ArticleAnalytical chemistry2017
Deep-Dive Targeted Quantification for Ultrasensitive Analysis of Proteins in Nondepleted Human Blood Plasma/Serum and Tissues.
Article in Analytical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Recent developments in mass-spectrometry-based targeted proteomics of clinical cancer biomarkers.Clinical proteomics · 2024Review
- Mass Spectrometry-Based Approaches for Clinical Biomarker Discovery in Traumatic Brain Injury.Current treatment options in neurology · 2022Article
- An Introduction to Advanced Targeted Acquisition Methods.Molecular & cellular proteomics : MCP · 2021Review
- Article
- The role of proteomics in assessing beta-cell dysfunction and death in type 1 diabetes.Expert review of proteomics · 2019Article
- Clinical potential of mass spectrometry-based proteogenomics.Nature reviews. Clinical oncology · 2019Review
- Surface Enhanced Raman Spectroscopy of Lactoferrin Adsorbed on Silvered Porous Silicon Covered with Graphene.Biosensors · 2019Article
- Existing and novel biomarkers for precision medicine in systemic sclerosis.Nature reviews. Rheumatology · 2018Review
- Facile carrier-assisted targeted mass spectrometric approach for proteomic analysis of low numbers of mammalian cells.Communications biology · 2018Article
- Multiplexed targeted mass spectrometry assays for prostate cancer-associated urinary proteins.Oncotarget · 2017Article
- Revisiting biomarker discovery by plasma proteomics.Molecular systems biology · 2017Review
Corrections and comments
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
Abstract
Mass spectrometry-based targeted proteomics (e.g., selected reaction monitoring, SRM) is emerging as an attractive alternative to immunoassays for protein quantification. Recently we have made significant progress in SRM sensitivity for enabling quantification of low nanograms per milliliter to sub-naograms per milliliter level proteins in nondepleted human blood plasma/serum without affinity enrichment. However, precise quantification of extremely low abundance proteins (e.g., ≤ 100 pg/mL in blood plasma/serum) using targeted proteomics approaches still remains challenging, especially for these samples without available antibodies for enrichment. To address this need, we have developed an antibody-independent deep-dive SRM (DD-SRM) approach that capitalizes on multidimensional high-resolution reversed-phase liquid chromatography (LC) separation for target peptide separation and enrichment combined with precise selection of target peptide fractions of interest, significantly improving SRM sensitivity by ∼5 orders of magnitude when compared to conventional LC-SRM. Application of DD-SRM to human serum and tissue provides precise quantification of endogenous proteins at the ∼10 pg/mL level in nondepleted serum and at <10 copies per cell level in tissue. Thus, DD-SRM holds great promise for precisely measuring extremely low abundance proteins or protein modifications, especially when high-quality antibodies are not available.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.