000			03527cam a2200553Ia 4500
001			ocn704379416
003			OCoLC
005			20141103172214.0
006			m o d
007			cr |||||||||||
008			110224s2011 caua ob 001 0 eng d
040			_aBTCTA _beng _cBTCTA _dYDXCP _dUMC _dE7B _dOCLCQ _dCDX _dOPELS _dOCLCQ _dCUS _dOCLCO _dCUS _dOPELS _dOCLCF _dVVL _dOCLCO _dKUK
020			_a9780123864710 (electronic bk.)
020			_a0123864712 (electronic bk.)
035			_a(OCoLC)704379416
050		4	_aQP601 _b.M49 v.499
060		4	_aQU 136
082	0	4	_a612.01575 _223
049			_aTEFA
245	0	0	_aBiology of serpins _h[electronic resource] / _cedited by James C. Whisstock and Phillip I. Bird.
250			_a1st ed.
260			_aSan Diego, CA : _bAcademic Press, _c2011.
300			_a1 online resource (l, 405 p.) : _bill.
490	1		_aMethods in enzymology, _x0076-6879 ; _vv. 499
504			_aIncludes bibliographical references and indexes.
505	0		_aAnalysis of Serpin Secretion, Misfolding, and Surveillance in the Endoplasmic Reticulum -- Serpin-Enzyme Receptors: LDL Receptor-Related Protein 1 -- The Role of Autophagy in Alpha-1-Antitrypsin Deficiency -- Serpins and the Complement System -- Use of Mouse Models to Study Plasminogen Activator Inhibitor-1 -- Plasminogen Activator Inhibitor Type 2: Still an Enigmatic Serpin but a Model for Gene Regulation -- The SerpinB1 Knockout Mouse: A Model for Studying Neutrophil Protease Regulation in Homeostasis and Inflammation -- Investigating Maspin in Breast Cancer Progression Using Mouse Models -- Hsp47 as a collagen-specific molecular chaperone -- Assays for the Antiangiogenic and Neurotrophic Serpin Pigment Epithelium-Derived Factor -- The Drosophila Serpins: Multiple Functions in Immunity and Morphogenesis -- Modeling Serpin Conformational Diseases in Drosophila melanogaster -- Using Caenorhabditis elegans to Study Serpinopathies -- Using C. elegans to Identify the Protease Targets of Serpins In Vivo -- Viral Serpin Therapeutics: From Concept to Clinic -- man SCCA Serpins Inhibit Staphylococcal Cysteine Proteases by Forming Classic "Serpin-Like' Covalent Complexes -- Plants and the Study of Serpin Biology
520			_aSerpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases. This volume of Methods in Ezymology is split into 2 parts and comprehensively covers the subject.
650		0	_aSerpins.
650		0	_aProteins.
650		0	_aProtein folding.
650		0	_aProteins _xBiotechnology.
650		7	_aProtein folding. _2fast _0(OCoLC)fst01079687
650		7	_aProteins. _2fast _0(OCoLC)fst01079711
650		7	_aProteins _xBiotechnology. _2fast _0(OCoLC)fst01079721
650		7	_aSerpins. _2fast _0(OCoLC)fst01113358
650		2	_aSerpins.
655		4	_aElectronic books.
700	1		_aWhisstock, James C.
700	1		_aBird, Phillip I.
830		0	_aMethods in enzymology ; _vv. 499. _x0076-6879
856	4	0	_3ScienceDirect _uhttp://www.sciencedirect.com/science/book/9780123864710
856	4	0	_3ScienceDirect _uhttp://www.sciencedirect.com/science/bookseries/00766879/499
938			_aBaker and Taylor _bBTCP _nBK0009618297
938			_aYBP Library Services _bYANK _n3635678
938			_aebrary _bEBRY _nebr10481921
938			_aCoutts Information Services _bCOUT _n18201572
942			_cEB
994			_aC0 _bTEF
999			_c21174 _d21174