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Membrane Protein Structure and Function Characterization

Overview of attention for book
Cover of 'Membrane Protein Structure and Function Characterization'

Table of Contents

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    Book Overview
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    Chapter 1 Recombinant Overexpression of Mammalian TSPO Isoforms 1 and 2
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    Chapter 2 Functional Assembly of Soluble and Membrane Recombinant Proteins of Mammalian NADPH Oxidase Complex
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    Chapter 3 Direct Extraction and Purification of Recombinant Membrane Proteins from Pichia pastoris Protoplasts
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    Chapter 4 Cell-Free Expression for the Study of Hydrophobic Proteins: The Example of Yeast ATP-Synthase Subunits
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    Chapter 5 Wheat Germ Cell-Free Overexpression for the Production of Membrane Proteins
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    Chapter 6 Methyl-Specific Isotope Labeling Strategies for NMR Studies of Membrane Proteins
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    Chapter 7 Labeling of Membrane Complexes for Electron Microscopy
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    Chapter 8 Expression, Biochemistry, and Stabilization with Camel Antibodies of Membrane Proteins: Case Study of the Mouse 5-HT3 Receptor
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    Chapter 9 Characterization of New Detergents and Detergent Mimetics by Scattering Techniques for Membrane Protein Crystallization
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    Chapter 10 Secondary Structure Determination by Means of ATR-FTIR Spectroscopy
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    Chapter 11 Native Mass Spectrometry for the Characterization of Structure and Interactions of Membrane Proteins
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    Chapter 12 Mass Spectrometry of Mitochondrial Membrane Protein Complexes
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    Chapter 13 Functional Studies on Membrane Proteins by Means of H/D Exchange in Infrared: Structural Changes in Na+ NQR from V. cholerae in the Presence of Lipids
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    Chapter 14 Reconstitution of Membrane Proteins in Liposomes
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    Chapter 15 Ion Channels as Reporters of Membrane Receptor Function: Automated Analysis in Xenopus Oocytes
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    Chapter 16 The CRACAM Robot: Two-Dimensional Crystallization of Membrane Protein
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    Chapter 17 Reconstitution of Membrane Proteins into Nanodiscs for Single-Particle Electron Microscopy
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    Chapter 18 Solid-State NMR of Membrane Protein Reconstituted in Proteoliposomes, the Case of TSPO
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    Chapter 19 Sample Preparation for Membrane Protein Structural Studies by Solid-State NMR
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    Chapter 20 Simulation of Ligand Binding to Membrane Proteins
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    Chapter 21 Molecular Modeling of Transporters: From Low Resolution Cryo-Electron Microscopy Map to Conformational Exploration. The Example of TSPO
Attention for Chapter 8: Expression, Biochemistry, and Stabilization with Camel Antibodies of Membrane Proteins: Case Study of the Mouse 5-HT3 Receptor
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Chapter title
Expression, Biochemistry, and Stabilization with Camel Antibodies of Membrane Proteins: Case Study of the Mouse 5-HT3 Receptor
Chapter number 8
Book title
Membrane Protein Structure and Function Characterization
Published in
Methods in molecular biology, January 2017
DOI 10.1007/978-1-4939-7151-0_8
Pubmed ID
28755368
Book ISBNs
978-1-4939-7149-7, 978-1-4939-7151-0
Authors

Ghérici Hassaïne, Cédric Deluz, Luigino Grasso, Romain Wyss, Ruud Hovius, Henning Stahlberg, Takashi Tomizaki, Aline Desmyter, Christophe Moreau, Lucie Peclinovska, Sonja Minniberger, Lamia Mebarki, Xiao-Dan Li, Horst Vogel, Hugues Nury, Hassaïne, Ghérici, Deluz, Cédric, Grasso, Luigino, Wyss, Romain, Hovius, Ruud, Stahlberg, Henning, Tomizaki, Takashi, Desmyter, Aline, Moreau, Christophe, Peclinovska, Lucie, Minniberger, Sonja, Mebarki, Lamia, Li, Xiao-Dan, Vogel, Horst, Nury, Hugues

Abstract

There is growing interest in the use of mammalian protein expression systems, and in the use of antibody-derived chaperones, for structural studies. Here, we describe protocols ranging from the production of recombinant membrane proteins in stable inducible cell lines to biophysical characterization of purified membrane proteins in complex with llama antibody domains. These protocols were used to solve the structure of the mouse 5-HT3 serotonin receptor but are of broad applicability for crystallization or cryo-electron microscopy projects.

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X Demographics

The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
 Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 13 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 13 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 2 15%
Student > Ph. D. Student 2 15%
Student > Bachelor 1 8%
Lecturer > Senior Lecturer 1 8%
Student > Doctoral Student 1 8%
Other 1 8%
Unknown 5 38%
Readers by discipline Count As %
Agricultural and Biological Sciences 2 15%
Biochemistry, Genetics and Molecular Biology 2 15%
Medicine and Dentistry 2 15%
Veterinary Science and Veterinary Medicine 1 8%
Chemistry 1 8%
Other 0 0%
Unknown 5 38%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 02 August 2018.
All research outputs
#15,474,679
of 22,996,001 outputs
Outputs from Methods in molecular biology
#5,381
of 13,151 outputs
Outputs of similar age
#257,271
of 421,191 outputs
Outputs of similar age from Methods in molecular biology
#468
of 1,074 outputs
Altmetric has tracked 22,996,001 research outputs across all sources so far. This one is in the 22nd percentile – i.e., 22% of other outputs scored the same or lower than it.
So far Altmetric has tracked 13,151 research outputs from this source. They receive a mean Attention Score of 3.4. This one is in the 44th percentile – i.e., 44% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 421,191 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 30th percentile – i.e., 30% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 1,074 others from the same source and published within six weeks on either side of this one. This one is in the 40th percentile – i.e., 40% of its contemporaries scored the same or lower than it.

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