Expression, purification, and projection structure by single particle electron microscopy of functional human TRPM4 heterologously expressed in Xenopus laevis oocytes-Reference-Cited by-同舟云学术

Expression, purification, and projection structure by single particle electron microscopy of functional human TRPM4 heterologously expressed in Xenopus laevis oocytes

Published:2014-03 Issue: Volume:95 Page:169-176
ISSN:1046-5928
Container-title:Protein Expression and Purification
language:en
Short-container-title:Protein Expression and Purification

Author:

Clémençon Benjamin,Fine Michael,Lüscher Benjamin,Baumann Marc U.,Surbek Daniel V.,Abriel Hugues,Hediger Matthias A.

Publisher

Elsevier BV

Subject

Biotechnology

Reference26 articles.

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3. Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform;Xu;Proc. Natl. Acad. Sci. USA,2001

4. TRPM4 controls insulin secretion in pancreatic β-cells;Cheng;Cell Calcium,2007

5. Increased IgE-dependent mast cell activation and anaphylactic nonselective cation channel TRPM4;Vennekens;Nat. Immunol.,2007

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2. Electron cryo-microscopy structure of a human TRPM4 channel;Nature;2017-12

3. Heterologously-expressed and Liposome-reconstituted Human Transient Receptor Potential Melastatin 4 Channel (TRPM4) is a Functional Tetramer;Scientific Reports;2016-01-20

4. Purification of Human and Mammalian Membrane Proteins Expressed in Xenopus laevis Frog Oocytes for Structural Studies;Methods in Molecular Biology;2016

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