[go: up one dir, main page]
More Web Proxy on the site http://driver.im/

Lu et al., 2005 - Google Patents

A new approach for sequencing human IRS1 phosphotyrosine‐containing peptides using CapLC‐Q‐TOFmicro

Lu et al., 2005

Document ID
2489670264041042072
Author
Lu X
Lu M
Fischman A
Tompkins R
Publication year
Publication venue
Journal of mass spectrometry

External Links

Snippet

Reversible phosphorylation of proteins functions as a biological switching network for activation and inhibition of downstream biological processes. Since phosphorylations of these sites are often transient processes, and hence sub‐stoichiometric, systematic …
Continue reading at analyticalsciencejournals.onlinelibrary.wiley.com (other versions)

Classifications

    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
    • G01N33/6848—Methods of protein analysis involving mass spectrometry
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
    • G01N33/6842—Proteomic analysis of subsets of protein mixtures with reduced complexity, e.g. membrane proteins, phosphoproteins, organelle proteins
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N30/00—Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
    • G01N30/02—Column chromatography
    • G01N30/62—Detectors specially adapted therefor
    • G01N30/72—Mass spectrometers
    • G01N30/7233—Mass spectrometers interfaced to liquid or superfluid chromatograph
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N30/00—Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
    • G01N30/02—Column chromatography
    • G01N30/86—Signal analysis
    • G01N30/8665—Signal analysis for calibrating the measuring apparatus
    • H—ELECTRICITY
    • H01—BASIC ELECTRIC ELEMENTS
    • H01J—ELECTRIC DISCHARGE TUBES OR DISCHARGE LAMPS
    • H01J49/00—Particle spectrometer or separator tubes
    • H01J49/02—Details
    • H01J49/04—Arrangements for introducing or extracting samples to be analysed, e.g. vacuum locks; Arrangements for external adjustment of electron- or ion-optical components
    • H—ELECTRICITY
    • H01—BASIC ELECTRIC ELEMENTS
    • H01J—ELECTRIC DISCHARGE TUBES OR DISCHARGE LAMPS
    • H01J49/00—Particle spectrometer or separator tubes
    • H01J49/02—Details
    • H01J49/10—Ion sources; Ion guns
    • H01J49/16—Ion sources; Ion guns using surface ionisation, e.g. field-, thermionic- or photo-emission
    • H01J49/161—Ion sources; Ion guns using surface ionisation, e.g. field-, thermionic- or photo-emission using photoionisation, e.g. by laser
    • H01J49/164—Laser desorption/ionisation, e.g. matrix-assisted laser desorption/ionisation [MALDI]

Similar Documents

Publication Publication Date Title
Guerrera et al. Application of mass spectrometry in proteomics
Zhang et al. Overview of peptide and protein analysis by mass spectrometry
Hardouin Protein sequence information by matrix‐assisted laser desorption/ionization in‐source decay mass spectrometry
Chen et al. Application of LC/MS to proteomics studies: current status and future prospects
EP3091562B1 (en) Quantitation of insulin by mass spectrometry
Servais et al. Capillary electrophoresis‐mass spectrometry, an attractive tool for drug bioanalysis and biomarker discovery
Peterman et al. A novel approach for identification and characterization of glycoproteins using a hybrid linear ion trap/FT-ICR mass spectrometer
Reid et al. Selective identification and quantitative analysis of methionine containing peptides by charge derivatization and tandem mass spectrometry
CA3000178C (en) Amyloid beta detection by mass spectrometry
EP1495332A2 (en) Quantitation of biological molecules
Choi et al. Single‐step perfusion chromatography with a throughput potential for enhanced peptide detection by matrix‐assisted laser desorption/ionization‐mass spectrometry
Schmidt et al. Enhanced detection and identification of multiply phosphorylated peptides using TiO2 enrichment in combination with MALDI TOF/TOF MS
Zhang et al. Peptide photodissociation with 157 nm light in a commercial tandem time-of-flight mass spectrometer
Salzano et al. Mass spectrometry for protein identification and the study of post translational modifications
Mueller et al. LC-MALDI MS and MS/MS—an efficient tool in proteome analysis
US7371514B2 (en) Serial derivatization of peptides for de novo sequencing using tandem mass spectrometry
US7693665B2 (en) Identification of modified peptides by mass spectrometry
Lu et al. A new approach for sequencing human IRS1 phosphotyrosine‐containing peptides using CapLC‐Q‐TOFmicro
EP1916526A1 (en) Method for diagnostic and therapeutic target discovery by combining isotopic and isobaric labels
US20060014293A1 (en) Lock mass ions for use with derivatized peptides for de novo sequencing using tandem mass spectrometry
Beck et al. Identification of an in vitro insulin receptor substrate-1 phosphorylation site by negative-ion μLC/ES-API-CID-MS hybrid scan technique
US20080138909A1 (en) Mass Spectrometry of Arginine-Containing Peptides
Shen et al. Liquid chromatography-mass spectrometry and tandem mass spectrometry of peptides and proteins
Hjernø et al. MALDI‐MS in protein chemistry and proteomics
Garcia et al. Peptide analysis using LC-MS