Journal ArticleDOI
Affinity selection of histidine-containing peptides using metal chelate methacrylate monolithic disk for targeted LC-MS/MS approach in high-throughput proteomics.
Rajasekar R. Prasanna,Sinash Sidhik,A. S. Kamalanathan,Krishna Bhagavatula,Mookambeswaran A. Vijayalakshmi +4 more
TLDR
Fast flow metal chelate methacrylate monolithic system - CIM (Convective Interaction Media) disk chelated with Cu(II) disk was found to be highly efficient in capturing His-containing peptides with high degree of specificity and selectivity and demonstrated a significant reduction in sample complexity.About:
This article is published in Journal of Chromatography B.The article was published on 2014-04-01. It has received 20 citations till now.read more
Citations
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Journal ArticleDOI
Current trends in affinity-based monoliths in microextraction approaches: A review.
María Vergara-Barberán,Enrique Javier Carrasco-Correa,María Jesús Lerma-García,Ernesto F. Simó-Alfonso,José Manuel Herrero-Martínez +4 more
TL;DR: The research contributions along the past five years concerning to monolithic materials for the development of affinity-based sorbents in the field of microextraction techniques are reviewed.
Journal ArticleDOI
Middle-down approach: a choice to sequence and characterize proteins/proteomes by mass spectrometry
TL;DR: The high-throughput TD approach (TD proteomics) is yet in its infancy, Nevertheless, TD characterization of purified intact proteins has been useful for detecting PTMs and the MD concept might have widespread applications in future for various research areas, such as clinical, biopharmaceuticals and even for general/routine characterization of proteins including therapeutic proteins.
Journal ArticleDOI
Antibody-free workflows for protein quantification by LC–MS/MS
TL;DR: Antibody-free approaches for quantitative LC-MS/MS-based protein bioanalysis are reviewed and critically evaluated, and compared with the more widely used immunoaffinity-based approaches.
Journal ArticleDOI
Enhancing protein discoverability by data independent acquisition assisted by ion mobility mass spectrometry
TL;DR: It is demonstrated in this study that both acquisition modes provide complementary information about the proteome under investigation, except that DIA demonstrated a better sensitivity than DDA.
Journal ArticleDOI
Improvement of the performance of targeted LC-MS assays through enrichment of histidine-containing peptides.
Cédric Mesmin,Bruno Domon +1 more
TL;DR: This method, used in conjunction with recent improvements in the instrument's peak capacity, addresses a bottleneck generally encountered in quantitative proteomics studies by providing the robustness and throughput required for the analysis of large sample series without compromising the number of proteins monitored.
References
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Journal ArticleDOI
Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
TL;DR: An approach for the accurate quantification and concurrent sequence identification of the individual proteins within complex mixtures based on isotope-coded affinity tags and tandem mass spectrometry is described.
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Large-scale analysis of the yeast proteome by multidimensional protein identification technology.
TL;DR: MudPIT was applied to the proteome of the Saccharomyces cerevisiae strain BJ5460 grown to mid-log phase and yielded the largest proteome analysis to date, identifying 131 proteins with three or more predicted transmembrane domains which allowed us to map the soluble domains of many of the integral membrane proteins.
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Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome.
TL;DR: The combination of strong cation exchange (SCX) and reversed-phase (RP) chromatography to achieve two-dimensional separation prior to MS/MS and 1,504 yeast proteins were unambiguously identified in this single analysis.
Journal ArticleDOI
Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level.
Ashley L. McCormack,David Schieltz,Bruce L. Goode,Shirley Yang,Georjana Barnes,and David Drubin,John R. Yates +6 more
TL;DR: Results from standard protein mixtures show that proteins present in simple mixtures can be readily identified with a 30-fold difference in molar quantity, that the identifications are reproducible, and that proteins within the mixture can be identified at low femtomole levels.
Journal ArticleDOI
Protein abundance profiling of the Escherichia coli cytosol
Yasushi Ishihama,Yasushi Ishihama,Thorsten Schmidt,Juri Rappsilber,Juri Rappsilber,Matthias Mann,Matthias Mann,F. Ulrich Hartl,Michael J. Kerner,Dmitrij Frishman +9 more
TL;DR: Abundance measurements for more than 1000 E. coli proteins presented in this work represent the most complete study of protein abundance in a bacterial cell so far and show significant associations between the abundance of a protein and its properties and functions in the cell.