
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:
New PARP targets for cancer therapy
Sejal Vyas, Paul Chang
Nature reviews. Cancer (2014) Vol. 14, Iss. 7, pp. 502-509
Open Access | Times Cited: 162
Sejal Vyas, Paul Chang
Nature reviews. Cancer (2014) Vol. 14, Iss. 7, pp. 502-509
Open Access | Times Cited: 162
Showing 1-25 of 162 citing articles:
Mitochondria and Cancer
Sejal Vyas, Elma Zaganjor, Marcia C. Haigis
Cell (2016) Vol. 166, Iss. 3, pp. 555-566
Open Access | Times Cited: 1417
Sejal Vyas, Elma Zaganjor, Marcia C. Haigis
Cell (2016) Vol. 166, Iss. 3, pp. 555-566
Open Access | Times Cited: 1417
Small molecules in targeted cancer therapy: advances, challenges, and future perspectives
Lei Zhong, Yueshan Li, Liang Xiong, et al.
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 1127
Lei Zhong, Yueshan Li, Liang Xiong, et al.
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 1127
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: 271
Michael S. Cohen, Paul Chang
Nature Chemical Biology (2018) Vol. 14, Iss. 3, pp. 236-243
Open Access | Times Cited: 271
Functions of PARylation in DNA Damage Repair Pathways
Huiting Wei, Xiaochun Yu
Genomics Proteomics & Bioinformatics (2016) Vol. 14, Iss. 3, pp. 131-139
Open Access | Times Cited: 262
Huiting Wei, Xiaochun Yu
Genomics Proteomics & Bioinformatics (2016) Vol. 14, Iss. 3, pp. 131-139
Open Access | Times Cited: 262
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: 222
Bernhard Lüscher, Mareike Bütepage, Laura Eckei, et al.
Chemical Reviews (2017) Vol. 118, Iss. 3, pp. 1092-1136
Closed Access | Times Cited: 222
Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
Rita Martello, Mario Leutert, Stephanie Jungmichel, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 212
Rita Martello, Mario Leutert, Stephanie Jungmichel, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 212
Niraparib activates interferon signaling and potentiates anti-PD-1 antibody efficacy in tumor models
Zebin Wang, Kaiming Sun, Yonghong Xiao, et al.
Scientific Reports (2019) Vol. 9, Iss. 1
Open Access | Times Cited: 205
Zebin Wang, Kaiming Sun, Yonghong Xiao, et al.
Scientific Reports (2019) Vol. 9, Iss. 1
Open Access | Times Cited: 205
An Update on Poly(ADP-ribose)polymerase-1 (PARP-1) Inhibitors: Opportunities and Challenges in Cancer Therapy
Ying-Qing Wang, Pingyuan Wang, Yu-Ting Wang, et al.
Journal of Medicinal Chemistry (2016) Vol. 59, Iss. 21, pp. 9575-9598
Closed Access | Times Cited: 200
Ying-Qing Wang, Pingyuan Wang, Yu-Ting Wang, et al.
Journal of Medicinal Chemistry (2016) Vol. 59, Iss. 21, pp. 9575-9598
Closed Access | Times Cited: 200
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: 199
Marie-France Langelier, Levani Zandarashvili, Pedro M. Aguiar, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 199
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
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
Crosstalk between protein post-translational modifications and phase separation
Yang Liu, Wenjuan Feng, Yunshan Wang, et al.
Cell Communication and Signaling (2024) Vol. 22, Iss. 1
Open Access | Times Cited: 18
Yang Liu, Wenjuan Feng, Yunshan Wang, et al.
Cell Communication and Signaling (2024) Vol. 22, Iss. 1
Open Access | Times Cited: 18
Niraparib: A Poly(ADP-ribose) Polymerase (PARP) Inhibitor for the Treatment of Tumors with Defective Homologous Recombination
Philip Jones, Keith Wilcoxen, Michael Rowley, et al.
Journal of Medicinal Chemistry (2015) Vol. 58, Iss. 8, pp. 3302-3314
Closed Access | Times Cited: 145
Philip Jones, Keith Wilcoxen, Michael Rowley, et al.
Journal of Medicinal Chemistry (2015) Vol. 58, Iss. 8, pp. 3302-3314
Closed Access | Times Cited: 145
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
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
A Focused DNA-Encoded Chemical Library for the Discovery of Inhibitors of NAD+-Dependent Enzymes
Lik Hang Yuen, Srikanta Dana, Yu Liu, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 13, pp. 5169-5181
Closed Access | Times Cited: 98
Lik Hang Yuen, Srikanta Dana, Yu Liu, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 13, pp. 5169-5181
Closed Access | Times Cited: 98
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
HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones
Fa-Hui Sun, Peng Zhao, Nan Zhang, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 66
Fa-Hui Sun, Peng Zhao, Nan Zhang, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 66
MARTs and MARylation in the Cytosol: Biological Functions, Mechanisms of Action, and Therapeutic Potential
Sridevi Challa, MiKayla S Stokes, W. Lee Kraus
Cells (2021) Vol. 10, Iss. 2, pp. 313-313
Open Access | Times Cited: 56
Sridevi Challa, MiKayla S Stokes, W. Lee Kraus
Cells (2021) Vol. 10, Iss. 2, pp. 313-313
Open Access | Times Cited: 56
A potent and selective PARP14 inhibitor decreases protumor macrophage gene expression and elicits inflammatory responses in tumor explants
Laurie B. Schenkel, Jennifer R. Molina, Kerren K. Swinger, et al.
Cell chemical biology (2021) Vol. 28, Iss. 8, pp. 1158-1168.e13
Open Access | Times Cited: 56
Laurie B. Schenkel, Jennifer R. Molina, Kerren K. Swinger, et al.
Cell chemical biology (2021) Vol. 28, Iss. 8, pp. 1158-1168.e13
Open Access | Times Cited: 56
New directions in poly(ADP‐ribose) polymerase biology
Florian J. Bock, Paul Chang
FEBS Journal (2016) Vol. 283, Iss. 22, pp. 4017-4031
Open Access | Times Cited: 77
Florian J. Bock, Paul Chang
FEBS Journal (2016) Vol. 283, Iss. 22, pp. 4017-4031
Open Access | Times Cited: 77
Zinc finger domains as therapeutic targets for metal-based compounds – an update
Camilla Abbehausen
Metallomics (2018) Vol. 11, Iss. 1, pp. 15-28
Closed Access | Times Cited: 77
Camilla Abbehausen
Metallomics (2018) Vol. 11, Iss. 1, pp. 15-28
Closed Access | Times Cited: 77
Intracellular STING inactivation sensitizes breast cancer cells to genotoxic agents
Julie Gaston, Laura Cheradame, Vanessa Yvonnet, et al.
Oncotarget (2016) Vol. 7, Iss. 47, pp. 77205-77224
Open Access | Times Cited: 71
Julie Gaston, Laura Cheradame, Vanessa Yvonnet, et al.
Oncotarget (2016) Vol. 7, Iss. 47, pp. 77205-77224
Open Access | Times Cited: 71
Poly-ADP ribosylation in DNA damage response and cancer therapy
Wei‐Hsien Hou, Shih-Hsun Chen, Xiaochun Yu
Mutation Research/Reviews in Mutation Research (2017) Vol. 780, pp. 82-91
Open Access | Times Cited: 71
Wei‐Hsien Hou, Shih-Hsun Chen, Xiaochun Yu
Mutation Research/Reviews in Mutation Research (2017) Vol. 780, pp. 82-91
Open Access | Times Cited: 71