The DOI matches its Crossref record; 104 of the 104 references it cites were found in a registry or an index.
Bacterial Type III Secretion Systems: Specialized Nanomachines for Protein Delivery into Target Cells
Open accessAbstract
One of the most exciting developments in the field of bacterial pathogenesis in recent years is the discovery that many pathogens utilize complex nanomachines to deliver bacterially encoded effector proteins into target eukaryotic cells. These effector proteins modulate a variety of cellular functions for the pathogen's benefit. One of these protein-delivery machines is the type III secretion system (T3SS). T3SSs are widespread in nature and are encoded not only by bacteria pathogenic to vertebrates or plants but also by bacteria that are symbiotic to plants or insects. A central component of T3SSs is the needle complex, a supramolecular structure that mediates the passage of the secreted proteins across the bacterial envelope. Working in conjunction with several cytoplasmic components, the needle complex engages specific substrates in sequential order, moves them across the bacterial envelope, and ultimately delivers them into eukaryotic cells. The central role of T3SSs in pathogenesis makes them great targets for novel antimicrobial strategies.
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Cites
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The type III secretion injectisome
Cornelis, G. R. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1526 · Cited by 1,067
Protein delivery into eukaryotic cells by type III secretion machines
Galán, J. E., & Wolf-Watz, H. (2006) · Nature · doi:10.1038/nature05272 · Cited by 1,041
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Self-citationSupramolecular Structure of the Salmonella typhimurium Type III Protein Secretion System
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Self-citationAssembly and Function of Type III Secretory Systems
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Biological Diversity of Prokaryotic Type IV Secretion Systems
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Cited by
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
Xu, Z., Xu, X., Gong, Q., Li, Z., Li, Y., Wang, S., Yang, Y., Ma, W., Liu, L., Zhu, B., et al. (2019) · Molecular Plant · doi:10.1016/j.molp.2019.08.006 · Cited by 339
Casson, C. N., Yu, J., Reyes, V. M., Taschuk, F. O., Yadav, A., Copenhaver, A. M., Nguyen, H. T., Collman, R. G., & Shin, S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1421699112 · Cited by 276
An essential and highly selective protein import pathway encoded by nucleus-forming phage
Morgan, C. J., Enustun, E., Armbruster, E. G., Birkholz, E. A., Prichard, A., Forman, T., Aindow, A., Wannasrichan, W., Peters, S., Inlow, K., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2321190121 · Cited by 25
Assembly and architecture of the type III secretion sorting platform
Soto, J. E., Galán, J. E., & Lara-Tejero, M. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2218010119 · Cited by 22
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Metadata
- Authors
- Galán, J. E., Lara-Tejero, M., Marlovits, T. C., & Wagner, S.
- Venue
- Annual Review of Microbiology
- Publisher
- Annual Reviews
- Published
- 2014-09-08
- Volume
- 68
- Issue
- 1
- Pages
- 415-438
- ISSN
- 0066-4227 (ISSN-L)
- 1545-3251
- OpenAlex
- W2031923764
- Cited by
- 526
- References
- 104
- FWCI
- 5.63
- Type
- journal article
- Language
- en
- Open access
- bronze
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