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:

The impact of PARPs and ADP-ribosylation on inflammation and host–pathogen interactions
Anthony R. Fehr, Sasha A. Singh, Catherine M. Kerr, et al.
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 341-359
Open Access | Times Cited: 188

Showing 26-50 of 188 citing articles:

AAV-Txnip prolongs cone survival and vision in mouse models of retinitis pigmentosa
Yunlu Xue, Sean K. Wang, Parimal Rana, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 41

COVID‐19 metabolism: Mechanisms and therapeutic targets
Tianshi Wang, Ying Cao, Haiyan Zhang, et al.
MedComm (2022) Vol. 3, Iss. 3
Open Access | Times Cited: 35

The Conserved Macrodomain Is a Potential Therapeutic Target for Coronaviruses and Alphaviruses
Anthony K. L. Leung, Diane E. Griffin, Jürgen Bosch, et al.
Pathogens (2022) Vol. 11, Iss. 1, pp. 94-94
Open Access | Times Cited: 32

A single inactivating amino acid change in the SARS-CoV-2 NSP3 Mac1 domain attenuates viral replication in vivo
Taha Y. Taha, Rahul K. Suryawanshi, Irene P. Chen, et al.
PLoS Pathogens (2023) Vol. 19, Iss. 8, pp. e1011614-e1011614
Open Access | Times Cited: 20

Recurrent Loss of Macrodomain Activity in Host Immunity and Viral Proteins
Sofia E. Delgado-Rodriguez, Andrew P. Ryan, Matthew D. Daugherty
Pathogens (2023) Vol. 12, Iss. 5, pp. 674-674
Open Access | Times Cited: 17

Specific and shared biological functions of PARP2 – is PARP2 really a lil’ brother of PARP1?
Magdolna Szántó, José Yélamos, Péter Bai
Expert Reviews in Molecular Medicine (2024) Vol. 26
Open Access | Times Cited: 8

Mutation of a highly conserved isoleucine residue in loop 2 of several 𝛽-coronavirus macrodomains indicates that enhanced ADP-ribose binding is detrimental to infection
Catherine M. Kerr, Jessica J. Pfannenstiel, Yousef M. Alhammad, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 6

ADPriboDB 2.0: an updated database of ADP-ribosylated proteins
Vinay Ayyappan, Ricky Wat, Calvin Barber, et al.
Nucleic Acids Research (2020) Vol. 49, Iss. D1, pp. D261-D265
Open Access | Times Cited: 42

The Critical Role of PARPs in Regulating Innate Immune Responses
Huifang Zhu, Yan‐Dong Tang, Guoqing Zhan, et al.
Frontiers in Immunology (2021) Vol. 12
Open Access | Times Cited: 36

PARP7 and Mono-ADP-Ribosylation Negatively Regulate Estrogen Receptor α Signaling in Human Breast Cancer Cells
Marit Rasmussen, Susanna Tan, Venkata S. Somisetty, et al.
Cells (2021) Vol. 10, Iss. 3, pp. 623-623
Open Access | Times Cited: 34

PARP-1 regulates inflammasome activity by poly-ADP-ribosylation of NLRP3 and interaction with TXNIP in primary macrophages
Ling‐Ya Chiu, Duen-Yi Huang, Wan‐Wan Lin
Cellular and Molecular Life Sciences (2022) Vol. 79, Iss. 2
Open Access | Times Cited: 28

Structurally distinct PARP7 inhibitors provide new insights into the function of PARP7 in regulating nucleic acid-sensing and IFN-β signaling
Daniel J. Sanderson, Kelsie M. Rodriguez, Daniel S. Bejan, et al.
Cell chemical biology (2022) Vol. 30, Iss. 1, pp. 43-54.e8
Open Access | Times Cited: 23

Discovery and Development Strategies for SARS-CoV-2 NSP3 Macrodomain Inhibitors
M. Schuller, Tryfon Zarganes‐Tzitzikas, James M. Bennett, et al.
Pathogens (2023) Vol. 12, Iss. 2, pp. 324-324
Open Access | Times Cited: 14

SARS-CoV-2 infection dysregulates NAD metabolism
Amin Izadpanah, Joseph C. Mudd, Joe G. N. Garcia, et al.
Frontiers in Immunology (2023) Vol. 14
Open Access | Times Cited: 13

Functional and druggability analysis of the SARS-CoV-2 proteome
Claudio N. Cavasotto, Maximiliano Sánchez‐Lamas, Julián Maggini
European Journal of Pharmacology (2020) Vol. 890, pp. 173705-173705
Open Access | Times Cited: 39

Structural, Biophysical, and Biochemical Elucidation of the SARS-CoV-2 Nonstructural Protein 3 Macro Domain
Meng-Hsuan Lin, San-Chi Chang, Yi-Chih Chiu, et al.
ACS Infectious Diseases (2020) Vol. 6, Iss. 11, pp. 2970-2978
Open Access | Times Cited: 38

Zinc finger proteins in the host-virus interplay: multifaceted functions based on their nucleic acid-binding property
Guanming Wang, Chunfu Zheng
FEMS Microbiology Reviews (2020) Vol. 45, Iss. 3
Closed Access | Times Cited: 38

PARPs and ADP-ribosylation: 60 years on
W. Lee Kraus
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 251-253
Open Access | Times Cited: 34

Gut microbiome ADP-ribosyltransferases are widespread phage-encoded fitness factors
Eric Brown, Hugo Arellano-Santoyo, Emily R. Temple, et al.
Cell Host & Microbe (2021) Vol. 29, Iss. 9, pp. 1351-1365.e11
Open Access | Times Cited: 32

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

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

Design, synthesis and evaluation of inhibitors of the SARS-CoV-2 nsp3 macrodomain
Lavinia M. Sherrill, Elva E. Joya, AnnMarie Walker, et al.
Bioorganic & Medicinal Chemistry (2022) Vol. 67, pp. 116788-116788
Open Access | Times Cited: 20

Protein and RNA ADP-ribosylation detection is influenced by sample preparation and reagents used
Lisa Weixler, Nonso Josephat Ikenga, Jim Voorneveld, et al.
Life Science Alliance (2022) Vol. 6, Iss. 1, pp. e202201455-e202201455
Open Access | Times Cited: 20

Neuroprotective Effects of PARP Inhibitors in Drosophila Models of Alzheimer’s Disease
Anna Maggiore, Assunta Maria Casale, Walter Toscanelli, et al.
Cells (2022) Vol. 11, Iss. 8, pp. 1284-1284
Open Access | Times Cited: 19

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