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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:

A Bifunctional NAD+ for Profiling Poly-ADP-Ribosylation-Dependent Interacting Proteins
Albert T. Lam, Xiaonan Zhang, Valentine V. Courouble, et al.
ACS Chemical Biology (2021) Vol. 16, Iss. 2, pp. 389-396
Open Access | Times Cited: 24

Showing 24 citing articles:

Recent advances in activity-based probes (ABPs) and affinity-based probes (AfBPs) for profiling of enzymes
Haixiao Fang, Bo Peng, Sing Yee Ong, et al.
Chemical Science (2021) Vol. 12, Iss. 24, pp. 8288-8310
Open Access | Times Cited: 124
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
PARPs and ADP-ribosylation-mediated biomolecular condensates: determinants, dynamics, and disease implications
Hongrui Liu, Meenakshi Pillai, Anthony K. L. Leung
Trends in Biochemical Sciences (2025)
Closed Access | Times Cited: 1
Channeling Nicotinamide Phosphoribosyltransferase (NAMPT) to Address Life and Death
Velma Ganga Reddy, Isabella S. Krider, Erick T. M. Alves, et al.
Journal of Medicinal Chemistry (2024) Vol. 67, Iss. 8, pp. 5999-6026
Open Access | Times Cited: 6
Reading ADP-ribosylation signaling using chemical biology and interaction proteomics
Katarzyna W. Kliza, Qiang Liu, Laura W.M. Roosenboom, et al.
Molecular Cell (2021) Vol. 81, Iss. 21, pp. 4552-4567.e8
Open Access | Times Cited: 40
Regulation of stress granule maturation and dynamics by poly(ADP-ribose) interaction with PARP13
Shang-Jung Cheng, Temitope Gafaar, Jijin R. A. Kuttiyatveetil, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Functionalised Cofactor Mimics for Interactome Discovery and Beyond
Isabel V. L. Wilkinson, Martin Pfanzelt, Stephan A. Sieber
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 29
Open Access | Times Cited: 18
Recent advances in the synthesis of poly (ADP-ribose)
Yidan Wu, Tang Li, Qiang Liu
Bioorganic & Medicinal Chemistry (2025) Vol. 125, pp. 118202-118202
Closed Access
Discovery of an NAD+ analogue with enhanced specificity for PARP1
Xiaonan Zhang, Albert T. Lam, Qinqin Cheng, et al.
Chemical Science (2022) Vol. 13, Iss. 7, pp. 1982-1991
Open Access | Times Cited: 16
Synthesis of Bispecific Antibody Conjugates Using Functionalized Poly-ADP-ribose Polymers
Qinqin Cheng, Xiaonan Zhang, Jiawei Li, et al.
Biochemistry (2023) Vol. 62, Iss. 6, pp. 1138-1144
Closed Access | Times Cited: 7
Cofactor and Process Engineering for Nicotinamide Recycling and Retention in Intensified Biocatalysis
Raquel Abdallah da Rocha, Andrea J. North, Robert Speight, et al.
Catalysts (2022) Vol. 12, Iss. 11, pp. 1454-1454
Open Access | Times Cited: 10
Evaluation of micropillar array columns for chromatographic separation of phosphorothioated oligonucleotides and their diastereomers
Lieve Dillen, Tiny Deschrijver, Kurt Van Mol, et al.
Analytical Science Advances (2021) Vol. 2, Iss. 7-8, pp. 354-363
Open Access | Times Cited: 11
A ribose-functionalized NAD+ with versatile activity for ADP-ribosylation
Elisa Stephens, Xiaonan Zhang, Albert T. Lam, et al.
Chemical Communications (2023) Vol. 59, Iss. 93, pp. 13843-13846
Closed Access | Times Cited: 4
A Poly-ADP-Ribose Polymer–GCSF Conjugate
Qinqin Cheng, Xiaonan Zhang, Lei Zhang, et al.
Biomacromolecules (2022) Vol. 23, Iss. 12, pp. 5267-5272
Open Access | Times Cited: 6
Catching mono- and poly-ADP-ribose readers with synthetic ADP-ribose baits
Michael S. Cohen
Molecular Cell (2021) Vol. 81, Iss. 21, pp. 4351-4353
Closed Access | Times Cited: 4
Nicotinamide Riboside and CD38: Covalent Inhibition and Live-Cell Labeling
Guoyun Kao, Xiaonan Zhang, Fariborz Nasertorabi, et al.
JACS Au (2024) Vol. 4, Iss. 11, pp. 4345-4360
Open Access
An NAD+ with Dually Modified Adenine for Labeling ADP-Ribosylation-Specific Proteins
Lei Zhang, Xiaonan Zhang, Arshad J. Ansari, et al.
Tetrahedron (2024) Vol. 168, pp. 134361-134361
Closed Access
Mass spectrometry-based candidate substrate and site identification of PTM enzymes
Weiyu Chen, Guanghui Ji, Roujun Wu, et al.
TrAC Trends in Analytical Chemistry (2023) Vol. 160, pp. 116991-116991
Closed Access | Times Cited: 1
The quest to identify ADP-ribosylation readers: methodological advances
S. Weijers, Michiel Vermeulen, Katarzyna W. Kliza
Trends in Biochemical Sciences (2024) Vol. 49, Iss. 11, pp. 1000-1013
Closed Access
Discovery of PARP1-Sparing Inhibitors for Protein ADP-Ribosylation
Elisa Stephens, Liang‐Chieh Chen, Arshad J. Ansari, et al.
ACS Medicinal Chemistry Letters (2024) Vol. 15, Iss. 11, pp. 1940-1946
Open Access
Funktionalisierte Cofaktor‐Analoga für die Erforschung von Interaktomen und darüber hinaus
Isabel V. L. Wilkinson, Martin Pfanzelt, Stephan A. Sieber
Angewandte Chemie (2022) Vol. 134, Iss. 29
Open Access | Times Cited: 2
Generation of Bispecific Antibodies by Functionalized Poly‐ADP‐Ribose Polymers
Hyo Sun Kim, Yong Zhang
Current Protocols (2023) Vol. 3, Iss. 12
Open Access
Synthesis and biological evaluation of novel photo-clickable adenosine and cyclic ADP-ribose analogs: 8-N3-2′-O-propargyladenosine and 8-N3-2′-O-propargyl-cADPR
Divya Andy, Gihan S. Gunaratne, Jonathan S. Marchant, et al.
Bioorganic & Medicinal Chemistry (2022) Vol. 76, pp. 117099-117099
Open Access
Analyzing PARP1 Activity: Small Molecule Reactants and Attached Chains of Poly (ADP-Ribose)
Johannes Rudolph, Karolin Luger
Methods in molecular biology (2022), pp. 61-73
Closed Access
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