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:

PTM-Shepherd: Analysis and Summarization of Post-Translational and Chemical Modifications From Open Search Results
Daniel Geiszler, Andy T. Kong, Dmitry M. Avtonomov, et al.
Molecular & Cellular Proteomics (2020) Vol. 20, pp. 100018-100018
Open Access | Times Cited: 104

Showing 1-25 of 104 citing articles:

Identification of modified peptides using localization-aware open search
Fengchao Yu, Guo Ci Teo, Andy T. Kong, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 227

Decoding Post-Translational Modification Crosstalk With Proteomics
Mario Leutert, Samuel W. Entwisle, Judit Villén
Molecular & Cellular Proteomics (2021) Vol. 20, pp. 100129-100129
Open Access | Times Cited: 160

Glycoproteomics
Ieva Bagdonaite, Stacy A. Malaker, Daniel A. Polasky, et al.
Nature Reviews Methods Primers (2022) Vol. 2, Iss. 1
Open Access | Times Cited: 156

Cancer proteogenomics: current impact and future prospects
D.R. Mani, Karsten Krug, Bing Zhang, et al.
Nature reviews. Cancer (2022) Vol. 22, Iss. 5, pp. 298-313
Closed Access | Times Cited: 148

MSBooster: improving peptide identification rates using deep learning-based features
Kevin Yang, Fengchao Yu, Guo Ci Teo, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 99

Glyco-Decipher enables glycan database-independent peptide matching and in-depth characterization of site-specific N-glycosylation
Zheng Fang, Hongqiang Qin, Jiawei Mao, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 79

In Search of a Universal Method: A Comparative Survey of Bottom-Up Proteomics Sample Preparation Methods
Gina Varnavides, Moritz Madern, Dorothea Anrather, et al.
Journal of Proteome Research (2022) Vol. 21, Iss. 10, pp. 2397-2411
Open Access | Times Cited: 71

Mechanisms of assembly and remodelling of the extracellular matrix
Alexandra Naba
Nature Reviews Molecular Cell Biology (2024)
Closed Access | Times Cited: 42

Acquisition and Analysis of DIA-Based Proteomic Data: A Comprehensive Survey in 2023
Ronghui Lou, Wenqing Shui
Molecular & Cellular Proteomics (2024) Vol. 23, Iss. 2, pp. 100712-100712
Open Access | Times Cited: 39

diaTracer enables spectrum-centric analysis of diaPASEF proteomics data
Kai Li, Guo Ci Teo, Kevin Yang, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 3

The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome
Ivo A. Hendriks, Sara C. Buch-Larsen, Evgeniia Prokhorova, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 81

Proteomes Are of Proteoforms: Embracing the Complexity
Katrina Carbonara, Martin Andonovski, Jens R. Coorssen
Proteomes (2021) Vol. 9, Iss. 3, pp. 38-38
Open Access | Times Cited: 78

Post-translational modifications reshape the antigenic landscape of the MHC I immunopeptidome in tumors
Assaf Kacen, Aaron Javitt, Matthias P. Kramer, et al.
Nature Biotechnology (2022) Vol. 41, Iss. 2, pp. 239-251
Closed Access | Times Cited: 68

Identification and characterization of post-translational modifications: Clinical implications
Juliane Hermann, Leon J. Schurgers, Vera Jankowski
Molecular Aspects of Medicine (2022) Vol. 86, pp. 101066-101066
Open Access | Times Cited: 67

Reversed-Phase Liquid Chromatography of Peptides for Bottom-Up Proteomics: A Tutorial
Juraj Lenčo, Siddharth Jadeja, Denis K. Naplekov, et al.
Journal of Proteome Research (2022) Vol. 21, Iss. 12, pp. 2846-2892
Open Access | Times Cited: 41

De novo peptide sequencing with InstaNovo: Accurate, database-free peptide identification for large scale proteomics experiments
Kevin Eloff, Konstantinos Kalogeropoulos, Oliver Morell, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 27

Comprehensive proteogenomic characterization of rare kidney tumors
Ginny Xiaohe Li, Lijun Chen, Yi Hsiao, et al.
Cell Reports Medicine (2024) Vol. 5, Iss. 5, pp. 101547-101547
Open Access | Times Cited: 13

A multi-purpose, regenerable, proteome-scale, human phosphoserine resource for phosphoproteomics
Brandon M. Gassaway, Jiaming Li, Ramin Rad, et al.
Nature Methods (2022) Vol. 19, Iss. 11, pp. 1371-1375
Open Access | Times Cited: 34

Multiattribute Glycan Identification and FDR Control for Glycoproteomics
Daniel A. Polasky, Daniel Geiszler, Fengchao Yu, et al.
Molecular & Cellular Proteomics (2022) Vol. 21, Iss. 3, pp. 100205-100205
Open Access | Times Cited: 29

Detecting diagnostic features in MS/MS spectra of post-translationally modified peptides
Daniel Geiszler, Daniel A. Polasky, Fengchao Yu, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 22

A region‐resolved proteomic map of the human brain enabled by high‐throughput proteomics
Johanna Tüshaus, Amirhossein Sakhteman, Severin Lechner, et al.
The EMBO Journal (2023) Vol. 42, Iss. 23
Open Access | Times Cited: 15

Identification of triazenyl indoles as inhibitors of fungal fatty acid biosynthesis with broad-spectrum activity
Kali R. Iyer, Sheena C. Li, Nicole M. Revie, et al.
Cell chemical biology (2023) Vol. 30, Iss. 7, pp. 795-810.e8
Open Access | Times Cited: 14

Comparative study on composition and functional properties of brewer’s spent grain proteins precipitated by citric acid and hydrochloric acid
Toktam Farjami, Animesh Sharma, Lars Hagen, et al.
Food Chemistry (2024) Vol. 446, pp. 138863-138863
Closed Access | Times Cited: 5

PTMVision: An Interactive Visualization Webserver for Post-translational Modifications of Proteins
Simon T. Hackl, Caroline Jachmann, Mathias Witte Paz, et al.
Journal of Proteome Research (2025) Vol. 24, Iss. 2, pp. 919-928
Open Access

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