Combined 1H-Detected Solid-State NMR Spectroscopy and Electron Cryotomography to Study Membrane Proteins across Resolutions in Native Environments-Reference-Cited by-同舟云学术

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Combined 1H-Detected Solid-State NMR Spectroscopy and Electron Cryotomography to Study Membrane Proteins across Resolutions in Native Environments

Published:2018-01 Issue:1 Volume:26 Page:161-170.e3
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Baker Lindsay A.,Sinnige Tessa,Schellenberger Pascale,de Keyzer Jeanine,Siebert C. Alistair,Driessen Arnold J.M.,Baldus Marc,Grünewald Kay

Funder

Wellcome Trust

MRC

BBSRC

Human Frontier Science Program

Canadian Institutes of Health Research

NWO

iNEXT

Horizon 2020

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference83 articles.

1. Magic angle spinning NMR investigation of influenza A M2(18-60): support for an allosteric mechanism of inhibition;Andreas;J. Am. Chem. Soc.,2010

2. Nuclear magnetic resonance spectra from a crystal rotated at high speed;Andrew;Nature,1958

3. Proton-detected solid-state NMR spectroscopy at aliphatic sites: application to crystalline systems;Asami;Acc. Chem. Res.,2013

4. A structural model for microtubule minus-end recognition and protection by CAMSAP proteins;Atherton;Nat. Struct. Mol. Biol.,2017

5. Characterization of membrane protein function by solid-state NMR spectroscopy;Baker;Curr. Opin. Struct. Biol.,2014

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