ArticleClinical mass spectrometry (Del Mar, Calif.)2019
Rapid method towards proteomic analysis of dried blood spots by MALDI mass spectrometry.
Article in Clinical mass spectrometry (Del Mar, Calif.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- From blood drops to biomarkers: a scoping review of microsampling in mass spectrometry-based proteomics.Clinical proteomics · 2025Review
- 6-Aza-2-Thiothymine as an Alternative Matrix for Spatial Proteomics with MALDI-MSI.International journal of molecular sciences · 2024Article
- Advancements in clinical approaches, analytical methods, and smart sampling for LC-MS-based protein determination from dried matrix spots.Journal of separation science · 2024Review
- Current State and Innovations in Newborn Screening: Continuing to Do Good and Avoid Harm.International journal of neonatal screening · 2023Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neonatal dried blood spots (DBS) are routinely utilized in the clinical setting as a diagnostic tool for various genetic disorders and infectious diseases. DBS allow for minimally invasive, small volume blood collection and are stored at room temperature. Neonatal whole blood and serum samples can be important in determining genetic risk factors and predicting infantile disease; however, at the present time, limited methods exist for rapidly analyzing DBS samples for their proteomic profile, years after samples have been collected. A novel method is presented for the extraction and analysis of target proteins and peptides from neonatal DBS using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Extraction parameters were optimized to achieve ideal signal intensity and resolution to obtain protein identifications. Samples were extracted from filter paper with 0.1% TFA in H
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Registered trials
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