Literature DB >> 27856345

Drug targeting of heme proteins in Mycobacterium tuberculosis.

Kirsty J McLean1, Andrew W Munro2.   

Abstract

TB, caused by the human pathogen Mycobacterium tuberculosis (Mtb), causes more deaths than any other infectious disease. Iron is crucial for Mtb to infect the host and to sustain infection, with Mtb encoding large numbers of iron-binding proteins. Many of these are hemoproteins with key roles, including defense against oxidative stress, cellular signaling and regulation, host cholesterol metabolism, and respiratory processes. Various heme enzymes in Mtb are validated drug targets and/or products of genes essential for bacterial viability or survival in the host. Here, we review the structure, function, and druggability of key Mtb heme enzymes and strategies used for their inhibition.
Copyright © 2016. Published by Elsevier Ltd.

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Year:  2016        PMID: 27856345     DOI: 10.1016/j.drudis.2016.11.004

Source DB:  PubMed          Journal:  Drug Discov Today        ISSN: 1359-6446            Impact factor:   7.851


  8 in total

1.  Determination of heme in microorganisms using HPLC-MS/MS and cobalt(III) protoporphyrin IX inhibition of heme acquisition in Escherichia coli.

Authors:  Jonas Fyrestam; Conny Östman
Journal:  Anal Bioanal Chem       Date:  2017-10-17       Impact factor: 4.142

Review 2.  The Red Color of Life Transformed - Synthetic Advances and Emerging Applications of Protoporphyrin IX in Chemical Biology.

Authors:  Elisabeth Sitte; Mathias O Senge
Journal:  European J Org Chem       Date:  2020-03-30

3.  Mycobacterium tuberculosis and pemphigus vulgaris.

Authors:  Katarzyna Osipowicz; Cezary Kowalewski; Katarzyna Woźniak
Journal:  Postepy Dermatol Alergol       Date:  2018-07-19       Impact factor: 1.837

4.  High-throughput structures of protein-ligand complexes at room temperature using serial femtosecond crystallography.

Authors:  Tadeo Moreno-Chicano; Ali Ebrahim; Danny Axford; Martin V Appleby; John H Beale; Amanda K Chaplin; Helen M E Duyvesteyn; Reza A Ghiladi; Shigeki Owada; Darren A Sherrell; Richard W Strange; Hiroshi Sugimoto; Kensuke Tono; Jonathan A R Worrall; Robin L Owen; Michael A Hough
Journal:  IUCrJ       Date:  2019-10-10       Impact factor: 4.769

5.  Structure-function characterization of the mono- and diheme forms of MhuD, a noncanonical heme oxygenase from Mycobacterium tuberculosis.

Authors:  Samuel N Snyder; Piotr J Mak
Journal:  J Biol Chem       Date:  2021-12-06       Impact factor: 5.157

Review 6.  Functionalised Cofactor Mimics for Interactome Discovery and Beyond.

Authors:  Isabel V L Wilkinson; Martin Pfanzelt; Stephan A Sieber
Journal:  Angew Chem Int Ed Engl       Date:  2022-05-31       Impact factor: 16.823

7.  Heme oxygenase-1 modulates ferroptosis by fine-tuning levels of intracellular iron and reactive oxygen species of macrophages in response to Bacillus Calmette-Guerin infection.

Authors:  Chenjie Ma; Xiaoling Wu; Xu Zhang; Xiaoming Liu; Guangcun Deng
Journal:  Front Cell Infect Microbiol       Date:  2022-09-23       Impact factor: 6.073

8.  Dissecting the Mycobacterium bovis BCG Response to Macrophage Infection to Help Prioritize Targets for Anti-Tuberculosis Drug and Vaccine Discovery.

Authors:  Jamie Medley; Aaron Goff; Paulo J G Bettencourt; Madelaine Dare; Liam Cole; Daire Cantillon; Simon J Waddell
Journal:  Vaccines (Basel)       Date:  2022-01-13
  8 in total

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