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description
| - artículu científicu espublizáu en 2006 (ast)
- vědecký článek publikovaný v roce 2006 (cs)
- 2006 թուականի Մայիսին հրատարակուած գիտական յօդուած (hyw)
- наукова стаття, опублікована в травні 2006 (uk)
- 2006 թվականի մայիսին հրատարակված գիտական հոդված (hy)
- vedecký článok (publikovaný 2006/05/19) (sk)
- مقالة علمية (نشرت في 19-5-2006) (ar)
- wetenschappelijk artikel (gepubliceerd op 2006/05/19) (nl)
- article publié dans la revue scientifique Journal of Biological Chemistry (fr)
- scientific journal article (en)
- im Mai 2006 veröffentlichter wissenschaftlicher Artikel (de)
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author name string
| - Tomohiro Yamaguchi
- Fumiko Hirose
- Takashi Osumi
- Shuhei Matsushita
- Kiyoto Motojima
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rdfs:label
| - MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor alpha (en)
- MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor alpha (nl)
- MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor alpha (ast)
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skos:prefLabel
| - MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor alpha (en)
- MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor alpha (nl)
- MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor alpha (ast)
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name
| - MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor alpha (en)
- MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor alpha (nl)
- MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor alpha (ast)
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title
| - MLDP, a novel PAT family protein localized to lipid droplets and enriched in the heart, is regulated by peroxisome proliferator-activated receptor alpha (en)
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is cites work
of | - The lipid droplet coat protein perilipin 5 also localizes to muscle mitochondria
- Unique regulation of adipose triglyceride lipase (ATGL) by perilipin 5, a lipid droplet-associated protein
- Peroxisome proliferator-activated receptor alpha target genes.
- Evolutionarily conserved gene family important for fat storage
- Skeletal muscle perilipin 3 and coatomer proteins are increased following exercise and are associated with fat oxidation
- Sprint interval and traditional endurance training increase net intramuscular triglyceride breakdown and expression of perilipin 2 and 5
- Fat-specific protein 27 regulates storage of triacylglycerol
- Perilipin A and the control of triacylglycerol metabolism
- Proteomic insights into an expanded cellular role for cytoplasmic lipid droplets
- Absence of adipose differentiation related protein upregulates hepatic VLDL secretion, relieves hepatosteatosis, and improves whole body insulin resistance in leptin-deficient mice
- Lipolysis - a highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores
- Adoption of PERILIPIN as a unifying nomenclature for the mammalian PAT-family of intracellular lipid storage droplet proteins
- Perilipin family members preferentially sequester to either triacylglycerol-specific or cholesteryl-ester-specific intracellular lipid storage droplets.
- Lipid droplets: a classic organelle with new outfits
- PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores.
- Fatty acids regulate perilipin5 in muscle by activating PPARδ
- Deficiency of a lipid droplet protein, perilipin 5, suppresses myocardial lipid accumulation, thereby preventing type 1 diabetes-induced heart malfunction
- Ectopic lipid storage and insulin resistance: a harmful relationship
- Fatty acid trafficking in starved cells: regulation by lipid droplet lipolysis, autophagy, and mitochondrial fusion dynamics
- Adipophilin/perilipin-2 as a lipid droplet-specific marker for metabolically active cells and diseases associated with metabolic dysregulation
- Skeletal muscle triglycerides, diacylglycerols, and ceramides in insulin resistance: another paradox in endurance-trained athletes?
- Expression of perilipin 5 promotes lipid droplet formation in yeast
- Liver fatty acid binding protein (L-Fabp) modulates murine stellate cell activation and diet-induced nonalcoholic fatty liver disease
- Perilipin 5, a lipid droplet-binding protein, protects heart from oxidative burden by sequestering fatty acid from excessive oxidation
- Perilipin 5, a lipid droplet-associated protein, provides physical and metabolic linkage to mitochondria
- Cardiomyocyte-specific perilipin 5 overexpression leads to myocardial steatosis and modest cardiac dysfunction
- Oxidative tissue: perilipin 5 links storage with the furnace
- Roles of PPARs on regulating myocardial energy and lipid homeostasis
- Myocardial triacylglycerol metabolism.
- Interactions of perilipin-5 (Plin5) with adipose triglyceride lipase
- Functional interactions between Mldp (LSDP5) and Abhd5 in the control of intracellular lipid accumulation
- Higher PLIN5 but not PLIN3 content in isolated skeletal muscle mitochondria following acute in vivo contraction in rat hindlimb
- Retinyl ester homeostasis in the adipose differentiation-related protein-deficient retina
- PLIN5 deletion remodels intracellular lipid composition and causes insulin resistance in muscle.
- The interplay of protein kinase A and perilipin 5 regulates cardiac lipolysis
- Perilipin 5, a lipid droplet protein adapted to mitochondrial energy utilization
- Cardiac-specific overexpression of perilipin 5 provokes severe cardiac steatosis via the formation of a lipolytic barrier
- Conserved Amphipathic Helices Mediate Lipid Droplet Targeting of Perilipins 1-3
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