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:
Nudix hydrolases degrade protein-conjugated ADP-ribose
Casey M. Daniels, Puchong Thirawatananond, Shao‐En Ong, et al.
Scientific Reports (2015) Vol. 5, Iss. 1
Open Access | Times Cited: 62
Casey M. Daniels, Puchong Thirawatananond, Shao‐En Ong, et al.
Scientific Reports (2015) Vol. 5, Iss. 1
Open Access | Times Cited: 62
Showing 1-25 of 62 citing articles:
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
Rebecca Gupte, Ziying Liu, W. Lee Kraus
Genes & Development (2017) Vol. 31, Iss. 2, pp. 101-126
Open Access | Times Cited: 618
Serine ADP-Ribosylation Depends on HPF1
Juán José Bonfiglio, Pietro Fontana, Qi Zhang, et al.
Molecular Cell (2017) Vol. 65, Iss. 5, pp. 932-940.e6
Open Access | Times Cited: 315
Juán José Bonfiglio, Pietro Fontana, Qi Zhang, et al.
Molecular Cell (2017) Vol. 65, Iss. 5, pp. 932-940.e6
Open Access | Times Cited: 315
Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination
Sagar Bhogaraju, Sissy Kalayil, Yaobin Liu, et al.
Cell (2016) Vol. 167, Iss. 6, pp. 1636-1649.e13
Open Access | Times Cited: 281
Sagar Bhogaraju, Sissy Kalayil, Yaobin Liu, et al.
Cell (2016) Vol. 167, Iss. 6, pp. 1636-1649.e13
Open Access | Times Cited: 281
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
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: 224
Bernhard Lüscher, Mareike Bütepage, Laura Eckei, et al.
Chemical Reviews (2017) Vol. 118, Iss. 3, pp. 1092-1136
Closed Access | Times Cited: 224
Serine is a new target residue for endogenous ADP-ribosylation on histones
Orsolya Leidecker, Juán José Bonfiglio, Thomas Colby, et al.
Nature Chemical Biology (2016) Vol. 12, Iss. 12, pp. 998-1000
Open Access | Times Cited: 220
Orsolya Leidecker, Juán José Bonfiglio, Thomas Colby, et al.
Nature Chemical Biology (2016) Vol. 12, Iss. 12, pp. 998-1000
Open Access | Times Cited: 220
A Single Legionella Effector Catalyzes a Multistep Ubiquitination Pathway to Rearrange Tubular Endoplasmic Reticulum for Replication
Kristin M. Kotewicz, Vinay Ramabhadran, Nicole M. Sjoblom, et al.
Cell Host & Microbe (2016) Vol. 21, Iss. 2, pp. 169-181
Open Access | Times Cited: 189
Kristin M. Kotewicz, Vinay Ramabhadran, Nicole M. Sjoblom, et al.
Cell Host & Microbe (2016) Vol. 21, Iss. 2, pp. 169-181
Open Access | Times Cited: 189
ADP-ribosylhydrolase activity of Chikungunya virus macrodomain is critical for virus replication and virulence
Robert Lyle McPherson, Rachy Abraham, Easwaran Sreekumar, et al.
Proceedings of the National Academy of Sciences (2017) Vol. 114, Iss. 7, pp. 1666-1671
Open Access | Times Cited: 176
Robert Lyle McPherson, Rachy Abraham, Easwaran Sreekumar, et al.
Proceedings of the National Academy of Sciences (2017) Vol. 114, Iss. 7, pp. 1666-1671
Open Access | Times Cited: 176
Reversible mono‐ADP‐ribosylation of DNA breaks
Deeksha Munnur, Ivan Ahel
FEBS Journal (2017) Vol. 284, Iss. 23, pp. 4002-4016
Open Access | Times Cited: 142
Deeksha Munnur, Ivan Ahel
FEBS Journal (2017) Vol. 284, Iss. 23, pp. 4002-4016
Open Access | Times Cited: 142
Emerging roles of eraser enzymes in the dynamic control of protein ADP-ribosylation
Julia O’Sullivan, Maria Tedim Ferreira, Jean‐Philippe Gagné, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 141
Julia O’Sullivan, Maria Tedim Ferreira, Jean‐Philippe Gagné, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 141
Luca Palazzo, Andreja Mikoč, Ivan Ahel
FEBS Journal (2017) Vol. 284, Iss. 18, pp. 2932-2946
Open Access | Times Cited: 129
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
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
An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation
Juán José Bonfiglio, Orsolya Leidecker, Helen Dauben, et al.
Cell (2020) Vol. 183, Iss. 4, pp. 1086-1102.e23
Open Access | Times Cited: 90
Juán José Bonfiglio, Orsolya Leidecker, Helen Dauben, et al.
Cell (2020) Vol. 183, Iss. 4, pp. 1086-1102.e23
Open Access | Times Cited: 90
PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools
Morgan Dasovich, Anthony K. L. Leung
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1552-1572
Open Access | Times Cited: 34
Morgan Dasovich, Anthony K. L. Leung
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1552-1572
Open Access | Times Cited: 34
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: 72
Wei‐Hsien Hou, Shih-Hsun Chen, Xiaochun Yu
Mutation Research/Reviews in Mutation Research (2017) Vol. 780, pp. 82-91
Open Access | Times Cited: 72
Luca Palazzo, Casey M. Daniels, Joanne E. Nettleship, et al.
FEBS Journal (2016) Vol. 283, Iss. 18, pp. 3371-3388
Open Access | Times Cited: 71
ELTA: Enzymatic Labeling of Terminal ADP-Ribose
Yoshinari Ando, Elad Elkayam, Robert Lyle McPherson, et al.
Molecular Cell (2019) Vol. 73, Iss. 4, pp. 845-856.e5
Open Access | Times Cited: 65
Yoshinari Ando, Elad Elkayam, Robert Lyle McPherson, et al.
Molecular Cell (2019) Vol. 73, Iss. 4, pp. 845-856.e5
Open Access | Times Cited: 65
The evolution of function within the Nudix homology clan
John R. Srouji, Anting Xu, Annsea Park, et al.
Proteins Structure Function and Bioinformatics (2016) Vol. 85, Iss. 5, pp. 775-811
Open Access | Times Cited: 64
John R. Srouji, Anting Xu, Annsea Park, et al.
Proteins Structure Function and Bioinformatics (2016) Vol. 85, Iss. 5, pp. 775-811
Open Access | Times Cited: 64
Why structure and chain length matter: on the biological significance underlying the structural heterogeneity of poly(ADP-ribose)
Julia M. Reber, Aswin Mangerich
Nucleic Acids Research (2021) Vol. 49, Iss. 15, pp. 8432-8448
Open Access | Times Cited: 45
Julia M. Reber, Aswin Mangerich
Nucleic Acids Research (2021) Vol. 49, Iss. 15, pp. 8432-8448
Open Access | Times Cited: 45
High-Throughput Activity Assay for Screening Inhibitors of the SARS-CoV-2 Mac1 Macrodomain
Morgan Dasovich, Junlin Zhuo, Jack A. Goodman, et al.
ACS Chemical Biology (2021) Vol. 17, Iss. 1, pp. 17-23
Open Access | Times Cited: 42
Morgan Dasovich, Junlin Zhuo, Jack A. Goodman, et al.
ACS Chemical Biology (2021) Vol. 17, Iss. 1, pp. 17-23
Open Access | Times Cited: 42
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
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
PARPs in genome stability and signal transduction: implications for cancer therapy
Luca Palazzo, Ivan Ahel
Biochemical Society Transactions (2018) Vol. 46, Iss. 6, pp. 1681-1695
Open Access | Times Cited: 59
Luca Palazzo, Ivan Ahel
Biochemical Society Transactions (2018) Vol. 46, Iss. 6, pp. 1681-1695
Open Access | Times Cited: 59
MacroD1 Is a Promiscuous ADP-Ribosyl Hydrolase Localized to Mitochondria
Thomas Agnew, Deeksha Munnur, Kerryanne Crawford, et al.
Frontiers in Microbiology (2018) Vol. 9
Open Access | Times Cited: 49
Thomas Agnew, Deeksha Munnur, Kerryanne Crawford, et al.
Frontiers in Microbiology (2018) Vol. 9
Open Access | Times Cited: 49
Mass spectrometry for serine ADP-ribosylation? Think o-glycosylation!
Juán José Bonfiglio, Thomas Colby, Ivan Matić
Nucleic Acids Research (2017) Vol. 45, Iss. 11, pp. 6259-6264
Open Access | Times Cited: 47
Juán José Bonfiglio, Thomas Colby, Ivan Matić
Nucleic Acids Research (2017) Vol. 45, Iss. 11, pp. 6259-6264
Open Access | Times Cited: 47
