000 05852cam a2200661Ii 4500
001 ocn861559596
003 OCoLC
005 20141103172213.0
006 m o d
007 cr |n|||||||||
008 131026s2013 vtu o 000 0 eng d
040 _aEBLCP
_beng
_epn
_cEBLCP
_dOCLCQ
_dCUI
_dCUS
_dE7B
_dCDX
_dOCLCQ
_dN$T
_dOPELS
_dCUS
_dOCLCF
_dOCLCQ
020 _a9780124104709
_q(electronic bk.)
020 _a0124104703
_q(electronic bk.)
020 _z9780124081437
020 _z0124081436
029 1 _aAU@
_b000052223954
029 1 _aDEBSZ
_b405358180
035 _a(OCoLC)861559596
050 4 _aQH603.C43
072 7 _aSCI
_x056000
_2bisacsh
082 0 4 _a571.64
_223
049 _aTEFA
245 0 0 _aReceptor-receptor interactions
_h[electronic resource] /
_cedited by P. Michael Conn.
260 _aBurlington :
_bElsevier Science,
_c2013.
300 _a1 online resource (539 pages).
336 _atext
_btxt
_2rdacontent
337 _acomputer
_bc
_2rdamedia
338 _aonline resource
_bcr
_2rdacarrier
490 1 _aMethods in cell biology ;
_vv. 117
505 0 _aFront Cover; Receptor-Receptor Interactions; Copyright; Contents; Contributors; Preface; References; Chapter 1: Spatial Intensity Distribution Analysis (SpIDA) : A New Tool for Receptor Tyrosine Kinase Activation and Transactivation Quantification; Introduction; 1.1. Theory of Spatial Intensity Distribution Analysis; 1.1.1. Theoretical basis of SpIDA; 1.2. SpIDA: Examples of Application to RTK; 1.2.1. Quantification of EGFR-eGFP; 1.2.2. Application to RTK transactivation in a native system: neurons expressing dopamine receptors; 1.3. Procedure for SpIDA; 1.3.1. Material and apparatus.
505 8 _a1.3.1.1. Sample preparation; 1.3.2. Necessary experimental controls : defining the QB for monomeric moiety; 1.3.2.1. Determining the monomeric QB for receptors tagged with fluorescent proteins; 1.3.2.2. Determining the monomeric QB for antibody labeling using detection of a reference monomeric protein; 1.3.2.3. Determining the monomeric QB by using pharmacological agents that block oligomerization and induce monomeric conformation; 1.3.3. Image acquisitions; 1.3.4. Analysis with the SpIDA program graphical user interface; 1.3.4.1. Description of histogram parameters; 1.3.4.2. SpIDA GUI procedures.
505 8 _a1.3.5. Determination of analog detector signal broadening; 1.3.5.1. Analog detector calibration procedure; 1.3.6. Data interpretation and pharmacological analysis; 1.4. Discussion; Acknowledgments; References; Chapter 2: Dimerization of Nuclear Receptors; Introduction; 2.1. Methods; 2.1.1. Studies of NR-NR interactions through protein crystallization; 2.1.1.1. Required materials; 2.1.1.2. Protocol; 2.1.2. Expression and purification of NR-NR complexes; 2.1.2.1. Required materials; 2.1.2.2. Protocol; 2.1.3. Monitoring NR-NR interactions by noncovalent electrospray ionization mass spectrometry.
505 8 _a2.1.3.1. Required materials2.1.3.2. Protocol; 2.1.4. Monitoring NR-NR interactions by electrophoretic mobility shift assays; 2.1.4.1. Required materials; 2.1.4.2. Protocol; 2.1.4.2.1. In vitro transcription-translation; 2.1.4.2.2. Electrophoretic mobility shift assay; 2.1.5. Two-hybrid assays to define NR-NR interactions in living cells; 2.1.5.1. Required materials; 2.1.5.2. Protocol; 2.1.5.2.1. Transient transfection of HeLa cells; 2.1.5.2.2. Cell lysis; 2.1.5.2.3. Preparation of luciferase assay; 2.1.5.2.4. Luciferase measurement; 2.1.5.2.5. Measurement of {Beta]gal activity.
505 8 _a2.1.5.2.6. Normalization; 2.1.6. Fluorescence cross-correlation spectroscopy to measure the concentrations and interactions of NRs in living cells; 2.1.6.1. Required materials; 2.1.6.2. Protocol; 2.1.6.2.1. Cell culture and transfection; 2.1.6.2.2. Fluorescence cross-correlation microscopy; 2.1.6.2.3. Data analysis; Acknowledgments; References; Chapter 3 : Network Analysis to Uncover the Structural Communication in GPCRs; Introduction; 3.1. Materials; 3.2. Methods; 3.2.1. Workflow of the PSN-MD and PSN-ENM approaches; 3.2.2. Building the PSG; 3.2.3. Search for the shortest communication paths.
500 _a3.3. Discussion.
520 _aThis new volume of Methods in Cell Biology looks at receptor-receptor interactions, with sections on allosteric and effector interactions, crystallization and modeling, measuring receptor-receptor interactions and oligomerization in individual classes. With cutting-edge material, this comprehensive collection is intended to guide researchers of receptor-receptor interactions for years to come. Covers sections on allosteric and effector interactions, crystallization and modeling, measuring receptor-receptor interactions and oligomerization in individual class.
588 0 _aPrint version record.
650 0 _aCell receptors.
650 2 _aReceptors, Cell Surface.
650 2 _aSignal Transduction.
650 2 _aStructure-Activity Relationship.
650 7 _aSCIENCE
_xLife Sciences
_xAnatomy & Physiology.
_2bisacsh
650 7 _aCell receptors.
_2fast
_0(OCoLC)fst00850227
655 4 _aElectronic books.
700 1 _aConn, P. Michael,
_eeditor.
776 0 8 _iPrint version:
_aConn, P. Michael.
_tReceptor-Receptor Interactions : Methods in Cell Biology.
_dBurlington : Elsevier Science, �2013
_z9780124081437
830 0 _aMethods in cell biology ;
_vv. 117.
856 4 0 _3ScienceDirect
_uhttp://www.sciencedirect.com
856 4 0 _3ScienceDirect
_uhttp://www.sciencedirect.com/science/bookseries/0091679X/117
856 4 0 _3ScienceDirect
_uhttp://www.sciencedirect.com/science/book/9780124081437
938 _aCoutts Information Services
_bCOUT
_n26537270
938 _aEBL - Ebook Library
_bEBLB
_nEBL1495650
938 _aebrary
_bEBRY
_nebr10787043
938 _aEBSCOhost
_bEBSC
_n655265
942 _cEB
994 _aC0
_bTEF
999 _c21093
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