Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Generation and Characterization of Recombinant Antibody-like ADP-Ribose Binding Proteins
Bryan A. Gibson, Lesley B. Conrad, Dan Huang, et al.
Biochemistry (2017) Vol. 56, Iss. 48, pp. 6305-6316
Open Access | Times Cited: 113

Showing 1-25 of 113 citing articles:

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: 214
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
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
ADP-ribosylation from molecular mechanisms to therapeutic implications
Marcin J. Suskiewicz, Evgeniia Prokhorova, J.G.M. Rack, et al.
Cell (2023) Vol. 186, Iss. 21, pp. 4475-4495
Open Access | Times Cited: 72
HPF1-dependent histone ADP-ribosylation triggers chromatin relaxation to promote the recruitment of repair factors at sites of DNA damage
Rebecca Smith, Siham Zentout, Magdalena B. Rother, et al.
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 5, pp. 678-691
Open Access | Times Cited: 45
Ubiquitin is directly linked via an ester to protein-conjugated mono-ADP-ribose
Daniel S. Bejan, Rachel E. Lacoursiere, Jonathan N. Pruneda, et al.
The EMBO Journal (2025)
Open Access | Times Cited: 3
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
The SARS-CoV-2 Conserved Macrodomain Is a Mono-ADP-Ribosylhydrolase
Yousef M. Alhammad, M.M. Kashipathy, Anuradha Roy, et al.
Journal of Virology (2020) Vol. 95, Iss. 3
Open Access | Times Cited: 121
ADP-ribosyl–binding and hydrolase activities of the alphavirus nsP3 macrodomain are critical for initiation of virus replication
Rachy Abraham, Debra Hauer, Robert Lyle McPherson, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 44
Open Access | Times Cited: 119
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
Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease
Evgeniia Prokhorova, Thomas Agnew, Anne R. Wondisford, et al.
Molecular Cell (2021) Vol. 81, Iss. 12, pp. 2640-2655.e8
Open Access | Times Cited: 81
ADP-ribosylation of RNA and DNA: fromin vitrocharacterization toin vivofunction
Lisa Weixler, Katja Schäringer, Jeffrey Momoh, et al.
Nucleic Acids Research (2021) Vol. 49, Iss. 7, pp. 3634-3650
Open Access | Times Cited: 68
Ribosome ADP-ribosylation inhibits translation and maintains proteostasis in cancers
Sridevi Challa, B.R. Khulpateea, Tulip Nandu, et al.
Cell (2021) Vol. 184, Iss. 17, pp. 4531-4546.e26
Open Access | Times Cited: 67
HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications
Marie-France Langelier, Ramya Billur, Aleksandr Sverzhinsky, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 56
Poly(ADP-ribosylation) of P-TEFb by PARP1 disrupts phase separation to inhibit global transcription after DNA damage
Huanyi Fu, Rongdiao Liu, Zixuan Jia, et al.
Nature Cell Biology (2022) Vol. 24, Iss. 4, pp. 513-525
Open Access | Times Cited: 52
Modular antibodies reveal DNA damage-induced mono-ADP-ribosylation as a second wave of PARP1 signaling
Edoardo José Longarini, Helen Dauben, Carolina Locatelli, et al.
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1743-1760.e11
Open Access | Times Cited: 38
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
A viral ADP-ribosyltransferase attaches RNA chains to host proteins
Maik Wolfram-Schauerte, Nadiia Pozhydaieva, Julia Grawenhoff, et al.
Nature (2023) Vol. 620, Iss. 7976, pp. 1054-1062
Open Access | Times Cited: 29
Chemoenzymatic and Synthetic Approaches To Investigate Aspartate- and Glutamate-ADP-Ribosylation
Kyuto Tashiro, Sven Wijngaarden, Jugal Mohapatra, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 25, pp. 14000-14009
Open Access | Times Cited: 25
PARP14 is a writer, reader, and eraser of mono-ADP-ribosylation
Archimede Torretta, Constantinos Chatzicharalampous, Carmen Ebenwaldner, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 9, pp. 105096-105096
Open Access | Times Cited: 24
Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
Edoardo José Longarini, Ivan Matić
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 16
PARP14 is regulated by the PARP9/DTX3L complex and promotes interferon γ-induced ADP-ribosylation
Victória Chaves Ribeiro, Lilian C. Russo, Nícolas C. Hoch
The EMBO Journal (2024) Vol. 43, Iss. 14, pp. 2908-2928
Open Access | Times Cited: 9
Engineering Af1521 improves ADP-ribose binding and identification of ADP-ribosylated proteins
Kathrin Nowak, Florian Rosenthal, T. Karlberg, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 67
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
Functional Interplay between Histone H2B ADP-Ribosylation and Phosphorylation Controls Adipogenesis
Dan Huang, Cristel V. Camacho, Rohit Setlem, et al.
Molecular Cell (2020) Vol. 79, Iss. 6, pp. 934-949.e14
Open Access | Times Cited: 58
Page 1 - Next Page

Scroll to top