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:
Protocol for high-throughput semi-automated label-free- or TMT-based phosphoproteome profiling
Claire Koenig, Ana Martínez‐Val, Previn Naicker, et al.
STAR Protocols (2023) Vol. 4, Iss. 3, pp. 102536-102536
Open Access | Times Cited: 14
Claire Koenig, Ana Martínez‐Val, Previn Naicker, et al.
STAR Protocols (2023) Vol. 4, Iss. 3, pp. 102536-102536
Open Access | Times Cited: 14
Showing 14 citing articles:
One-Tip enables comprehensive proteome coverage in minimal cells and single zygotes
Zilu Ye, Pierre Sabatier, Javier Martín‐González, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 35
Zilu Ye, Pierre Sabatier, Javier Martín‐González, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 35
Systematic Optimization of Automated Phosphopeptide Enrichment for High-Sensitivity Phosphoproteomics
Patricia Bortel, Ilaria Piga, Claire Koenig, et al.
Molecular & Cellular Proteomics (2024) Vol. 23, Iss. 5, pp. 100754-100754
Open Access | Times Cited: 18
Patricia Bortel, Ilaria Piga, Claire Koenig, et al.
Molecular & Cellular Proteomics (2024) Vol. 23, Iss. 5, pp. 100754-100754
Open Access | Times Cited: 18
Mag-Net: Rapid enrichment of membrane-bound particles enables high coverage quantitative analysis of the plasma proteome
Christine Wu, Kristine A. Tsantilas, Jea Park, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 26
Christine Wu, Kristine A. Tsantilas, Jea Park, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 26
TIMAHAC: Streamlined Tandem IMAC-HILIC Workflow for Simultaneous and High-Throughput Plant Phosphoproteomics and N-glycoproteomics
Chin-Wen Chen, Pei-Yi Lin, Ying-Mi Lai, et al.
Molecular & Cellular Proteomics (2024) Vol. 23, Iss. 5, pp. 100762-100762
Open Access | Times Cited: 6
Chin-Wen Chen, Pei-Yi Lin, Ying-Mi Lai, et al.
Molecular & Cellular Proteomics (2024) Vol. 23, Iss. 5, pp. 100762-100762
Open Access | Times Cited: 6
Macrocycle-based PROTACs selectively degrade cyclophilin A and inhibit HIV-1 and HCV
Lydia S. Newton, Clara Gathmann, Sophie Ridewood, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Lydia S. Newton, Clara Gathmann, Sophie Ridewood, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Addressing NHS chemistry: Efficient quenching of excess TMT reagent and reversing TMT-over labelling in proteomic samples by methylamine
Yana Demyanenko, Xintong Sui, Andrew M. Giltrap, et al.
Molecular & Cellular Proteomics (2025), pp. 100948-100948
Open Access
Yana Demyanenko, Xintong Sui, Andrew M. Giltrap, et al.
Molecular & Cellular Proteomics (2025), pp. 100948-100948
Open Access
Repurposed 3D Printer Allows Economical and Programmable Fraction Collection for Proteomics of Nanogram Scale Samples
Eduardo S. Kitano, Gareth Nisbet, Yana Demyanenko, et al.
Analytical Chemistry (2024) Vol. 96, Iss. 28, pp. 11439-11447
Open Access | Times Cited: 1
Eduardo S. Kitano, Gareth Nisbet, Yana Demyanenko, et al.
Analytical Chemistry (2024) Vol. 96, Iss. 28, pp. 11439-11447
Open Access | Times Cited: 1
Advancements in Global Phosphoproteomics Profiling: Overcoming Challenges in Sensitivity and Quantification
Gul Muneer, Ciao‐Syuan Chen, Yu‐Ju Chen
PROTEOMICS (2024)
Open Access | Times Cited: 1
Gul Muneer, Ciao‐Syuan Chen, Yu‐Ju Chen
PROTEOMICS (2024)
Open Access | Times Cited: 1
Systematic optimization of automated phosphopeptide enrichment for high-sensitivity phosphoproteomics
Patricia Bortel, Ilaria Piga, Claire Koenig, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
Patricia Bortel, Ilaria Piga, Claire Koenig, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
Cheap, Robust and Versatile Two-Dimensional Chromatography system for Proteomics of Nanogram Scale Samples
Eduardo S. Kitano, Gareth Nisbet, Yana Demyanenko, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Eduardo S. Kitano, Gareth Nisbet, Yana Demyanenko, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Removal of NHS-labelling by-products in Proteomic Samples
Yana Demyanenko, Andrew M. Giltrap, Benjamin G. Davis, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Yana Demyanenko, Andrew M. Giltrap, Benjamin G. Davis, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Phosphoproteomics highlights complex resource management upon inflammatory stimulation of fibroblasts
Patricia Bortel, Ana Martínez‐Val, Gerhard Hagn, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Patricia Bortel, Ana Martínez‐Val, Gerhard Hagn, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Multi-layered proteomics identifies insulin-induced upregulation of the EphA2 receptor via the ERK pathway which is dependent on low IGF1R level
Sarah Hyllekvist Jørgensen, Kristina B. Emdal, Anna-Kathrine Pedersen, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access
Sarah Hyllekvist Jørgensen, Kristina B. Emdal, Anna-Kathrine Pedersen, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access
Multi-layered proteomics identifies insulin-induced upregulation of the EphA2 receptor via the ERK pathway and dependent on low IGF1R level
Sarah Hyllekvist Jørgensen, Kristina B. Emdal, Anna-Kathrine Pedersen, et al.
(2023)
Closed Access
Sarah Hyllekvist Jørgensen, Kristina B. Emdal, Anna-Kathrine Pedersen, et al.
(2023)
Closed Access
