Literature DB >> 16043238

Shedding light on membrane proteins.

Chris S Gandhi1, Ehud Y Isacoff.   

Abstract

Membrane proteins are a cell's first line of communication with the world that exists just beyond the plasma membrane. These proteins afford the cell a peek at its external environment, signal the cell to adjust its internal chemistry in response to its surroundings, and ensure that the cell's metabolic state is faithfully coupled to the outside world. Because of their importance in cellular communication, membrane proteins have been the focus of intense study at the functional and structural levels. Here, we describe optical techniques that can either passively monitor or actively control the structural rearrangements that take place as these proteins peek at the outside world. Our focus is on ion channels, but the techniques described can be applied to a host of other proteins.

Mesh:

Substances:

Year:  2005        PMID: 16043238     DOI: 10.1016/j.tins.2005.07.005

Source DB:  PubMed          Journal:  Trends Neurosci        ISSN: 0166-2236            Impact factor:   13.837


  15 in total

1.  Operation of the voltage sensor of a human voltage- and Ca2+-activated K+ channel.

Authors:  Antonios Pantazis; Vadym Gudzenko; Nicoletta Savalli; Daniel Sigg; Riccardo Olcese
Journal:  Proc Natl Acad Sci U S A       Date:  2010-02-16       Impact factor: 11.205

2.  Ligand- and subunit-specific conformational changes in the ligand-binding domain and the TM2-TM3 linker of {alpha}1 {beta}2 {gamma}2 GABAA receptors.

Authors:  Qian Wang; Stephan A Pless; Joseph W Lynch
Journal:  J Biol Chem       Date:  2010-10-11       Impact factor: 5.157

3.  Function of hyperekplexia-causing α1R271Q/L glycine receptors is restored by shifting the affected residue out of the allosteric signalling pathway.

Authors:  Qiang Shan; Lu Han; Joseph W Lynch
Journal:  Br J Pharmacol       Date:  2012-04       Impact factor: 8.739

4.  Distinct properties of glycine receptor β+/α- interface: unambiguously characterizing heteromeric interface reconstituted in homomeric protein.

Authors:  Qiang Shan; Lu Han; Joseph W Lynch
Journal:  J Biol Chem       Date:  2012-04-25       Impact factor: 5.157

5.  Activation and desensitization induce distinct conformational changes at the extracellular-transmembrane domain interface of the glycine receptor.

Authors:  Qian Wang; Joseph W Lynch
Journal:  J Biol Chem       Date:  2011-09-14       Impact factor: 5.157

Review 6.  Emerging approaches to probing ion channel structure and function.

Authors:  Wei-Guang Li; Tian-Le Xu
Journal:  Neurosci Bull       Date:  2012-08       Impact factor: 5.203

7.  The relative orientation of the TM3 and TM4 domains varies between α1 and α3 glycine receptors.

Authors:  Lu Han; Sahil Talwar; Joseph W Lynch
Journal:  ACS Chem Neurosci       Date:  2012-11-28       Impact factor: 4.418

8.  Molecular dynamics simulations reveal that AEDANS is an inert fluorescent probe for the study of membrane proteins.

Authors:  Werner L Vos; Marieke Schor; Artur Baumgaertner; D Peter Tieleman; Marcus A Hemminga
Journal:  Eur Biophys J       Date:  2009-08-11       Impact factor: 1.733

Review 9.  Monitoring protein interactions and dynamics with solvatochromic fluorophores.

Authors:  Galen S Loving; Matthieu Sainlos; Barbara Imperiali
Journal:  Trends Biotechnol       Date:  2009-12-03       Impact factor: 19.536

10.  Patch-clamp coordinated spectroscopy shows P2X2 receptor permeability dynamics require cytosolic domain rearrangements but not Panx-1 channels.

Authors:  Severine Chaumont; Baljit S Khakh
Journal:  Proc Natl Acad Sci U S A       Date:  2008-08-08       Impact factor: 11.205

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.