Structure of the mycobacterial ATP synthase Fo rotor ring in complex with the anti-TB drug bedaquiline (Q27342142)

26 June 2017

title

Structure of the mycobacterial ATP synthase Fo rotor ring in complex with the anti-TB drug bedaquiline (English)

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26 June 2017

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3

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26 June 2017

Julian D Langer

2

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26 June 2017

Luise Eckhardt-Strelau

4

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26 June 2017

Jérôme E G Guillemont

5

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26 June 2017

Anil Koul

6

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26 June 2017

Thomas Meier

7

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26 June 2017

Laura Preiss

1

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26 June 2017

language of work or name

English

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publication date

8 May 2015

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26 June 2017

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26 June 2017

volume

1

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26 June 2017

issue

4

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26 June 2017

page(s)

e1500106

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The c-ring ion binding site of the ATP synthase fromBacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle

26 June 2017

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21 March 2017

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21 March 2017

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7 April 2017

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High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na⁺-coupled ATP synthase

7 April 2017

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Multidrug-resistant tuberculosis and culture conversion with bedaquiline.

29 September 2017

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Delayed bactericidal response of Mycobacterium tuberculosis to bedaquiline involves remodelling of bacterial metabolism.

29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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Selectivity of TMC207 towards mycobacterial ATP synthase compared with that towards the eukaryotic homologue

29 September 2017

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29 September 2017

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29 September 2017

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In vitro antimycobacterial spectrum of a diarylquinoline ATP synthase inhibitor

29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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New mutations in the mycobacterial ATP synthase: new insights into the binding of the diarylquinoline TMC207 to the ATP synthase C-ring structure

29 September 2017

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2 June 2018

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2 June 2018

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2 June 2018

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2 June 2018

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19 June 2018

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27 November 2018

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Essential arginine residue of the F(o)-a subunit in F(o)F(1)-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the F(o) proton channel

27 November 2018

1 reference

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Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus

27 November 2018

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27 November 2018

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27 November 2018

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On the interaction of aliphatic amines and ammonium ions with carboxylic acids in solution and in receptor pockets

27 November 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/26601184

12 December 2020

inferred from PubMed ID database lookup

Kinetics of inactivation of the F1Fo ATPase of Propionigenium modestum by dicyclohexylcarbodiimide in relationship to H+ and Na+ concentration: probing the binding site for the coupling ions

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/26601184

12 December 2020

inferred from PubMed ID database lookup

Infectious disease: TB's revenge

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PubMed

https://pubmed.ncbi.nlm.nih.gov/26601184

12 December 2020

inferred from PubMed ID database lookup

Identifiers

DOI

10.1126/SCIADV.1500106

1 reference

release_ps5lqs7f5bavfcnckzjjn6l4ti

26 June 2017

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/ps5lqs7f5bavfcnckzjjn6l4ti

24 November 2022

mapped directly with Wikidata item

OpenCitations bibliographic resource ID

3573004

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3573004

1 reference