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05413nam a2200529 4500 |
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ocn861559596 |
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OCoLC |
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20180501122014.0 |
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m o d |
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131026s2013 vtu o 000 0 eng d |
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|a EBLCP
|b eng
|e pn
|c EBLCP
|d OCLCQ
|d CUI
|d CUS
|d E7B
|d CDX
|d OCLCQ
|d N$T
|d OPELS
|d CUS
|d OCLCF
|d OCLCQ
|d DEBSZ
|d NLGGC
|d OCLCQ
|d CASUM
|d MERUC
|d MEU
|d GrThAP
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|a 1029056556
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|a 9780124104709
|q (electronic bk.)
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|a 0124104703
|q (electronic bk.)
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|a 9780124081437
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|a 0124081436
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|a (OCoLC)861559596
|z (OCoLC)1029056556
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|a QH603.C43
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| 072 |
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|a SCI
|x 056000
|2 bisacsh
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|a 571.64
|2 23
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| 049 |
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|a TEFA
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| 245 |
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|a Receptor-receptor interactions /
|c edited by P. Michael Conn.
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| 260 |
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|a Burlington :
|b Elsevier Science,
|c 2013.
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| 300 |
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|a 1 online resource (539 pages).
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| 336 |
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|a text
|b txt
|2 rdacontent
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|a computer
|b c
|2 rdamedia
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|a online resource
|b cr
|2 rdacarrier
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| 490 |
1 |
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|a Methods in cell biology ;
|v v. 117
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|a Front 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.
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|a 1.3.1.1. 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.
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|a 1.3.5. 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.
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|a 2.1.3.1. 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.
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|a 2.1.5.2.6. 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.
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|a 3.3. Discussion.
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|a This 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.
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| 588 |
0 |
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|a Print version record.
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| 546 |
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|a Text in English.
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| 650 |
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|a Cell receptors.
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| 650 |
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7 |
|a SCIENCE
|x Life Sciences
|x Anatomy & Physiology.
|2 bisacsh
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| 650 |
|
7 |
|a Cell receptors.
|2 fast
|0 (OCoLC)fst00850227
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| 650 |
1 |
2 |
|a Receptors, Cell Surface.
|0 (DNLM)D011956
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| 655 |
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4 |
|a Electronic books.
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| 700 |
1 |
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|a Conn, P. Michael,
|e editor.
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| 776 |
0 |
8 |
|i Print version:
|a Conn, P. Michael.
|t Receptor-Receptor Interactions : Methods in Cell Biology.
|d Burlington : Elsevier Science, ©2013
|z 9780124081437
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| 830 |
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0 |
|a Methods in cell biology ;
|v v. 117.
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| 856 |
4 |
0 |
|u https://www.sciencedirect.com/science/bookseries/0091679X/117
|z Full Text via HEAL-Link
|
