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 ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Rebecca Gupte, Ziying Liu, W. Lee Kraus
Genes & Development (2017) Vol. 31, Iss. 2, pp. 101-126
Open Access | Times Cited: 618

Showing 1-25 of 618 citing articles:

Why does COVID-19 disproportionately affect older people?
Amber L. Mueller, Maeve S. McNamara, David Sinclair
Aging (2020) Vol. 12, Iss. 10, pp. 9959-9981
Open Access | Times Cited: 985

Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence
Luis A. Rajman, Karolina Chwalek, David Sinclair
Cell Metabolism (2018) Vol. 27, Iss. 3, pp. 529-547
Open Access | Times Cited: 710

NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential
Na Xie, Lu Zhang, Wei Gao, et al.
Signal Transduction and Targeted Therapy (2020) Vol. 5, Iss. 1
Open Access | Times Cited: 653

Poly(ADP-ribose) polymerase inhibition: past, present and future
Nicola J. Curtin, Csaba Szabó
Nature Reviews Drug Discovery (2020) Vol. 19, Iss. 10, pp. 711-736
Closed Access | Times Cited: 403

Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins
Elizaveta E. Alemasova, Olga I. Lavrik
Nucleic Acids Research (2019) Vol. 47, Iss. 8, pp. 3811-3827
Open Access | Times Cited: 387

Regulation of chromatin and gene expression by metabolic enzymes and metabolites
Xinjian Li, Gábor Egervári, Yugang Wang, et al.
Nature Reviews Molecular Cell Biology (2018) Vol. 19, Iss. 9, pp. 563-578
Open Access | Times Cited: 375

Born to run: control of transcription elongation by RNA polymerase II
Fei Chen, Edwin R. Smith, Ali Shilatifard
Nature Reviews Molecular Cell Biology (2018) Vol. 19, Iss. 7, pp. 464-478
Open Access | Times Cited: 363

Properties of Stress Granule and P-Body Proteomes
Ji‐Young Youn, Boris J.A. Dyakov, Jianping Zhang, et al.
Molecular Cell (2019) Vol. 76, Iss. 2, pp. 286-294
Open Access | Times Cited: 361

Insights into the biogenesis, function, and regulation of ADP-ribosylation
Michael S. Cohen, Paul Chang
Nature Chemical Biology (2018) Vol. 14, Iss. 3, pp. 236-243
Open Access | Times Cited: 272

Structural basis for allosteric PARP-1 retention on DNA breaks
Levani Zandarashvili, Marie-France Langelier, Uday Kiran Velagapudi, et al.
Science (2020) Vol. 368, Iss. 6486
Open Access | Times Cited: 272

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

HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation
Marcin J. Suskiewicz, Florian Zobel, T.E.H. Ogden, et al.
Nature (2020) Vol. 579, Iss. 7800, pp. 598-602
Open Access | Times Cited: 217

Activation of PARP-1 by snoRNAs Controls Ribosome Biogenesis and Cell Growth via the RNA Helicase DDX21
Dae-Seok Kim, Cristel V. Camacho, Anusha Nagari, et al.
Molecular Cell (2019) Vol. 75, Iss. 6, pp. 1270-1285.e14
Open Access | Times Cited: 213

Protein Posttranslational Modifications: Roles in Aging and Age‐Related Disease
Ana L. Santos, Ariel B. Lindner
Oxidative Medicine and Cellular Longevity (2017) Vol. 2017, Iss. 1
Open Access | Times Cited: 207

Serine is the major residue for ADP-ribosylation upon DNA damage
Luca Palazzo, Orsolya Leidecker, Evgeniia Prokhorova, et al.
eLife (2018) Vol. 7
Open Access | Times Cited: 207

NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains
Marie-France Langelier, Levani Zandarashvili, Pedro M. Aguiar, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 201

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

Cellular functions of the protein kinase ATM and their relevance to human disease
Ji‐Hoon Lee, Tanya T. Paull
Nature Reviews Molecular Cell Biology (2021) Vol. 22, Iss. 12, pp. 796-814
Closed Access | Times Cited: 186

Neuronal enhancers are hotspots for DNA single-strand break repair
Wei Wu, Sarah E. Hill, William J. Nathan, et al.
Nature (2021) Vol. 593, Iss. 7859, pp. 440-444
Open Access | Times Cited: 176

Mitophagy in tumorigenesis and metastasis
Logan P. Poole, Kay F. Macleod
Cellular and Molecular Life Sciences (2021) Vol. 78, Iss. 8, pp. 3817-3851
Open Access | Times Cited: 169

Metabolic Signaling to the Nucleus in Cancer
Sydney L. Campbell, Kathryn E. Wellen
Molecular Cell (2018) Vol. 71, Iss. 3, pp. 398-408
Open Access | Times Cited: 167

Coronavirus infection and PARP expression dysregulate the NAD metabolome: An actionable component of innate immunity
Collin D. Heer, Daniel J. Sanderson, Lynden S. Voth, et al.
Journal of Biological Chemistry (2020) Vol. 295, Iss. 52, pp. 17986-17996
Open Access | Times Cited: 164

Systems-wide Analysis of Serine ADP-Ribosylation Reveals Widespread Occurrence and Site-Specific Overlap with Phosphorylation
Sara C. Buch-Larsen, Ivo A. Hendriks, David Lyon, et al.
Cell Reports (2018) Vol. 24, Iss. 9, pp. 2493-2505.e4
Open Access | Times Cited: 163

PARP family enzymes: regulation and catalysis of the poly(ADP-ribose) posttranslational modification
Marie-France Langelier, Travis Eisemann, Amanda A. Riccio, et al.
Current Opinion in Structural Biology (2018) Vol. 53, pp. 187-198
Open Access | Times Cited: 162

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