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:
RNA Regulation by Poly(ADP-Ribose) Polymerases
Florian J. Bock, Tanya Todorova, Paul Chang
Molecular Cell (2015) Vol. 58, Iss. 6, pp. 959-969
Open Access | Times Cited: 100
Florian J. Bock, Tanya Todorova, Paul Chang
Molecular Cell (2015) Vol. 58, Iss. 6, pp. 959-969
Open Access | Times Cited: 100
Showing 1-25 of 100 citing articles:
NAD + in aging, metabolism, and neurodegeneration
Eric Verdin
Science (2015) Vol. 350, Iss. 6265, pp. 1208-1213
Closed Access | Times Cited: 1037
Eric Verdin
Science (2015) Vol. 350, Iss. 6265, pp. 1208-1213
Closed Access | Times Cited: 1037
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
Luis A. Rajman, Karolina Chwalek, David Sinclair
Cell Metabolism (2018) Vol. 27, Iss. 3, pp. 529-547
Open Access | Times Cited: 710
Biology of Poly(ADP-Ribose) Polymerases: The Factotums of Cell Maintenance
Péter Bai
Molecular Cell (2015) Vol. 58, Iss. 6, pp. 947-958
Open Access | Times Cited: 415
Péter Bai
Molecular Cell (2015) Vol. 58, Iss. 6, pp. 947-958
Open Access | Times Cited: 415
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
Elizaveta E. Alemasova, Olga I. Lavrik
Nucleic Acids Research (2019) Vol. 47, Iss. 8, pp. 3811-3827
Open Access | Times Cited: 387
Phase Separation: Linking Cellular Compartmentalization to Disease
Adriano Aguzzi, Matthias Altmeyer
Trends in Cell Biology (2016) Vol. 26, Iss. 7, pp. 547-558
Closed Access | Times Cited: 321
Adriano Aguzzi, Matthias Altmeyer
Trends in Cell Biology (2016) Vol. 26, Iss. 7, pp. 547-558
Closed Access | Times Cited: 321
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
Michael S. Cohen, Paul Chang
Nature Chemical Biology (2018) Vol. 14, Iss. 3, pp. 236-243
Open Access | Times Cited: 272
The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular scaffold
Gavin J. Knott, Charles S. Bond, Archa H. Fox
Nucleic Acids Research (2016) Vol. 44, Iss. 9, pp. 3989-4004
Open Access | Times Cited: 265
Gavin J. Knott, Charles S. Bond, Archa H. Fox
Nucleic Acids Research (2016) Vol. 44, Iss. 9, pp. 3989-4004
Open Access | Times Cited: 265
Readers of poly(ADP-ribose): designed to be fit for purpose
Federico Teloni, Matthias Altmeyer
Nucleic Acids Research (2015) Vol. 44, Iss. 3, pp. 993-1006
Open Access | Times Cited: 226
Federico Teloni, Matthias Altmeyer
Nucleic Acids Research (2015) Vol. 44, Iss. 3, pp. 993-1006
Open Access | Times Cited: 226
ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease
Bernhard Lüscher, Mareike Bütepage, Laura Eckei, et al.
Chemical Reviews (2017) Vol. 118, Iss. 3, pp. 1092-1136
Closed Access | Times Cited: 223
Bernhard Lüscher, Mareike Bütepage, Laura Eckei, et al.
Chemical Reviews (2017) Vol. 118, Iss. 3, pp. 1092-1136
Closed Access | Times Cited: 223
Undercover: gene control by metabolites and metabolic enzymes
Jan A. van der Knaap, C. Peter Verrijzer
Genes & Development (2016) Vol. 30, Iss. 21, pp. 2345-2369
Open Access | Times Cited: 198
Jan A. van der Knaap, C. Peter Verrijzer
Genes & Development (2016) Vol. 30, Iss. 21, pp. 2345-2369
Open Access | Times Cited: 198
Opportunities for the repurposing of PARP inhibitors for the therapy of non‐oncological diseases
Nathan A. Berger, Valérie C. Besson, A. Hamid Boulares, et al.
British Journal of Pharmacology (2017) Vol. 175, Iss. 2, pp. 192-222
Open Access | Times Cited: 193
Nathan A. Berger, Valérie C. Besson, A. Hamid Boulares, et al.
British Journal of Pharmacology (2017) Vol. 175, Iss. 2, pp. 192-222
Open Access | Times Cited: 193
PARP-1 Activation Directs FUS to DNA Damage Sites to Form PARG-Reversible Compartments Enriched in Damaged DNA
Anastasia S. Singatulina, Loïc Hamon, Maria V. Sukhanova, et al.
Cell Reports (2019) Vol. 27, Iss. 6, pp. 1809-1821.e5
Open Access | Times Cited: 191
Anastasia S. Singatulina, Loïc Hamon, Maria V. Sukhanova, et al.
Cell Reports (2019) Vol. 27, Iss. 6, pp. 1809-1821.e5
Open Access | Times Cited: 191
Multifaceted Role of PARP-1 in DNA Repair and Inflammation: Pathological and Therapeutic Implications in Cancer and Non-Cancer Diseases
Simonetta Pazzaglia, Claudio Pioli
Cells (2019) Vol. 9, Iss. 1, pp. 41-41
Open Access | Times Cited: 172
Simonetta Pazzaglia, Claudio Pioli
Cells (2019) Vol. 9, Iss. 1, pp. 41-41
Open Access | Times Cited: 172
PARPs and ADP-Ribosylation: 50 Years … and Counting
W. Lee Kraus
Molecular Cell (2015) Vol. 58, Iss. 6, pp. 902-910
Open Access | Times Cited: 166
W. Lee Kraus
Molecular Cell (2015) Vol. 58, Iss. 6, pp. 902-910
Open Access | Times Cited: 166
The conserved macrodomains of the non-structural proteins of Chikungunya virus and other pathogenic positive strand RNA viruses function as mono-ADP-ribosylhydrolases
Laura Eckei, Sarah Krieg, Mareike Bütepage, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 134
Laura Eckei, Sarah Krieg, Mareike Bütepage, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 134
Luca Palazzo, Andreja Mikoč, Ivan Ahel
FEBS Journal (2017) Vol. 284, Iss. 18, pp. 2932-2946
Open Access | Times Cited: 129
PARPs and ADP-ribosylation in RNA biology: from RNA expression and processing to protein translation and proteostasis
Dae-Seok Kim, Sridevi Challa, Aarin Jones, et al.
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 302-320
Open Access | Times Cited: 122
Dae-Seok Kim, Sridevi Challa, Aarin Jones, et al.
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 302-320
Open Access | Times Cited: 122
Use of poly ADP-ribose polymerase [PARP] inhibitors in cancer cells bearing DDR defects: the rationale for their inclusion in the clinic
Aniello Cerrato, Francesco Morra, Angela Celetti
Journal of Experimental & Clinical Cancer Research (2016) Vol. 35, Iss. 1
Open Access | Times Cited: 112
Aniello Cerrato, Francesco Morra, Angela Celetti
Journal of Experimental & Clinical Cancer Research (2016) Vol. 35, Iss. 1
Open Access | Times Cited: 112
ADP-ribosylation signalling and human disease
Luca Palazzo, Petra Mikolčević, Andreja Mikoč, et al.
Open Biology (2019) Vol. 9, Iss. 4
Open Access | Times Cited: 92
Luca Palazzo, Petra Mikolčević, Andreja Mikoč, et al.
Open Biology (2019) Vol. 9, Iss. 4
Open Access | Times Cited: 92
Intracellular Mono-ADP-Ribosylation in Signaling and Disease
Mareike Bütepage, Laura Eckei, Patricia Verheugd, et al.
Cells (2015) Vol. 4, Iss. 4, pp. 569-595
Open Access | Times Cited: 91
Mareike Bütepage, Laura Eckei, Patricia Verheugd, et al.
Cells (2015) Vol. 4, Iss. 4, pp. 569-595
Open Access | Times Cited: 91
Specificity of reversible ADP-ribosylation and regulation of cellular processes
Kerryanne Crawford, Juán José Bonfiglio, Andreja Mikoč, et al.
Critical Reviews in Biochemistry and Molecular Biology (2017) Vol. 53, Iss. 1, pp. 64-82
Closed Access | Times Cited: 91
Kerryanne Crawford, Juán José Bonfiglio, Andreja Mikoč, et al.
Critical Reviews in Biochemistry and Molecular Biology (2017) Vol. 53, Iss. 1, pp. 64-82
Closed Access | Times Cited: 91
Angiogenic patterning by STEEL, an endothelial-enriched long noncoding RNA
H. S. Jeffrey Man, Aravin N. Sukumar, Gabrielle C. Lam, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 10, pp. 2401-2406
Open Access | Times Cited: 87
H. S. Jeffrey Man, Aravin N. Sukumar, Gabrielle C. Lam, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 10, pp. 2401-2406
Open Access | Times Cited: 87
PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities
N Mimica Dukic, Øyvind Strømland, Jonas D. Elsborg, et al.
Science Advances (2023) Vol. 9, Iss. 37
Open Access | Times Cited: 38
N Mimica Dukic, Øyvind Strømland, Jonas D. Elsborg, et al.
Science Advances (2023) Vol. 9, Iss. 37
Open Access | Times Cited: 38
Updated protein domain annotation of the PARP protein family sheds new light on biological function
Marcin J. Suskiewicz, Deeksha Munnur, Øyvind Strømland, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 15, pp. 8217-8236
Open Access | Times Cited: 35
Marcin J. Suskiewicz, Deeksha Munnur, Øyvind Strømland, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 15, pp. 8217-8236
Open Access | Times Cited: 35
Combining Higher-Energy Collision Dissociation and Electron-Transfer/Higher-Energy Collision Dissociation Fragmentation in a Product-Dependent Manner Confidently Assigns Proteomewide ADP-Ribose Acceptor Sites
Vera Bilan, Mario Leutert, Paolo Nanni, et al.
Analytical Chemistry (2016) Vol. 89, Iss. 3, pp. 1523-1530
Closed Access | Times Cited: 82
Vera Bilan, Mario Leutert, Paolo Nanni, et al.
Analytical Chemistry (2016) Vol. 89, Iss. 3, pp. 1523-1530
Closed Access | Times Cited: 82
