The DOI matches its Crossref record; 93 of the 93 references it cites were found in a registry or an index.
Take five — Type VII secretion systems of Mycobacteria
Open accessAbstract
Mycobacteria use type VII secretion (T7S) systems to secrete proteins across their complex cell envelope. Pathogenic mycobacteria, such as the notorious pathogen Mycobacterium tuberculosis, have up to five of these secretion systems, named ESX-1 to ESX-5. At least three of these secretion systems are essential for mycobacterial virulence and/or viability. Elucidating T7S is therefore essential to understand the success of M. tuberculosis and other pathogenic mycobacteria as pathogens, and could be instrumental to identify novel targets for drug- and vaccine-development. Recently, significant progress has been achieved in the identification of T7S substrates and a general secretion motif. In addition, a start has been made with unraveling the mechanism of secretion and the structural analysis of the different subunits. This review summarizes these recent findings, which are incorporated in a working model of this complex machinery. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey.
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“ESX-4 is one of the least well-characterized ESX systems, although it is considered the most ancestral esx locus in mycobacteria (21,82).”
From ESX/Type VII Secretion Systems—An Important Way Out for Mycobacterial Proteins (2019) · cites this paper as [82]
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Secretion systems in Gram-negative bacteria: Structural and mechanistic insights
Costa, T. R. D., Felisberto-Rodrigues, C., Meir, A., Prevost, M. S., Redzej, A., Trokter, M., & Waksman, G. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3456 · Cited by 1,132
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Ohno, H. (2015) · The Journal of Biochemistry · doi:10.1093/jb/mvv121 · Cited by 224
Metadata
- Authors
- Houben, E. N. G., Korotkov, K. V., & Bitter, W.
- Affiliations
- Vrije Universiteit Amsterdam (NL)
- University of Kentucky (US)
- Corresponding author
- Houben, Edith N.G.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2014-08
- Volume
- 1843
- Issue
- 8
- Pages
- 1707-1716
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2107983230
- Cited by
- 223
- References
- 93
- Citations by year
- 2026: 6 · 2025: 15 · 2024: 8 · 2023: 5 · 2022: 9 · 2021: 37 · 2020: 19 · 2019: 21 · 2018: 20 · 2017: 22 · 2016: 30 · 2015: 24 · 2014: 7
- FWCI
- 2.64
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Amsterdam UMC (VU Amsterdam) - Institutional Repository (publishedVersion)
- VU Research Portal (publishedVersion, other-oa)
- Pure Amsterdam UMC (submittedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (P20GM103486)
- Netherlands Organization for Scientific Research (NWO)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Epidemiology › Mycobacterium research and diagnosis
- Keywords
- type VII secretion system, ESX secretion system, Mycobacterium tuberculosis, mycobacterial virulence, bacterial protein secretion, secretion mechanism, ESX-1, therapeutic target, vaccine targets
- MeSH terms
- Bacterial Proteins, Cell Wall, Humans, Mycobacterium tuberculosis, Tuberculosis, Protein Structure, Tertiary, Molecular Chaperones, Protein Transport, Bacterial Secretion Systems
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