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Using iRT, a normalized retention time for more targeted measurement of peptides

Using iRT, a normalized retention time for more targeted measurement of peptides

http://www.wikidata.org/entity/Q41938071

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Proteomic tools to decipher microbial community structure and functioning Emerging proteomic technologies for elucidating context-dependent cellular signaling events: A big challenge of tiny proportions Proteomics characterization of exosome cargo An open-source computational and data resource to analyze digital maps of immunopeptidomes Design, implementation and multisite evaluation of a system suitability protocol for the quantitative assessment of instrument performance in liquid chromatography-multiple reaction monitoring-MS (LC-MRM-MS)Automated selected reaction monitoring data analysis workflow for large-scale targeted proteomic studies.Citrullination of myofilament proteins in heart failure.DIANA--algorithmic improvements for analysis of data-independent acquisition MS data.Data-independent MS/MS quantification of neuropeptides for determination of putative feeding-related neurohormones in microdialysate.DIA-Umpire: comprehensive computational framework for data-independent acquisition proteomics Building high-quality assay libraries for targeted analysis of SWATH MS data.Automated Validation of Results and Removal of Fragment Ion Interferences in Targeted Analysis of Data-independent Acquisition Mass Spectrometry (MS) using SWATHProphet Extending the limits of quantitative proteome profiling with data-independent acquisition and application to acetaminophen-treated three-dimensional liver microtissues.Quantification of SAHA-Dependent Changes in Histone Modifications Using Data-Independent Acquisition Mass Spectrometry Identification of a Set of Conserved Eukaryotic Internal Retention Time Standards for Data-independent Acquisition Mass Spectrometry Multiplexed, Scheduled, High-Resolution Parallel Reaction Monitoring on a Full Scan QqTOF Instrument with Integrated Data-Dependent and Targeted Mass Spectrometric Workflows.Advancing Urinary Protein Biomarker Discovery by Data-Independent Acquisition on a Quadrupole-Orbitrap Mass Spectrometer Systematic evaluation of data-independent acquisition for sensitive and reproducible proteomics-a prototype design for a single injection assay.Human Leukocyte Antigen (HLA) B27 Allotype-Specific Binding and Candidate Arthritogenic Peptides Revealed through Heuristic Clustering of Data-independent Acquisition Mass Spectrometry (DIA-MS) Data.High-precision iRT prediction in the targeted analysis of data-independent acquisition and its impact on identification and quantitation.A hybrid retention time alignment algorithm for SWATH-MS data.Effect of peptide assay library size and composition in targeted data-independent acquisition-MS analyses.Generation of accurate peptide retention data for targeted and data independent quantitative LC-MS analysis: Chromatographic lessons in proteomics.Mapping Biological Networks from Quantitative Data-Independent Acquisition Mass Spectrometry: Data to Knowledge Pipelines.Automated SWATH Data Analysis Using Targeted Extraction of Ion Chromatograms.Second generation multiple reaction monitoring assays for enhanced detection of ultra-low abundance Mycobacterium tuberculosis peptides in human serum.Proteomic analysis by iTRAQ-MRM of soybean resistance to Lamprosema Indicate.Glycoproteomic analysis of prostate cancer tissues by SWATH mass spectrometry discovers N-acylethanolamine acid amidase and protein tyrosine kinase 7 as signatures for tumor aggressiveness.CPTAC Assay Portal: a repository of targeted proteomic assays.Panorama: a targeted proteomics knowledge base A RanGTP-independent mechanism allows ribosomal protein nuclear import for ribosome assembly.Reproducible quantification of cancer-associated proteins in body fluids using targeted proteomics.Application of adenosine triphosphate affinity probe and scheduled multiple-reaction monitoring analysis for profiling global kinome in human cells in response to arsenite treatment.A complete mass-spectrometric map of the yeast proteome applied to quantitative trait analysis.N-glycoprotein SRMAtlas: a resource of mass spectrometric assays for N-glycosites enabling consistent and multiplexed protein quantification for clinical applications.The Mtb proteome library: a resource of assays to quantify the complete proteome of Mycobacterium tuberculosis.Checkpoint blockade cancer immunotherapy targets tumour-specific mutant antigens.Quantifying protein interaction dynamics by SWATH mass spectrometry: application to the 14-3-3 system.A repository of assays to quantify 10,000 human proteins by SWATH-MS.Using PeptideAtlas, SRMAtlas, and PASSEL: Comprehensive Resources for Discovery and Targeted Proteomics.

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P2860

Using iRT, a normalized retention time for more targeted measurement of peptides

http://www.wikidata.org/entity/Q41938071

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

Using iRT, a normalized retention time for more targeted measurement of peptides

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type

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Using iRT, a normalized retention time for more targeted measurement of peptides

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prefLabel

Using iRT, a normalized retention time for more targeted measurement of peptides

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Using iRT, a normalized retention time for more targeted measurement of peptides

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Brendan MacLean

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Claudia Escher

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Franz Herzog

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John Chilton

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

Lukas Reiter

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Oliver Rinner

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

Reto Ossola

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P2860

Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor

Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics

Mass spectrometry-based proteomics

Skyline: an open source document editor for creating and analyzing targeted proteomics experiments

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.

Standardization of retention time data for AMT tag proteomics database generation.

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

High-throughput generation of selected reaction-monitoring assays for proteins and proteomes.

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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1111-1121

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10.1002/PMIC.201100463

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8

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12

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Michael J MacCoss

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2012-04-01T00:00:00Z

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224940199

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22577012

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3918884

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