About: Domain Identification of Hormone-sensitive Lipase by Circular Dichroism and Fluorescence Spectroscopy, Limited Proteolysis, and Mass Spectrometry

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About: Domain Identification of Hormone-sensitive Lipase by Circular Dichroism and Fluorescence Spectroscopy, Limited Proteolysis, and Mass Spectrometry Goto Sponge NotDistinct Permalink

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scientific article published in Journal of Biological Chemistry

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в травні 1999 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Mai 1999 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q57904257-3E8C5EA9-783A-4763-AF9E-28A4E15C9905
publication date	1999-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57904257-DD43DC4D-5484-4A2B-A3C3-A28D701DDAAB
language of work or name	English
cites work	wds:Q57904257-0B054080-EC8D-4F4C-8382-5F7725370954 wds:Q57904257-1BA64146-98C7-4BF9-B5E7-441F5F29888A wds:Q57904257-2D07A2D0-56B3-4C9E-B15A-6B067350B4D8 wds:Q57904257-4B12C4F0-F9A3-481B-892E-3D0EC809C981 wds:Q57904257-4B54F2EF-AC0D-4B23-8BAD-EA34027078AA wds:Q57904257-5ADDA045-DAF7-4093-8500-A4537C3989D4 wds:Q57904257-715E1906-BCF8-40EE-87BB-1C688D0B2E7F wds:Q57904257-AE3196F8-17D6-4738-9269-7AB0E3C967A0 wds:Q57904257-B7F817AC-8A95-4FE9-94E6-61E7B87B0432 wds:Q57904257-B8BFA5B8-E527-488B-94D6-8B9CE102B6C2 wds:Q57904257-D0F9ED9E-D2EA-4711-B0D3-26DCCFE0ECBB wds:Q57904257-DCC27811-B7DD-4F1A-A7DD-293698161940 wds:Q57904257-F27ABFD4-CD2A-4D83-B328-18D736EB8D12 wds:Q57904257-F38EC498-E4D4-467F-8938-31788E53FBBB wds:Q57904257-F6A304CE-DA37-4D04-813B-BB0B1D44A0E4
cites work	Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Structure, localization, and regulation of cGMP-inhibited phosphodiesterase (PDE3) [2] Regulation of hormone-sensitive lipase activity in adipose tissue Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants A simple method for displaying the hydropathic character of a protein Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism Identification of novel phosphorylation sites in hormone-sensitive lipase that are phosphorylated in response to isoproterenol and govern activation properties in vitro Inhibition of lipolysis and lipogenesis in isolated rat adipocytes with AICAR, a cell-permeable activator of AMP-activated protein kinase 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 Domain-structure analysis of recombinant rat hormone-sensitive lipase Large-scale purification and kinetic properties of recombinant hormone-sensitive lipase from baculovirus-insect cell systems Identification of the active site serine of hormone-sensitive lipase by site-directed mutagenesis Identification of essential aspartic acid and histidine residues of hormone-sensitive lipase: apparent residues of the catalytic triad Evidence for a multi-domain structure for hormone-sensitive lipase Incorporation of hormone-sensitive lipase into phosphatidylcholine vesicles
author name string	wds:Q57904257-2A12C71B-7E0B-415A-BC28-E56CE2229196 wds:Q57904257-2EB190B4-CDCF-4D3A-8E2D-9510B4D1CE1D wds:Q57904257-50E3C7F5-9BF6-42F5-8B95-A612BC027CB7 wds:Q57904257-6890A936-1639-4319-B3B2-49CCE1FD0D0D wds:Q57904257-9FBDE5DA-C7FC-469B-88CC-B7804BF61247 wds:Q57904257-D7FD3E59-81F2-4081-8BEA-B4492A50C875 wds:Q57904257-E7996258-2177-4D7D-92E8-32453D803E77 wds:Q57904257-FDBF6C1E-3EEC-4C0E-8486-7A0F3270DDC9 wds:Q57904257-FF7FCD35-992E-45B7-AC68-64BFEE24827B
author name string	Z S Derewenda C Holm J Shabanowitz D F Hunt M C Schotz D J Beussman P H Poon T Osterlund K Julenius
rdfs:label	Domain Identification of Hormone-sensitive Lipase by Circular Dichroism and Fluorescence Spectroscopy, Limited Proteolysis, and Mass Spectrometry (en) Domain Identification of Hormone-sensitive Lipase by Circular Dichroism and Fluorescence Spectroscopy, Limited Proteolysis, and Mass Spectrometry (nl)
skos:prefLabel	Domain Identification of Hormone-sensitive Lipase by Circular Dichroism and Fluorescence Spectroscopy, Limited Proteolysis, and Mass Spectrometry (en) Domain Identification of Hormone-sensitive Lipase by Circular Dichroism and Fluorescence Spectroscopy, Limited Proteolysis, and Mass Spectrometry (nl)
name	Domain Identification of Hormone-sensitive Lipase by Circular Dichroism and Fluorescence Spectroscopy, Limited Proteolysis, and Mass Spectrometry (en) Domain Identification of Hormone-sensitive Lipase by Circular Dichroism and Fluorescence Spectroscopy, Limited Proteolysis, and Mass Spectrometry (nl)
author	wds:Q57904257-F5472824-C5F0-456E-A5F0-189DAD1677DC
author	Sara Snogerup Linse
title	wds:Q57904257-860C4058-D9E1-4980-9393-2E481CAE985A
title	Domain identification of hormone-sensitive lipase by circular dichroism and fluorescence spectroscopy, limited proteolysis, and mass spectrometry (en)
page(s)	wds:Q57904257-107DA815-0AFB-4228-83B9-CCDC5B27F360
page(s)	15382-15388
instance of	wds:Q57904257-655B08B0-00BD-48FE-80B8-0E11B8715B8E
instance of	scholarly article
main subject	wds:Q57904257-332E44C5-5D84-4761-8A4E-AEDFCD66E10D wds:Q57904257-DB1AAF82-7562-4B2D-B214-E9EB34929884
main subject	proteolysis fluorescence spectroscopy
PubMed ID	wds:Q57904257-A92FF3F7-B91C-4AFA-A2B4-1A10B2E35C4E
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10336425
PubMed ID	10336425
published in	wds:Q57904257-7603DE18-0A5D-4A07-B525-97E45A825C5E
published in	Journal of Biological Chemistry
issue	wds:Q57904257-5322A85E-65F3-4898-BEAF-FDB39BF4DB3D
volume	wds:Q57904257-BF283B4D-2290-424A-BCFA-387CE76338EF
issue	22
volume	274
DOI	wds:Q57904257-6A0FD8B3-54F7-4186-B097-379034BEFBB0
DOI	http://dx.doi.org/10.1074/JBC.274.22.15382
DOI	10.1074/JBC.274.22.15382
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57904257
is cites work of	Structure-function relationships of hormone-sensitive lipase Stimulation of lipolysis and hormone-sensitive lipase via the extracellular signal-regulated kinase pathway Time-Resolved Fluorescence Allows Selective Monitoring of Trp30 Environmental Changes in the Seven-Trp-Containing Human Pancreatic Lipase Interaction of hormone-sensitive lipase with steroidogenic acute regulatory protein: facilitation of cholesterol transfer in adrenal DAG tales: the multiple faces of diacylglycerol--stereochemistry, metabolism, and signaling Hormone-sensitive lipase--new roles for an old enzyme Selective mobilization of fatty acids from adipose tissue triacylglycerols Chemical modulation of glycerolipid signaling and metabolic pathways Ser649 and Ser650 are the major determinants of protein kinase A-mediated activation of human hormone-sensitive lipase against lipid substrates Characterization of the bovine gene LIPE and possible influence on fatty acid composition of meat.

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