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001			234725
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008			100301s2005 xxu| s |||| 0|eng d
020			_a9781592598953
024	7		_a10.1385/1592598951 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC
245	1	0	_aUbiquitin-Proteasome Protocols _cedited by Cam Patterson, Douglas M. Cyr.
250			_a1st edition 2005
264		1	_aTotowa, NJ _bHumana Press _c2005
300			_a1 recurso en línea (XII, 381 páginas) _b172 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 _v301
505	0		_aBiochemical Methods to Study the Ubiquitin-Proteasome System -- Small-Molecule Inhibitors of Proteasome Activity -- Purification of E1 and E1-Like Enzymes -- Assays for RING Family Ubiquitin Ligases -- Ubiquitin Chain Synthesis -- Purification of Proteasomes, Proteasome Subcomplexes, and Proteasome-Associated Proteins From Budding Yeast -- Recognition and Processing of Misfolded Proteins by PA700, the 19S Regulatory Complex of the 26S Proteasome -- Cell-Free Assay for Ubiquitin-Independent Proteasomal Protein Degradation -- Assays of Proteasome-Dependent Cleavage Products -- Identification of Components of Protein Complexes -- Mass Spectrometric Determination of Protein Ubiquitination -- Reconstitution of Endoplasmic Reticulum-Associated Degradation Using Yeast Membranes and Cytosol -- Reticulocyte Lysate as a Model System to Study Endoplasmic Reticulum Membrane Protein Degradation -- Deubiquitinating Enzyme Purification, Assay Inhibitors, and Characterization -- Cellular Methods to Study Ubiquitin-Proteasome-Dependent Functions -- Measuring Ubiquitin Conjugation in Cells -- Assays for Proteasome Assembly and Maturation -- N-Terminal Ubiquitination -- Quantitating Defective Ribosome Products -- Endoplasmic Reticulum-Associated Protein Quality Control and Degradation -- Endoplasmic Reticulum-Associated Protein Quality Control and Degradation -- Cystic Fibrosis Transmembrane Conductance Regulator as a Model Substrate to Study Endoplasmic Reticulum Protein Quality Control in Mammalian Cells -- Aggresome Formation -- Detection of Sumoylated Proteins -- Proteasome Inhibitors in Cancer Therapy -- Parkinson's Disease.
520			_aThe targeted addition of ubiquitin to proteins is now known to regulate many cellular events, with the enzymes involved in protein ubiquitination linked to a variety of clinical problems, such as cancer, heart disease, and immune dysfunction. In Ubiquitin-Proteasome Protocols, hands-on leaders in the field, many of whom originally developed the methods they describe, detail cutting-edge techniques for studying ubiquitin-dependent protein degradation via the proteasome. The topics covered range broadly from basic biochemistry to cellular assays to discovery techniques using mass spectrometric analysis. These biochemical and cellular methods are necessary to explore the ubiquitin-proteasome system and ubiquitin-proteasome- dependent functions. The protocols follow the successful Methods in Molecular Biology™ series format, each offering step-by-step laboratory instructions, an introduction outlining the principle behind the technique, lists of the necessary equipment and reagents, and tips on troubleshooting and avoiding known pitfalls. State-of-the-art and user-friendly, Ubiquitin-Proteasome Protocols offers novice and experienced bench scientists alike a thorough compendium of readily reproducible techniques that will accelerate discovery, enhance productivity, and permit manipulation of the system for varied research purposes.
700	1		_aPatterson, Cam _eeditor literario _4edt _4http://id.loc.gov/vocabulary/relators/edt
700	1		_aCyr, Douglas M _eeditor literario _4edt _4http://id.loc.gov/vocabulary/relators/edt
776	0	8	_iPrinted edition: _z9781617374531
776	0	8	_iPrinted edition: _z9781588292520
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1385/1592598951 _z(usuarios Universidad Europea de Valencia)
942			_2lcc _cLE
988			_aSpringer_Protocols_2005
999			_c234725 _d234725