Highly multiplexed targeted proteomics using precise control of peptide retention time. - Wikidata - wikimedia - TriplyDB

Highly multiplexed targeted proteomics using precise control of peptide retention time.

Highly multiplexed targeted proteomics using precise control of peptide retention time.

http://www.wikidata.org/entity/Q44994830

about

Parallel Reaction Monitoring: A Targeted Experiment Performed Using High Resolution and High Mass Accuracy Mass Spectrometry Identification of a Set of Conserved Eukaryotic Internal Retention Time Standards for Data-independent Acquisition Mass Spectrometry Large-Scale Targeted Proteomics Using Internal Standard Triggered-Parallel Reaction Monitoring (IS-PRM).Targeted proteomic quantification on quadrupole-orbitrap mass spectrometer.Considerations on selected reaction monitoring experiments: implications for the selectivity and accuracy of measurements.Glycocapture-based proteomics for secretome analysis.Recent advances in targeted proteomics for clinical applications.Advances in high-resolution accurate mass spectrometry application to targeted proteomics.Advances in high-resolution quantitative proteomics: implications for clinical applications.Peptide retention time prediction.Characterization of a human pluripotent stem cell-derived model of neuronal development using multiplexed targeted proteomics.Mass spectrometry-assisted gel-based proteomics in cancer biomarker discovery: approaches and application.Reproducible and consistent quantification of the Saccharomyces cerevisiae proteome by SWATH-mass spectrometry.Quantitative proteomics using the high resolution accurate mass capabilities of the quadrupole-orbitrap mass spectrometer.Proteomic analysis of the cardiac extracellular matrix: clinical research applications.Targeted proteomics strategy applied to biomarker evaluation.

P2860

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P2860

Highly multiplexed targeted proteomics using precise control of peptide retention time.

http://www.wikidata.org/entity/Q44994830

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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2012年學術文章

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2012年學術文章

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name

Highly multiplexed targeted proteomics using precise control of peptide retention time.

@en

Highly multiplexed targeted proteomics using precise control of peptide retention time.

@nl

type

label

Highly multiplexed targeted proteomics using precise control of peptide retention time.

@en

Highly multiplexed targeted proteomics using precise control of peptide retention time.

@nl

prefLabel

Highly multiplexed targeted proteomics using precise control of peptide retention time.

@en

Highly multiplexed targeted proteomics using precise control of peptide retention time.

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Highly multiplexed targeted proteomics using precise control of peptide retention time

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Alan Schoen

http://www.w3.org/2001/XMLSchema#string

Bruno Domon

http://www.w3.org/2001/XMLSchema#string

Jamal Souady

http://www.w3.org/2001/XMLSchema#string

Reiko Kiyonami

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Scott Peterman

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Sebastien Gallien

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P2860

PRIDE: new developments and new datasets

Open source system for analyzing, validating, and storing protein identification data.

An improved model for prediction of retention times of tryptic peptides in ion pair reversed-phase HPLC: its application to protein peptide mapping by off-line HPLC-MALDI MS.

Sequence-specific retention calculator. Algorithm for peptide retention prediction in ion-pair RP-HPLC: application to 300- and 100-A pore size C18 sorbents.

Prediction of peptides observable by mass spectrometry applied at the experimental set level

Statistical learning of peptide retention behavior in chromatographic separations: a new kernel-based approach for computational proteomics.

Expediting the development of targeted SRM assays: using data from shotgun proteomics to automate method development.

Peptide retention standards and hydrophobicity indexes in reversed-phase high-performance liquid chromatography of peptides.

Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics

Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma.

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1122-1133

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10.1002/PMIC.201100533

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8

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