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DOI . ORG {}

  1. Analyzed Page
  2. Matching Content Categories
  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Doi.org Make Money
  6. Keywords
  7. Topics
  8. Schema
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We began analyzing https://www.nature.com/articles/ncb3166, but it redirected us to https://www.nature.com/articles/ncb3166. The analysis below is for the second page.

Title[redir]:
Degradation of lipid droplet-associated proteins by chaperone-mediated autophagy facilitates lipolysis | Nature Cell Biology
Description:
Chaperone-mediated autophagy (CMA) selectively degrades a subset of cytosolic proteins in lysosomes. A potent physiological activator of CMA is nutrient deprivation, a condition in which intracellular triglyceride stores or lipid droplets (LDs) also undergo hydrolysis (lipolysis) to generate free fatty acids for energetic purposes. Here we report that the LD-associated proteins perilipin 2 (PLIN2) and perilipin 3 (PLIN3) are CMA substrates and their degradation through CMA precedes lipolysis. In vivo studies revealed that CMA degradation of PLIN2 and PLIN3 was enhanced during starvation, concurrent with elevated levels of cytosolic adipose triglyceride lipase (ATGL) and macroautophagy proteins on LDs. CMA blockage both in cultured cells and mouse liver or expression of CMA-resistant PLINs leads to reduced association of ATGL and macrolipophagy-related proteins with LDs and the subsequent decrease in lipid oxidation and accumulation of LDs. We propose a role for CMA in LD biology and in the maintenance of lipid homeostasis. Cuervo and colleagues find that perilipin proteins associated with lipid droplets are degraded by chaperone-mediated autophagy to facilitate recruitment of the lipolytic machinery to lipid droplets.

Matching Content Categories {📚}

  • Science
  • Education
  • Telecommunications

Content Management System {📝}

What CMS is doi.org built with?

Custom-built

No common CMS systems were detected on Doi.org, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of doi.org audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 5,000,420 visitors per month in the current month.

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How Does Doi.org Make Money? {💸}

We find it hard to spot revenue streams.

Not all websites are made for profit; some exist to inform or educate users. Or any other reason why people make websites. And this might be the case. Doi.org could be getting rich in stealth mode, or the way it's monetizing isn't detectable.

Keywords {🔍}

pubmed, cells, article, google, scholar, cas, lipid, autophagy, supplementary, ctr, plin, experiments, shown, biol, central, cell, treated, independent, cuervo, proteins, chaperonemediated, protein, nature, condition, degradation, graph, experiment, cma, droplets, lysosomal, data, chem, plingfp, kaushik, access, colocalization, percentage, bodipy, bottom, perilipin, liver, fig, immunoblot, blots, higher, magnification, content, lipolysis, cytosolic, atgl,

Topics {✒️}

nature portfolio permissions reprints privacy policy advertising nature 458 nature author information authors deficient chaperone-mediated autophagy ana maria cuervo average fluorescence intensity/cell chaperone-mediated autophagy depends monitor chaperone-mediated autophagy microtubule-dependent complex formation wdr45-deficient cells caused adipose differentiation-related protein low glucose media gtp-mediated protein translocation high-content imaging serum-deprived media chaperone-mediated autophagic degradation author correspondence chaperone-mediated autophagy lipid-droplet proteome reveals springerlink instant access average ld number/cell permissions oligonol-induced degradation social media lipid droplet-localized proteins article kaushik cma-resistant plins leads lc3-positive limiting membranes1 receptor-mediated endocytosis privacy molecular biology average number/cell competing financial interests adipose triglyceride lipase percentage colocalization plin2-gfp molecular weight markers cma precedes lipolysis expressing mtkeima untreated based reporter protein sirt1-mediated lipophagy mt plin2-gfp treated age-related decline live-cell imaging liver triacylglycerol lipases l2ako liver sections neutral lipid stores

Schema {🗺️}

WebPage:
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         headline:Degradation of lipid droplet-associated proteins by chaperone-mediated autophagy facilitates lipolysis
         description:Chaperone-mediated autophagy (CMA) selectively degrades a subset of cytosolic proteins in lysosomes. A potent physiological activator of CMA is nutrient deprivation, a condition in which intracellular triglyceride stores or lipid droplets (LDs) also undergo hydrolysis (lipolysis) to generate free fatty acids for energetic purposes. Here we report that the LD-associated proteins perilipin 2 (PLIN2) and perilipin 3 (PLIN3) are CMA substrates and their degradation through CMA precedes lipolysis. In vivo studies revealed that CMA degradation of PLIN2 and PLIN3 was enhanced during starvation, concurrent with elevated levels of cytosolic adipose triglyceride lipase (ATGL) and macroautophagy proteins on LDs. CMA blockage both in cultured cells and mouse liver or expression of CMA-resistant PLINs leads to reduced association of ATGL and macrolipophagy-related proteins with LDs and the subsequent decrease in lipid oxidation and accumulation of LDs. We propose a role for CMA in LD biology and in the maintenance of lipid homeostasis. Cuervo and colleagues find that perilipin proteins associated with lipid droplets are degraded by chaperone-mediated autophagy to facilitate recruitment of the lipolytic machinery to lipid droplets.
         datePublished:2015-05-11T00:00:00Z
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         pageStart:759
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      headline:Degradation of lipid droplet-associated proteins by chaperone-mediated autophagy facilitates lipolysis
      description:Chaperone-mediated autophagy (CMA) selectively degrades a subset of cytosolic proteins in lysosomes. A potent physiological activator of CMA is nutrient deprivation, a condition in which intracellular triglyceride stores or lipid droplets (LDs) also undergo hydrolysis (lipolysis) to generate free fatty acids for energetic purposes. Here we report that the LD-associated proteins perilipin 2 (PLIN2) and perilipin 3 (PLIN3) are CMA substrates and their degradation through CMA precedes lipolysis. In vivo studies revealed that CMA degradation of PLIN2 and PLIN3 was enhanced during starvation, concurrent with elevated levels of cytosolic adipose triglyceride lipase (ATGL) and macroautophagy proteins on LDs. CMA blockage both in cultured cells and mouse liver or expression of CMA-resistant PLINs leads to reduced association of ATGL and macrolipophagy-related proteins with LDs and the subsequent decrease in lipid oxidation and accumulation of LDs. We propose a role for CMA in LD biology and in the maintenance of lipid homeostasis. Cuervo and colleagues find that perilipin proteins associated with lipid droplets are degraded by chaperone-mediated autophagy to facilitate recruitment of the lipolytic machinery to lipid droplets.
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      pageStart:759
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         Stem Cells
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Social Networks {👍}(1)

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Mail Servers:

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CDN Services {📦}

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