Examining the role of protein structural dynamics in drug resistance in Mycobacterium tuberculosis-Reference-Cited by-同舟云学术

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Examining the role of protein structural dynamics in drug resistance in Mycobacterium tuberculosis

Published:2017 Issue:12 Volume:8 Page:8384-8399
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Shaw Daniel J.¹²³⁴⁵^ORCID,Hill Rachel E.⁶⁷⁸⁵,Simpson Niall¹²³⁴⁵,Husseini Fouad S.⁶⁷⁸⁵,Robb Kirsty⁹²⁴⁵,Greetham Gregory M.¹⁰¹¹¹²¹³⁵,Towrie Michael¹⁰¹¹¹²¹³⁵,Parker Anthony W.¹⁰¹¹¹²¹³⁵^ORCID,Robinson David¹⁴¹⁵⁸⁵^ORCID,Hirst Jonathan D.⁶⁷⁸⁵^ORCID,Hoskisson Paul A.⁹²⁴⁵^ORCID,Hunt Neil T.¹²³⁴⁵^ORCID

Affiliation:

1. Department of Physics

2. University of Strathclyde

3. SUPA

4. Glasgow

5. UK

6. School of Chemistry

7. University of Nottingham

8. Nottingham

9. Strathclyde Institute of Pharmacy and Biomedical Science

10. STFC Central Laser Facility

11. Research Complex at Harwell

12. Rutherford Appleton Laboratory

13. Didcot

14. Department of Chemistry and Forensics

15. Nottingham Trent University

Abstract

2D-IR spectroscopy reveals a role for protein structural dynamics in antimicrobial-resistance.

Funder

Leverhulme Trust

STFC

EPSRC

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2017/SC/C7SC03336B

Reference51 articles.

1. WHO , Global tuberculosis report 2014 (WHO/HTM/TB/2014.08) , 2014 , WHO/HTM/TB/2014.08

2. A Structural and Energetic Model for the Slow-Onset Inhibition of the Mycobacterium tuberculosis Enoyl-ACP Reductase InhA

3. Probing mechanisms of resistance to the tuberculosis drug isoniazid: Conformational changes caused by inhibition of InhA, the enoyl reductase fromMycobacterium tuberculosis

4. The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: Adduct affinity and drug resistance

5. Modification of the NADH of the Isoniazid Target (InhA) from Mycobacterium tuberculosis

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