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References from The serine-rich C-terminal tail of the Listeria monocytogenes secretion chaperone PrsA2 is critical for bacterial virulence and resistance to cell-wall active antibiotics. Local targets link to admitted publications; unresolved targets remain external evidence.
Comparative proteome analysis of secretory proteins from pathogenic and nonpathogenic Listeria species
10.1002/pmic.200401024 · 2005 · External reference
Insight into the core and variant exoproteomes of Listeria monocytogenes species by comparative subproteomic analysis
10.1002/pmic.200800765 · 2009 · External reference
Post-translocational folding of secretory proteins in Gram-positive bacteria
2004 · External reference
Listeria monocytogenes virulence factor secretion: don’t leave the cell without a chaperone
10.3389/fcimb.2014.00013 · 2014 · External reference
Listeria monocytogenes PrsA2 is required for virulence factor secretion and bacterial viability within the host cell cytosol
10.1128/iai.00532-10 · 2010 · External reference
Protein transport across the cell wall of monoderm Gram-positive bacteria
10.1111/j.1365-2958.2012.08040.x · 2012 · External reference
Posttranslocation chaperone PrsA2 regulates the maturation and secretion of Listeria monocytogenes proprotein virulence factors
10.1128/jb.05307-11 · 2011 · External reference
Molecular chaperones and photoreceptor function
10.1016/j.preteyeres.2008.03.001 · 2008 · External reference
Molecular chaperones and protein quality control
10.1016/j.cell.2006.04.014 · 2006 · External reference
Chaperone-mediated protein folding
10.1152/physrev.1999.79.2.425 · 1999 · External reference
Listeria monocytogenes - from saprophyte to intracellular pathogen
10.1038/nrmicro2171 · 2009 · External reference
Human listeriosis
10.1128/cmr.00060-19 · 2023 · External reference
Listeriosis in pregnancy
10.1016/j.jmwh.2008.01.005 · 2008 · External reference
Listeria monocytogenes: epidemiology, human disease, and mechanisms of brain invasion
10.1111/j.1574-695x.2008.00404.x · 2008 · External reference
Dose-response model for Listeria monocytogenes-induced stillbirths in nonhuman primates
10.1128/iai.01366-06 · 2008 · External reference
The epidemiology of human listeriosis
10.1016/j.micinf.2007.05.011 · 2007 · External reference
Maternal-neonatal listeriosis
10.1080/21505594.2020.1759287 · 2020 · External reference
Current Trends in Foodborne Human Listeriosis
10.14252/foodsafetyfscj.2017020 · 2018 · External reference
Listeria monocytogenes - how this pathogen survives in food-production environments?
10.3389/fmicb.2022.866462 · 2022 · External reference
A review of Listeria monocytogenes: An update on outbreaks, virulence, dose-response, ecology, and risk assessments
10.1016/j.foodcont.2016.12.016 · 2017 · External reference
Regulation of Listeria monocytogenes virulence
10.1128/microbiolspec.gpp3-0064-2019 · 2019 · External reference
Activation of the Listeria monocytogenes virulence program by a reducing environment
10.1128/mbio.01595-17 · 2017 · External reference
The two distinct phospholipases C of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread
10.1128/iai.63.11.4231-4237.1995 · 1995 · External reference
The broad-range phospholipase C and a metalloprotease mediate listeriolysin O-independent escape of Listeria monocytogenes from a primary vacuole in human epithelial cells
10.1128/iai.63.11.4531-4534.1995 · 1995 · External reference
Proteolytic pathways of activation and degradation of a bacterial phospholipase C during intracellular infection by Listeria monocytogenes
10.1083/jcb.137.6.1381 · 1997 · External reference
Role of hemolysin for the intracellular growth of Listeria monocytogenes
10.1084/jem.167.4.1459 · 1988 · External reference
Listeriolysin O: a phagosome-specific lysin
10.1016/j.micinf.2007.05.005 · 2007 · External reference
Functional analysis of the Listeria monocytogenes secretion chaperone PrsA2 and its multiple contributions to bacterial virulence
10.1111/j.1365-2958.2011.07665.x · 2011 · External reference
Identification of Conserved and Species-Specific Functions of the Listeria monocytogenes PrsA2 Secretion Chaperone
10.1128/iai.00504-15 · 2015 · External reference
The posttranslocation chaperone PrsA2 contributes to multiple facets of Listeria monocytogenes pathogenesis
10.1128/iai.00280-09 · 2009 · External reference
The chaperone PrsA2 regulates the secretion, stability, and folding of listeriolysin O during Listeria monocytogenes infection
10.1128/mbio.00743-24 · 2024 · External reference
A structural comparison of Listeria monocytogenes protein chaperones PrsA1 and PrsA2 reveals molecular features required for virulence
10.1111/mmi.13367 · 2016 · External reference
Structural analysis of extracellular ATP-independent chaperones of streptococcal species and protein substrate interactions
2025 · External reference
flDPnn: Accurate intrinsic disorder prediction with putative propensities of disorder functions
10.1038/s41467-021-24773-7 · 2021 · External reference
Intrinsically Disordered Proteins: An Overview
10.3390/ijms232214050 · 2022 · External reference
The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease
10.1042/bst20160172 · 2016 · External reference
From sequence and forces to structure, function, and evolution of intrinsically disordered proteins
10.1016/j.str.2013.08.001 · 2013 · External reference
Diverse functional manifestations of intrinsic structural disorder in molecular chaperones
10.1042/bst20120108 · 2012 · External reference
Inactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes
10.1128/jb.00976-06 · 2007 · External reference
Structural analysis of extracellular ATP-independent chaperones of streptococcal species and protein substrate interactions
10.1128/msphere.01078-24 · 2025 · External reference
IUPred3: prediction of protein disorder enhanced with unambiguous experimental annotation and visualization of evolutionary conservation
10.1093/nar/gkab408 · 2021 · External reference
Listeria monocytogenes two component system PieRS regulates secretion chaperones PrsA1 and PrsA2 and enhances bacterial translocation across the intestine
10.1111/mmi.14967 · 2022 · External reference
Molecular basis of listeriolysin O pH dependence
10.1073/pnas.0500558102 · 2005 · External reference
3D interaction homology: The hydropathic interaction environments of even alanine are diverse and provide novel structural insight
10.1016/j.jsb.2019.05.007 · 2019 · External reference
Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis/trans isomerase (PPlase) activity
10.1111/j.1365-2958.1992.tb00858.x · 1992 · External reference
Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis
10.1074/jbc.m400861200 · 2004 · External reference
Temperature-dependent expression of flagella of Listeria monocytogenes studied by electron microscopy, SDS-PAGE and western blotting
1988 · External reference
Resistance to bacitracin in Bacillus subtilis: unexpected requirement of the BceAB ABC transporter in the control of expression of its own structural genes
10.1128/jb.01132-07 · 2007 · External reference
The structure and mode of action of glycopeptide antibiotics of the vancomycin group
10.1146/annurev.mi.38.100184.002011 · 1984 · External reference
Streptococcus pneumoniae secretion chaperones PrsA, SlrA, and HtrA are required for competence, antibiotic resistance, colonization, and invasive disease
10.1128/iai.00490-23 · 2024 · External reference
Role of the penicillin-sensitive transpeptidation reaction in attachment of newly synthesized peptidoglycan to cell walls of Micrococcus luteus
10.1073/pnas.69.11.3355 · 1972 · External reference
Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria
10.1080/713610448 · 2003 · External reference
ClpB N-terminal domain plays a regulatory role in protein disaggregation
10.1073/pnas.1512783112 · 2015 · External reference
The C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate protein
10.1074/jbc.m114.577205 · 2014 · External reference
Structural basis of substrate progression through the bacterial chaperonin cycle
10.1073/pnas.2308933120 · 2023 · External reference
The protein secretion systems in Listeria: inside out bacterial virulence
10.1111/j.1574-6976.2006.00035.x · 2006 · External reference
Transposon mutagenesis as a tool to study the role of hemolysin in the virulence of Listeria monocytogenes
10.1128/iai.52.1.50-55.1986 · 1986 · External reference
Tn916-induced mutations in the hemolysin determinant affecting virulence of Listeria monocytogenes
10.1128/jb.169.3.1291-1297.1987 · 1987 · External reference
In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte-like cell line Caco-2
10.1128/iai.55.11.2822-2829.1987 · 1987 · External reference
Cytolysin-dependent delay of vacuole maturation in macrophages infected with Listeria monocytogenes
10.1111/j.1462-5822.2005.00604.x · 2006 · External reference
Hemolysin supports survival but not entry of the intracellular bacterium Listeria monocytogenes
10.1128/iai.56.1.79-82.1988 · 1988 · External reference
An mRNA-mRNA interaction couples expression of a virulence factor and its chaperone in Listeria monocytogenes
10.1016/j.celrep.2020.03.006 · 2020 · External reference
Dimeric Structure of the Bacterial Extracellular Foldase PrsA
10.1074/jbc.m114.622910 · 2015 · External reference
Unresolved reference
External reference
Intrinsic Disorder and Posttranslational Modifications: The Darker Side of the Biological Dark Matter
10.3389/fgene.2018.00158 · 2018 · External reference
Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci
10.1038/s41467-025-58692-8 · 2025 · External reference
The roles of the Listeria monocytogenes post-translocation chaperones PrsA1 and PrsA2 in protein secretion and stress resistance
10.1128/jb.00531-25 · 2026 · External reference
Intrinsically disordered protein regions are required for cell wall homeostasis in Bacillus subtilis
2022 · External reference
Tools for functional postgenomic analysis of listeria monocytogenes
10.1128/aem.00314-08 · 2008 · External reference
Secretion Chaperones PrsA2 and HtrA Are Required for Listeria monocytogenes Replication following Intracellular Induction of Virulence Factor Secretion
10.1128/iai.00312-16 · 2016 · External reference
A staphylococcal glucosaminidase drives inflammatory responses by processing peptidoglycan chains to physiological lengths
10.1128/iai.00500-22 · 2023 · External reference
Identification of a peptide-pheromone that enhances Listeria monocytogenes escape from host cell vacuoles
10.1371/journal.ppat.1004707 · 2015 · External reference
Isolation of Listeria monocytogenes small-plaque mutants defective for intracellular growth and cell-to-cell spread
10.1128/iai.58.11.3770-3778.1990 · 1990 · External reference
On the acquisition and analysis of microscale thermophoresis data
10.1016/j.ab.2015.12.013 · 2016 · External reference
Using two-site binding models to analyze microscale thermophoresis data
10.1016/j.ab.2017.10.013 · 2018 · External reference
Highly accurate protein structure prediction with AlphaFold
10.1038/s41586-021-03819-2 · 2021 · External reference
