Functional Differentiation of Antiporter-Like Polypeptides in Complex I; a Site-Directed Mutagenesis Study of Residues Conserved in MrpA and NuoL but Not in MrpD, NuoM, and NuoN-Reference-Cited by-同舟云学术

Functional Differentiation of Antiporter-Like Polypeptides in Complex I; a Site-Directed Mutagenesis Study of Residues Conserved in MrpA and NuoL but Not in MrpD, NuoM, and NuoN

Published:2016-07-08 Issue:7 Volume:11 Page:e0158972
ISSN:1932-6203
Container-title:PLOS ONE
language:en
Short-container-title:PLoS ONE

Author:

Sperling Eva,Górecki Kamil,Drakenberg Torbjörn,Hägerhäll Cecilia

Funder

Vetenskapsrådet

Crafoordska Stiftelsen

Publisher

Public Library of Science (PLoS)

Subject

Multidisciplinary

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1. Ion transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations;2022-01-24

2. Structure of the Dietzia Mrp complex reveals molecular mechanism of this giant bacterial sodium proton pump;Proceedings of the National Academy of Sciences;2020-11-23

3. Proton motive function of the terminal antiporter-like subunit in respiratory complex I;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2020-07

4. Towards understanding the mechanisms of proton pumps in Complex-I of the respiratory chain;Biophysics Reports;2019-10-01

5. Phylogenetic analysis of Na+/H+ (NuoL/MrpA) antiporters;ECORFAN Journal Republic of Guatemala;2019-06-30