ArticleJournal of bacteriology2000
The Yersinia pestis YscY protein directly binds YscX, a secreted component of the type III secretion machinery.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 59 citations in OpenAlex.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- The type III secretion chaperone SctY may shield the hydrophobic export gate-binding C-terminus of its substrate SctX.Acta crystallographica. Section D, Structural biology · 2023Article
- Direct interaction of a chaperone-bound type III secretion substrate with the export gate.Nature communications · 2022Article
- Type III secretion by Yersinia pseudotuberculosis is reliant upon an authentic N-terminal YscX secretor domain.Molecular microbiology · 2022Article
- Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells.FEMS microbiology letters · 2018Review
- Heterologous Complementation Studies With the YscX and YscY Protein Families Reveals a Specificity forFrontiers in cellular and infection microbiology · 2018Article
- Type III secretion systems: the bacterial flagellum and the injectisome.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- The Yersinia pestis type III secretion system: expression, assembly and role in the evasion of host defenses.Immunologic research · 2013Review
- The Aeromonas salmonicida subsp. salmonicida exoproteome: determination of the complete repertoire of Type-Three Secretion System effectors and identification of other virulence factors.Proteome science · 2013Article
- Regulation of the Yersinia type III secretion system: traffic control.Frontiers in cellular and infection microbiology · 2013Review
- Phylogenetic analysis of a gene cluster encoding an additional, rhizobial-like type III secretion system that is narrowly distributed among Pseudomonas syringae strains.BMC microbiology · 2012Article
- Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Microbiology and molecular biology reviews : MMBR · 2012Review
- A C-terminal region of Yersinia pestis YscD binds the outer membrane secretin YscC.Journal of bacteriology · 2011Article
- Control of gene expression by type III secretory activity.Current opinion in microbiology · 2008Review
- Regulatory role of PopN and its interacting partners in type III secretion of Pseudomonas aeruginosa.Journal of bacteriology · 2007Article
- Secretion signal recognition by YscN, the Yersinia type III secretion ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Mapping of a YscY binding domain within the LcrH chaperone that is required for regulation of Yersinia type III secretion.Journal of bacteriology · 2005Article
- Expression of a functional secreted YopN-TyeA hybrid protein in Yersinia pestis is the result of a +1 translational frameshift event.Journal of bacteriology · 2004Article
- Yersinia pestis YscG protein is a Syc-like chaperone that directly binds yscE.Infection and immunity · 2000Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Human pathogenic yersiniae organisms export and translocate the Yop virulence proteins and V antigen upon contact with a eukaryotic cell. Yersinia pestis mutants defective for production of YscX or YscY were unable to export the Yops and V antigen. YscX and YscY were both present in the Y. pestis cell pellet fraction; however, YscX was also found in the culture supernatant. YscY showed structural and amino acid sequence similarities to the Syc family of proteins. YscY specifically recognized and bound to a region of YscX that included a predicted coiled-coil region. These data suggest that YscY may function as a chaperone for YscX in Y. pestis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.