About: Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism

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About: Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism Goto Sponge NotDistinct Permalink

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scientific article published on 01 January 1989

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) artículu científicu espublizáu en 1989 (ast) artigo científico (publicado na 1989) (pt) наукова стаття, опублікована в січні 1989 (uk) im Januar 1989 veröffentlichter wissenschaftlicher Artikel (de) artikull shkencor i botuar më 01 janar 1989 (sq) scientific article published on 01 January 1989 (en)
publication date	wds:Q59975365-4E7E3451-60CF-4FE5-9B69-FC1257D466A9
publication date	1989-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59975365-FDE29B09-1D6E-4A43-A457-83C95FA5C89D
language of work or name	English
author name string	wds:Q59975365-0F87F7FF-523C-4E77-B5ED-845D51639B95 wds:Q59975365-1B55A2C7-2E56-476B-8E39-B78D967B8A69 wds:Q59975365-33DCCE85-B367-4DC3-9DC6-49D84E8B6E51 wds:Q59975365-5D0CC8DD-3EB0-43AC-BA12-F19E450AE4B7
author name string	A J Garton D G Campbell D G Hardie S J Yeaman
rdfs:label	Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism (en) Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism (nl) Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism (sq)
skos:prefLabel	Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism (en) Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism (nl) Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism (sq)
name	Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism (en) Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism (nl) Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism (sq)
author	wds:Q59975365-14C97E4D-D359-42CE-AE75-9875AF4A267F wds:Q59975365-B7C143DE-C512-4BE7-904F-D593D41A0475
author	David Carling Roger J. Colbran
title	wds:Q59975365-CC4057CE-EB2A-4826-80FB-7EE2459816B2
title	Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism (en)
page(s)	wds:Q59975365-F395F085-1F80-449C-949A-23574F4EC467
page(s)	249-254
instance of	wds:Q59975365-F57A5EF1-2D91-430C-BDB0-80CBDEDA3628
instance of	scholarly article
main subject	wds:Q59975365-31E3AC02-CC0C-4FC2-B798-B08A8F3B0380
main subject	phosphorylation
PubMed ID	wds:Q59975365-1460A98C-49B4-4653-BAFB-3F005F987258
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2537200
PubMed ID	2537200
published in	wds:Q59975365-0D1BF7C5-CFC6-4A2A-8A69-0EE8BDBE4AFC
published in	FEBS Journal
issue	wds:Q59975365-D27F71F4-3D93-4088-BAB9-E33436064A6A
volume	wds:Q59975365-D5821147-2CFD-4BD4-8927-3C21A791C340
issue	1
volume	179
number of pages	wds:Q59975365-9FE9C967-5452-424C-9783-ECB34B92DF39
number of pages	6 (xsd:decimal)
DOI	wds:Q59975365-6A3979E7-1A2C-4055-89CE-C06900E25D55
DOI	http://dx.doi.org/10.1111/J.1432-1033.1989.TB14548.X
DOI	10.1111/J.1432-1033.1989.TB14548.X
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59975365
is cites work of	Fatty acids stimulate AMP-activated protein kinase and enhance fatty acid oxidation in L6 myotubes AMP-activated protein kinase: maintaining energy homeostasis at the cellular and whole-body levels [2] Regulation of hormone-sensitive lipase activity in adipose tissue Species-specific alternative splicing generates a catalytically inactive form of human hormone-sensitive lipase. Mammalian AMP-activated protein kinase subfamily AMP-activated protein kinase signaling in metabolic regulation Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver The neurodegeneration mutant löchrig interferes with cholesterol homeostasis and Appl processing Lipolysis - a highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores The AMP-activated protein kinase--fuel gauge of the mammalian cell? The regulation of AMP-activated protein kinase by phosphorylation AMP-activated protein kinase is highly expressed in neurons in the developing rat brain and promotes neuronal survival following glucose deprivation Elevated sensitivity to diet-induced obesity and insulin resistance in mice lacking 4E-BP1 and 4E-BP2 Mechanism of hormone-stimulated lipolysis in adipocytes: translocation of hormone-sensitive lipase to the lipid storage droplet Evidence that AMP triggers phosphorylation as well as direct allosteric activation of rat liver AMP-activated protein kinase. A sensitive mechanism to protect the cell against ATP depletion AMP-Activated Protein Kinase in Metabolic Control and Insulin Signaling Mechanism of intracellular calcium ([Ca2+]i) inhibition of lipolysis in human adipocytes Metformin: a therapeutic opportunity in breast cancer Mechanisms underlying the metabolic actions of galegine that contribute to weight loss in mice Dietary restriction and aging in rodents: a current view on its molecular mechanisms Mammalian triacylglycerol metabolism: synthesis, lipolysis, and signaling Antiobesity activity of a sphingosine 1-phosphate analogue FTY720 observed in adipocytes and obese mouse model AMP-activated protein kinase: a target for drugs both ancient and modern Metabolism of lipids in human white adipocyte The activation of p38 MAPK by the beta-adrenergic agonist isoproterenol in rat epididymal fat cells AMP kinase activation with AICAR simultaneously increases fatty acid and glucose oxidation in resting rat soleus muscle Hormone-sensitive lipase serine phosphorylation and glycerol exchange across skeletal muscle in lean and obese subjects: effect of beta-adrenergic stimulation. Definition of optimal substrate recognition motifs of Ca2+-calmodulin-dependent protein kinases IV and II reveals shared and distinctive features Myocardial triacylglycerol metabolism. Biguanides and thiazolidinediones inhibit stimulated lipolysis in human adipocytes through activation of AMP-activated protein kinase PKA phosphorylates and inactivates AMPKalpha to promote efficient lipolysis AMP-activated protein kinase is activated as a consequence of lipolysis in the adipocyte: potential mechanism and physiological relevance Regulation of visceral and subcutaneous adipocyte lipolysis by acute AICAR-induced AMPK activation Adenosine Monophosphate-Activated Protein Kinase (AMPK) as a New Target for Antidiabetic Drugs: A Review on Metabolic, Pharmacological and Chemical Considerations. Adrenaline is a critical mediator of acute exercise-induced AMP-activated protein kinase activation in adipocytes Role of AMPK in skeletal muscle metabolic regulation and adaptation in relation to exercise Apelin decreases lipolysis via G(q), G(i), and AMPK-Dependent Mechanisms Cyclic GMP signaling in cardiomyocytes modulates fatty acid trafficking and prevents triglyceride accumulation Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium Hormone-sensitive lipase is structurally related to acetylcholinesterase, bile salt-stimulated lipase, and several fungal lipases. Building of a three-dimensional model for the catalytic domain of hormone-sensitive lipase Hormone-sensitive lipase--new roles for an old enzyme Domain-structure analysis of recombinant rat hormone-sensitive lipase Evidence of a possible role for Lys-gamma3-MSH in the regulation of adipocyte function The role of triglyceride lipases in cancer associated cachexia.

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