Lectin affinity as an approach to the proteomic analysis of membrane glycoproteins.
about
Identification and quantification of glycoproteins using ion-pairing normal-phase liquid chromatography and mass spectrometryInterplay of anionic charge, poly(ethylene glycol), and iodinated tyrosine incorporation within tyrosine-derived polycarbonates: Effects on vascular smooth muscle cell adhesion, proliferation, and motilityUse of quantitative membrane proteomics identifies a novel role of mitochondria in healing injured muscles.Glycoproteomics in neurodegenerative diseases.Simultaneous characterization of glyco- and phosphoproteomes of mouse brain membrane proteome with electrostatic repulsion hydrophilic interaction chromatographyAnalysis of glycoproteins for biomarker discoveryCharacterization of murine brain membrane glycoproteins by detergent assisted lectin affinity chromatography.Equal ratio of graphite carbon to activated charcoal for enrichment of N-glycopeptides prior to matrix-assisted laser desorption/ionization time-of-flight mass spectrometric identification.Challenges in plasma membrane phosphoproteomics.Integrated analysis of global proteome, phosphoproteome, and glycoproteome enables complementary interpretation of disease-related protein networks.Glycoproteomic analysis of the secretome of human endothelial cellsComplementary methods to assist subcellular fractionation in organellar proteomics.Identification of the plasticity-relevant fucose-alpha(1-2)-galactose proteome from the mouse olfactory bulb.Thematic review series: proteomics. Proteomic analysis of lipid-protein complexes.The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation.Solid-phase extraction and purification of membrane proteins using a UV-modified PMMA microfluidic bioaffinity μSPE device.Tools for phospho- and glycoproteomics of plasma membranes.Characterization of membrane-associated glycoproteins using lectin affinity chromatography and mass spectrometry.The antiretroviral lectin cyanovirin-N targets well-known and novel targets on the surface of Entamoeba histolytica trophozoites.Use of colloidal silica-beads for the isolation of cell-surface proteins for mass spectrometry-based proteomicsSurface Glycoproteins of Exosomes Shed by Myeloid-Derived Suppressor Cells Contribute to Function.Excessive activation of the alternative complement pathway in autosomal dominant polycystic kidney disease.An optimized approach for enrichment of glycoproteins from cell culture lysates using native multi-lectin affinity chromatography
P2860
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P2860
Lectin affinity as an approach to the proteomic analysis of membrane glycoproteins.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Lectin affinity as an approach to the proteomic analysis of membrane glycoproteins.
@ast
Lectin affinity as an approach to the proteomic analysis of membrane glycoproteins.
@en
type
label
Lectin affinity as an approach to the proteomic analysis of membrane glycoproteins.
@ast
Lectin affinity as an approach to the proteomic analysis of membrane glycoproteins.
@en
prefLabel
Lectin affinity as an approach to the proteomic analysis of membrane glycoproteins.
@ast
Lectin affinity as an approach to the proteomic analysis of membrane glycoproteins.
@en
P2093
P356
P1476
Lectin affinity as an approach to the proteomic analysis of membrane glycoproteins.
@en
P2093
Dhiman Ghosh
John A Wilkins
Kenneth G Standing
Mihaela Antonovici
Oleg Krokhin
Ronald C Beavis
Werner Ens
P304
P356
10.1021/PR049937F
P577
2004-07-01T00:00:00Z