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Perilipins 2 and 3 lack a carboxy-terminal domain present in perilipin 1 involved in sequestering ABHD5 and suppressing basal lipolysis

Lipid droplets (LDs) are a conserved feature of most organisms. Vertebrate adipocytes have evolved to efficiently store and release lipids for the whole organism from a single droplet. Perilipin 1, the most abundant lipid-coat protein in adipocytes, plays a key role in regulating lipolysis. In other... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America Jun 24, 2014, Vol.111(25), p.9163
Main Author: Patel, Satish
Other Authors: Yang, Wei , Kozusko, Kristina , Saudek, Vladimir , Savage, David
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 00278424 ; E-ISSN: 10916490
Link: http://search.proquest.com/docview/1543583404/?pq-origsite=primo
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title: Perilipins 2 and 3 lack a carboxy-terminal domain present in perilipin 1 involved in sequestering ABHD5 and suppressing basal lipolysis
format: Article
creator:
  • Patel, Satish
  • Yang, Wei
  • Kozusko, Kristina
  • Saudek, Vladimir
  • Savage, David
subjects:
  • Proteins
  • Oxidation
  • Metabolism
  • Cells
  • Lipids
  • Fluorescence
ispartof: Proceedings of the National Academy of Sciences of the United States of America, Jun 24, 2014, Vol.111(25), p.9163
description: Lipid droplets (LDs) are a conserved feature of most organisms. Vertebrate adipocytes have evolved to efficiently store and release lipids for the whole organism from a single droplet. Perilipin 1, the most abundant lipid-coat protein in adipocytes, plays a key role in regulating lipolysis. In other...
language: eng
source:
identifier: ISSN: 00278424 ; E-ISSN: 10916490
fulltext: fulltext
issn:
  • 00278424
  • 0027-8424
  • 10916490
  • 1091-6490
url: Link


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titlePerilipins 2 and 3 lack a carboxy-terminal domain present in perilipin 1 involved in sequestering ABHD5 and suppressing basal lipolysis
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identifierISSN: 00278424 ; E-ISSN: 10916490
subjectProteins ; Oxidation ; Metabolism ; Cells ; Lipids ; Fluorescence
descriptionLipid droplets (LDs) are a conserved feature of most organisms. Vertebrate adipocytes have evolved to efficiently store and release lipids for the whole organism from a single droplet. Perilipin 1, the most abundant lipid-coat protein in adipocytes, plays a key role in regulating lipolysis. In other...
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titlePerilipins 2 and 3 lack a carboxy-terminal domain present in perilipin 1 involved in sequestering ABHD5 and suppressing basal lipolysis
authorPatel, Satish ; Yang, Wei ; Kozusko, Kristina ; Saudek, Vladimir ; Savage, David
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abstractLipid droplets (LDs) are a conserved feature of most organisms. Vertebrate adipocytes have evolved to efficiently store and release lipids for the whole organism from a single droplet. Perilipin 1, the most abundant lipid-coat protein in adipocytes, plays a key role in regulating lipolysis. In other...
copWashington
pubNational Academy of Sciences
urlhttp://search.proquest.com/docview/1543583404/
doi10.1073/pnas.1318791111
pages9163-9168
date2014-06-24