Proteomic analysis of GPI-anchored membrane proteins

Hye Ryung Jung, Ole Nørregaard Jensen

Publikation: Bidrag til tidsskriftReviewForskning

Resumé

Glycosyl-phosphatidyl-inositol-anchored proteins (GPI-APs) represent a subset of post-translationally modified proteins that are tethered to the outer leaflet of the plasma membrane via a C-terminal GPI anchor. GPI-APs are found in a variety of eukaryote species, from pathogenic microorganisms to humans. GPI-APs confer important cellular functions as receptors, enzymes and scaffolding molecules. Specific enzymes and detergent extraction methods combined with separation technologies and mass spectrometry permit proteomic analysis of GPI-APs from plasma membrane preparations to reveal cell-type specific surface molecules, candidate biomarkers and potential therapeutic targets.
OriginalsprogEngelsk
TidsskriftDrug Discovery Today: Technologies
Vol/bind3
Udgave nummer3
Sider (fra-til)339-346
Antal sider8
ISSN1740-6749
DOI
StatusUdgivet - 2006

Fingeraftryk

Membrane Proteins
Proteins
Cell Membrane
Enzymes

Citer dette

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abstract = "Glycosyl-phosphatidyl-inositol-anchored proteins (GPI-APs) represent a subset of post-translationally modified proteins that are tethered to the outer leaflet of the plasma membrane via a C-terminal GPI anchor. GPI-APs are found in a variety of eukaryote species, from pathogenic microorganisms to humans. GPI-APs confer important cellular functions as receptors, enzymes and scaffolding molecules. Specific enzymes and detergent extraction methods combined with separation technologies and mass spectrometry permit proteomic analysis of GPI-APs from plasma membrane preparations to reveal cell-type specific surface molecules, candidate biomarkers and potential therapeutic targets.",
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Proteomic analysis of GPI-anchored membrane proteins. / Jung, Hye Ryung; Jensen, Ole Nørregaard.

I: Drug Discovery Today: Technologies, Bind 3, Nr. 3, 2006, s. 339-346.

Publikation: Bidrag til tidsskriftReviewForskning

TY - JOUR

T1 - Proteomic analysis of GPI-anchored membrane proteins

AU - Jung, Hye Ryung

AU - Jensen, Ole Nørregaard

PY - 2006

Y1 - 2006

N2 - Glycosyl-phosphatidyl-inositol-anchored proteins (GPI-APs) represent a subset of post-translationally modified proteins that are tethered to the outer leaflet of the plasma membrane via a C-terminal GPI anchor. GPI-APs are found in a variety of eukaryote species, from pathogenic microorganisms to humans. GPI-APs confer important cellular functions as receptors, enzymes and scaffolding molecules. Specific enzymes and detergent extraction methods combined with separation technologies and mass spectrometry permit proteomic analysis of GPI-APs from plasma membrane preparations to reveal cell-type specific surface molecules, candidate biomarkers and potential therapeutic targets.

AB - Glycosyl-phosphatidyl-inositol-anchored proteins (GPI-APs) represent a subset of post-translationally modified proteins that are tethered to the outer leaflet of the plasma membrane via a C-terminal GPI anchor. GPI-APs are found in a variety of eukaryote species, from pathogenic microorganisms to humans. GPI-APs confer important cellular functions as receptors, enzymes and scaffolding molecules. Specific enzymes and detergent extraction methods combined with separation technologies and mass spectrometry permit proteomic analysis of GPI-APs from plasma membrane preparations to reveal cell-type specific surface molecules, candidate biomarkers and potential therapeutic targets.

U2 - 10.1016/j.ddtec.2006.09.011

DO - 10.1016/j.ddtec.2006.09.011

M3 - Review

VL - 3

SP - 339

EP - 346

JO - Drug Discovery Today: Technologies

JF - Drug Discovery Today: Technologies

SN - 1740-6749

IS - 3

ER -