000			04166nam a22003975i 4500
999			_c393351 _d393351
001			393351
003			ES-MaUEC
005			20240210124246.0
006			a||||fo|||| 00| 0
007			cr nn 008mamaa
008			100301s1999 xxu| fo |||| 0|eng d
020			_a9781592592647
024	7		_a10.1385/1592592643 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC
050		4	_aQP552 .L5 _b1999 EB
245	0	0	_aProtein Lipidation Protocols _cedited by Michael H. Gelb.
250			_a1st edition 1999
264		1	_aTotowa, NJ _bHumana Press _c1999
300			_a1 recurso en línea (X, 240 páginas) _b35 ilustraciones
336			_atexto _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
347			_aarchivo de texto _bPDF
490	0		_aMethods in Molecular Biology _x1940-6029 _v116
505	0		_aIn Vitro Analysis of GPI Biosynthesis in Mammalian Cells -- Selection of Mammalian Cell Mutants in GPI Biosynthesis -- Analysis of the Cell-Surface Distribution of GPI-Anchored Proteins -- Imaging Fluorescence Resonance Energy Transfer as Probe of Membrane Organization and Molecular Associations of GPI-Anchored Proteins -- Purification of Caveolae-Derived Membrane Microdomains Containing Lipid-Anchored Signaling Molecules, Such as GPI-Anchored Proteins, H-Ras, Src-Family Tyrosine Kinases, eNOS, and G-Protein ?-, ?-, and ?-Subunits -- Analysis of Lipids in Caveolae -- Analysis of the Carbohydrate Components of Glycosylphosphatidylinositol Structures Using Fluorescent Labeling -- Analysis of the Lipid Moiety of GPI Anchor in the Yeast Saccharomyces cerevisiae -- Rapid Identification of Cysteine-Linked Isoprenyl Groups by Metabolic Labeling with [3H]Farnesol and [3H]Geranylgeraniol -- Incorporation of Radiolabeled Prenyl Alcohols and Their Analogs into Mammalian Cell Proteins -- Reconstitution of Yeast Farnesyltransferase from Individually Purified Subunits -- Probing the Role of H-Ras Lipidation for Signaling Functions in Xenopus laevis Oocytes -- Fluorescence Measurement of Lipid-Binding Affinity and Interbilayer Transfer of Bimane-Labeled Lipidated Peptides -- Determination of the Kinetics of Intervesicle Transfer and Transbilayer Diffusion of Bimane-Labeled Lipidated Peptides -- Preparation and Assay of Myristoyl-CoA:Protein N-Myristoyltransferase -- Metabolic Labeling of Protein-Derived Lipid Thioesters in Palmitoyl-Protein Thioesterase-Deficient Cells -- Fatty Acid Analysis of Protein-Derived Lipid Thioesters Isolated from Palmitoyl-Protein Thioesterase-Deficient Cells.
520			_aIn Protein Lipidation Protocols, Michael Gelb brings together a collection of readily reproducible techniques for studying protein lipidation, the covalent attachment of lipids to proteins. These cutting-edge methods-many never published before in a "hands-on" format-deal with glycosyl phosphatidylinositol (GPI)-containing compounds, protein fatty acylation, and protein prenylation. Included are novel techniques for determining the chemical structure of GPI-anchors, for radiolabeling the prenyl groups of protein in eukaryotic cells, a tool for developing inhibitors of the protein farnesyltransferase, and for an exciting lysosomal enzyme that cleaves fatty acyl groups from proteins, the first fatty acylase discovered. Protein Lipidation Protocols offers biochemists, cell and molecular biologists, medicinal chemists, and pharmaceutical researchers state-of-the-art tools for understanding the complex biochemistry of protein lipidation, as well as catalyzing the development of many important new biopharmaceuticals, including anticancer drugs.
988			_aSpringer_Protocols_1999
650		7	_2embne _9146390 _aLipoproteínas
776	0	8	_iPrinted edition: _z9781489943309
776	0	8	_iPrinted edition: _z9780896035348
776	0	8	_iPrinted edition: _z9781489943293
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1385/1592592643 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942			_2lcc _cLE
998			_b12/2023 _dz _ean _zSI