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OpenAlex Citation Counts

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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:

ADP-Ribosylated Peptide Enrichment and Site Identification: The Phosphodiesterase-Based Method
Casey M. Daniels, Shao‐En Ong, Anthony K. L. Leung
Methods in molecular biology (2017), pp. 79-93
Open Access | Times Cited: 20

Showing 20 citing articles:

The Role of Electron Transfer Dissociation in Modern Proteomics
Nicholas M. Riley, Joshua J. Coon
Analytical Chemistry (2017) Vol. 90, Iss. 1, pp. 40-64
Open Access | Times Cited: 156
Enabling drug discovery for the PARP protein family through the detection of mono-ADP-ribosylation
Alvin Lu, Ryan Abo, Yue Ren, et al.
Biochemical Pharmacology (2019) Vol. 167, pp. 97-106
Open Access | Times Cited: 46
Enrichments of post‐translational modifications in proteomic studies
Luisa Pieroni, Federica Iavarone, Alessandra Olianas, et al.
Journal of Separation Science (2019) Vol. 43, Iss. 1, pp. 313-336
Open Access | Times Cited: 45
The multifaceted role of PARP1 in RNA biogenesis
Rebekah Eleazer, Yvonne Fondufe‐Mittendorf
Wiley Interdisciplinary Reviews - RNA (2020) Vol. 12, Iss. 2
Open Access | Times Cited: 41
Androgen signaling uses a writer and a reader of ADP-ribosylation to regulate protein complex assembly
Chunsong Yang, Kasey Jividen, Teddy Kamata, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 29
PARPs and ADP-Ribosylation in Chronic Inflammation: A Focus on Macrophages
Diego Vinicius Santinelli Pestana, Elena Aïkawa, Sasha A. Singh, et al.
Pathogens (2023) Vol. 12, Iss. 7, pp. 964-964
Open Access | Times Cited: 8
ADPredict: ADP-ribosylation site prediction based on physicochemical and structural descriptors
Matteo Lo Monte, Candida Manelfi, Marica Gemei, et al.
Bioinformatics (2018) Vol. 34, Iss. 15, pp. 2566-2574
Open Access | Times Cited: 21
Uncommon posttranslational modifications in proteomics: ADP‐ribosylation, tyrosine nitration, and tyrosine sulfation
Aarti Bashyal, Jennifer S. Brodbelt
Mass Spectrometry Reviews (2022) Vol. 43, Iss. 2, pp. 289-326
Closed Access | Times Cited: 10
Hydrofluoric Acid-Based Derivatization Strategy To Profile PARP-1 ADP-Ribosylation by LC–MS/MS
Jean‐Philippe Gagné, Marie-France Langelier, John M. Pascal, et al.
Journal of Proteome Research (2018) Vol. 17, Iss. 7, pp. 2542-2551
Closed Access | Times Cited: 17
Dynamic ADP-Ribosylome, Phosphoproteome, and Interactome in LPS-Activated Macrophages
Casey M. Daniels, Pauline R. Kaplan, Isaac Bishof, et al.
Journal of Proteome Research (2020) Vol. 19, Iss. 9, pp. 3716-3731
Open Access | Times Cited: 16
Proteomics techniques in protein biomarker discovery
Mahsa Babaei, Soheila Kashanian, Huang‐Teck Lee, et al.
Quantitative Biology (2024) Vol. 12, Iss. 1, pp. 53-69
Open Access | Times Cited: 1
Cryptic phosphoribosylase activity of NAMPT restricts the virion incorporation of viral proteins
Shu Feng, Na Xie, Yongzhen Liu, et al.
Nature Metabolism (2024) Vol. 6, Iss. 12, pp. 2300-2318
Closed Access | Times Cited: 1
Insight into the Binding and Hydrolytic Preferences of hNudt16 Based on Nucleotide Diphosphate Substrates
Magdalena Chrabąszczewska, Maria Winiewska‐Szajewska, Natalia Ostrowska, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 20, pp. 10929-10929
Open Access | Times Cited: 9
Poly(ADP-Ribose) Polymerase
Alexei V. Tulin
Methods in molecular biology (2017)
Closed Access | Times Cited: 9
A Novel Spectral Annotation Strategy Streamlines Reporting of Mono-ADP-ribosylated Peptides Derived from Mouse Liver and Spleen in Response to IFN-γ
Shiori Kuraoka, Hideyuki Higashi, Yoshihiro Yanagihara, et al.
Molecular & Cellular Proteomics (2021) Vol. 21, Iss. 4, pp. 100153-100153
Open Access | Times Cited: 7
A Combined Gas-Phase Separation Strategy for ADP-ribosylated Peptides
Taku Kasai, Shiori Kuraoka, Hideyuki Higashi, et al.
Journal of the American Society for Mass Spectrometry (2023) Vol. 34, Iss. 10, pp. 2136-2145
Open Access | Times Cited: 1
Biomarker Discovery
Odangowei Inetiminebi Ogidi, Mukul Machhindra Barwant, Ebifanimi Okara
Advances in medical diagnosis, treatment, and care (AMDTC) book series (2024), pp. 115-150
Closed Access
Simultaneous, Quantitative Characterization of Protein ADP-Ribosylation and Protein Phosphorylation in Macrophages
Casey M. Daniels, Arthur Nuccio, Pauline R. Kaplan, et al.
Methods in molecular biology (2020), pp. 145-160
Closed Access | Times Cited: 2
The Interferon-inducible NAMPT acts as a protein phosphoribosylase to restrict viral infection
Shu Zhang, Na Xie, Yongzhen Liu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Development of a mass-spectrometry based method for the identification of thein vivowhole blood and plasma ADP-ribosylomes
Stephanie C. Lüthi, Anna Howald, Kathrin Nowak, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access
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