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The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage

The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7229681

The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage

About this item

Full title

The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2020-05, Vol.117 (19), p.10254-10264

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Lipases are enzymes necessary for the proper distribution and utilization of lipids in the human body. Lipoprotein lipase (LPL) is active in capillaries, where it plays a crucial role in preventing dyslipidemia by hydrolyzing triglycerides from packaged lipoproteins. Thirty years ago, the existence of a condensed and inactive LPL oligomer was propo...

Alternative Titles

Full title

The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7229681

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7229681

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1916555117

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