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The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity...

The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_3850f431a42a44abbc6c1bb3ca60c1bc

The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain

About this item

Full title

The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain

Publisher

England: eLife Science Publications, Ltd

Journal title

eLife, 2016-01, Vol.5, p.e12095-e12095

Language

English

Formats

Publication information

Publisher

England: eLife Science Publications, Ltd

More information

Scope and Contents

Contents

GPIHBP1 is a glycolipid-anchored membrane protein of capillary endothelial cells that binds lipoprotein lipase (LPL) within the interstitial space and shuttles it to the capillary lumen. The LPL•GPIHBP1 complex is responsible for margination of triglyceride-rich lipoproteins along capillaries and their lipolytic processing. The current work concept...

Alternative Titles

Full title

The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_3850f431a42a44abbc6c1bb3ca60c1bc

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_3850f431a42a44abbc6c1bb3ca60c1bc

Other Identifiers

ISSN

2050-084X

E-ISSN

2050-084X

DOI

10.7554/eLife.12095

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