristián
Translational Stroke Research (2017) Vol. 9, Iss. 3, pp. 223-237
Closed Access | Times Cited: 32
Mechanisms governing PARP expression, localization, and activity in cells
Daniel J. Sanderson, Michael S. Cohen
Critical Reviews in Biochemistry and Molecular Biology (2020) Vol. 55, Iss. 6, pp. 541-554
Closed Access | Times Cited: 27
Small-Molecule Inhibitors of PARPs: From Tools for Investigating ADP-Ribosylation to Therapeutics
Ilsa T. Kirby, Michael S. Cohen
Current topics in microbiology and immunology (2018), pp. 211-231
Closed Access | Times Cited: 25
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
In Vitro and Cellular Probes to Study PARP Enzyme Target Engagement
Tim J. Wigle, Danielle J. Blackwell, Laurie B. Schenkel, et al.
Cell chemical biology (2020) Vol. 27, Iss. 7, pp. 877-887.e14
Open Access | Times Cited: 22
Forced Self-Modification Assays as a Strategy to Screen MonoPARP Enzymes
Tim J. Wigle, W. David Church, Christina R. Majer, et al.
SLAS DISCOVERY (2019) Vol. 25, Iss. 3, pp. 241-252
Open Access | Times Cited: 22
A desthiobiotin labelled NAD+ analogue to uncover Poly(ADP‐ribose) polymerase 1 protein targets
Sonja Rieth, Daniel Spliesgar, Jan Orth, et al.
ChemBioChem (2024) Vol. 25, Iss. 5
Open Access | Times Cited: 2
Uncommon posttranslational modifications in proteomics: ADP‐ribosylation, tyrosine nitration, and tyrosine sulfation
Aarti Bashyal, Jennifer S. Brodbelt
Mass Spectrometry Reviews (2022) Vol. 43, Iss. 2, pp. 289-326
Closed Access | Times Cited: 10
Identification of Protein Substrates of Specific PARP Enzymes Using Analog-Sensitive PARP Mutants and a “Clickable” NAD+ Analog
Bryan A. Gibson, W. Lee Kraus
Methods in molecular biology (2017), pp. 111-135
Open Access | Times Cited: 17
Structure, Maintenance, and Regulation of Nuclear Pore Complexes: The Gatekeepers of the Eukaryotic Genome
Marcela Raı́ces, Maximiliano A. D’Angelo
Cold Spring Harbor Perspectives in Biology (2021) Vol. 14, Iss. 3, pp. a040691-a040691
Open Access | Times Cited: 14

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