Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast (Q27931759)

PubMed

16267052

1 December 2016

title

Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast (English)

1 reference

PubMed

Triacylglycerol lipase YKR089C

1 December 2016

0 references

1 reference

Bifunctional triglyceride lipase/lysophosphatidylethanolamine acyltransferase YMR313C

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

1 reference

Heimo Wolinski

4

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Sepp D Kohlwein

object named as

Sepp D Kohlwein

10

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Robert Zimmermann

object named as

Robert Zimmermann

7

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Rudolf Zechner

object named as

Rudolf Zechner

9

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author name string

Christoph F Kurat

1

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Klaus Natter

2

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Julia Petschnigg

3

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Kim Scheuringer

5

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Harald Scholz

6

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Regina Leber

Journal of Biological Chemistry

8

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language of work or name

English

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publication date

6 January 2006

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published in

1 reference

PubMed

16267052

Enzymes of triacylglycerol synthesis and their regulation

1 December 2016

volume

281

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issue

1

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page(s)

491-500

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cites work

1 reference

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The genetics of fatty acid metabolism in Saccharomyces cerevisiae

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Fatty acid metabolism in Saccharomyces cerevisiae

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The lipid droplet enzyme Tgl1p hydrolyzes both steryl esters and triglycerides in the yeast, Saccharomyces cerevisiae

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Mechanisms of lipid-body formation

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The spatial organization of lipid synthesis in the yeast Saccharomyces cerevisiae derived from large scale green fluorescent protein tagging and high resolution microscopy

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Identification of a gene encoding an acyl CoA:diacylglycerol acyltransferase, a key enzyme in triacylglycerol synthesis

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The DGA1 gene determines a second triglyceride synthetic pathway in yeast.

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Storage lipid synthesis is non-essential in yeast.

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Synthesis of triacylglycerols by the acyl-coenzyme A:diacyl-glycerol acyltransferase Dga1p in lipid particles of the yeast Saccharomyces cerevisiae

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Phospholipid:diacylglycerol acyltransferase: an enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants

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A lecithin cholesterol acyltransferase-like gene mediates diacylglycerol esterification in yeast.

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Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase

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Desnutrin, an adipocyte gene encoding a novel patatin domain-containing protein, is induced by fasting and glucocorticoids: ectopic expression of desnutrin increases triglyceride hydrolysis.

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Hormone-sensitive lipase deficiency in mice causes diglyceride accumulation in adipose tissue, muscle, and testis

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Tuber Storage Proteins

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A serine protease triad forms the catalytic centre of a triacylglycerol lipase

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Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism

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The alpha/beta hydrolase fold

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The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad

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The lipase gene family

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Lipolysis: pathway under construction

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Brummer lipase is an evolutionary conserved fat storage regulator in Drosophila

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The Saccharomyces cerevisiae YLL012/YEH1, YLR020/YEH2, and TGL1 genes encode a novel family of membrane-anchored lipases that are required for steryl ester hydrolysis

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YMR313c/TGL3 encodes a novel triacylglycerol lipase located in lipid particles of Saccharomyces cerevisiae

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Nte1p-mediated deacylation of phosphatidylcholine functionally interacts with Sec14p

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Neuropathy target esterase and its yeast homologue degrade phosphatidylcholine to glycerophosphocholine in living cells

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Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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The Acyl-CoA synthetases encoded within FAA1 and FAA4 in Saccharomyces cerevisiae function as components of the fatty acid transport system linking import, activation, and intracellular Utilization.

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YEH2/YLR020c encodes a novel steryl ester hydrolase of the yeast Saccharomyces cerevisiae

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Hydrophobic sequences target and anchor perilipin A to lipid droplets

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21 January 2018

Identifiers

DOI

10.1074/JBC.M508414200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

16267052

1 reference

Consolidated OpenCitations Corpus – April 2017