Attachment of capsular polysaccharide to the cell wall of Streptococcus pneumoniae type 2 is required for invasive disease.
about
Microbial protein-tyrosine kinasesBacterial phosphoproteomic analysis reveals the correlation between protein phosphorylation and bacterial pathogenicityAutophosphorylation of the Bacterial Tyrosine-Kinase CpsD Connects Capsule Synthesis with the Cell Cycle in Streptococcus pneumoniaeCrystal Structures of Wzb of Escherichia coli and CpsB of Streptococcus pneumoniae, Representatives of Two Families of Tyrosine Phosphatases that Regulate Capsule AssemblyA widespread family of bacterial cell wall assembly proteinsChemical inhibition of bacterial protein tyrosine phosphatase suppresses capsule productionDominant role of nucleotide substitution in the diversification of serotype 3 pneumococci over decades and during a single infectionChanges in capsular serotype alter the surface exposure of pneumococcal adhesins and impact virulenceEvolution of bacterial protein-tyrosine kinases and their relaxed specificity toward substratesStreptococcus pneumoniae phosphotyrosine phosphatase CpsB and alterations in capsule production resulting from changes in oxygen availability.Capsular polysaccharide inhibits adhesion of Bifidobacterium longum 105-A to enterocyte-like Caco-2 cells and phagocytosis by macrophages.Extracellular matrix formation enhances the ability of Streptococcus pneumoniae to cause invasive diseaseSelf-regulation of exopolysaccharide production in Bacillus subtilis by a tyrosine kinase.CcpA ensures optimal metabolic fitness of Streptococcus pneumoniae.Contribution of a genomic accessory region encoding a putative cellobiose phosphotransferase system to virulence of Streptococcus pneumoniae.A random six-phase switch regulates pneumococcal virulence via global epigenetic changesDeletion of arcD in Streptococcus pneumoniae D39 impairs its capsule and attenuates virulenceThe Streptococcus pneumoniae capsule inhibits complement activity and neutrophil phagocytosis by multiple mechanismsIdentification of Streptococcus pneumoniae Cps2C residues that affect capsular polysaccharide polymerization, cell wall ligation, and Cps2D phosphorylationModification of the CpsA protein reveals a role in alteration of the Streptococcus agalactiae cell envelopeSequence elements upstream of the core promoter are necessary for full transcription of the capsule gene operon in Streptococcus pneumoniae strain D39.In vitro expression of Streptococcus pneumoniae ply gene in human monocytes and pneumocytesA tyrosine phosphorylation switch controls the interaction between the transmembrane modulator protein Wzd and the tyrosine kinase Wze of Lactobacillus rhamnosusCpsA, a LytR-CpsA-Psr Family Protein in Mycobacterium marinum, Is Required for Cell Wall Integrity and VirulenceMutations blocking side chain assembly, polymerization, or transport of a Wzy-dependent Streptococcus pneumoniae capsule are lethal in the absence of suppressor mutations and can affect polymer transfer to the cell wallStrain-specific regulatory role of eukaryote-like serine/threonine phosphatase in pneumococcal adherence.Sequetyping: serotyping Streptococcus pneumoniae by a single PCR sequencing strategy.High levels of genetic recombination during nasopharyngeal carriage and biofilm formation in Streptococcus pneumoniaeThe Variable Region of Pneumococcal Pathogenicity Island 1 Is Responsible for Unusually High Virulence of a Serotype 1 IsolateRegulatory interactions between a bacterial tyrosine kinase and its cognate phosphatase.Roles of virulence genes (PsaA and CpsA) on the invasion of Streptococcus pneumoniae into blood system.Virulence factors in pneumococcal respiratory pathogenesis.Identification of a Gene Cluster for the Biosynthesis of a Long, Galactose-Rich Exopolysaccharide in Lactobacillus rhamnosus GG and Functional Analysis of the Priming Glycosyltransferase.Staphylococcus aureus mutants lacking the LytR-CpsA-Psr family of enzymes release cell wall teichoic acids into the extracellular mediumPhosphoproteomics in bacteria: towards a systemic understanding of bacterial phosphorylation networks.Interaction of bacterial fatty-acid-displaced regulators with DNA is interrupted by tyrosine phosphorylation in the helix-turn-helix domain.Protein tyrosine phosphatase structure-function relationships in regulation and pathogenesis.The role of bacterial protein tyrosine phosphatases in the regulation of the biosynthesis of secreted polysaccharides.Erythrocyte and leukocyte: two partners in bacteria killing.Pneumococcal capsule synthesis locus cps as evolutionary hotspot with potential to generate novel serotypes by recombination.
P2860
Q27022003-F6B8EB48-1DFE-4915-A36E-5D60520B1E0FQ27027627-84EC8B85-3BC1-4367-A5E3-BE712FD511C0Q27310278-F94347D6-79E0-40DD-8266-E467D3E55915Q27656537-07073C4C-C6FB-43E7-85A1-4183A1A444F6Q27674661-7B341DFF-9666-4607-B794-128027D8E03DQ28483843-FB586557-46C9-418C-8ED7-9A27C0A98647Q28534306-C7FF54D0-37AA-43B9-B5C3-3B5869EAD2B0Q28743699-431111D6-8A80-4EA1-9D57-92F1A66B9C61Q33556655-518A6B5A-56A6-4000-9F56-374F584CEE47Q33570187-A0733B14-F72A-4183-BE7F-2B32445D5CEBQ33623573-D75C12C3-A22C-41EC-A8D7-717B36B5961EQ33911080-DD4202E4-2CFE-4807-ACF5-B1C66864A84BQ33984513-E9CDEAB0-3FD2-477C-9C33-0D8B47D5267DQ34062595-0CEB5737-2D1A-4B38-B884-0D33BDADF0C7Q34171731-F341DE14-8D21-4A16-B7AD-6D47E75C0354Q34310334-52B9916A-1F7B-4DB1-A178-D575C20CC6F6Q34362097-15D450DA-C8BE-4F92-BCA4-B346A484FAD4Q35015208-623F96A9-05A0-4E02-868C-6FA71CC90CB5Q35095863-F6EA209C-18E3-4995-AA6A-A3A9D7E71A99Q35187511-837D57D3-89BB-429A-A961-093FFCB35B33Q35439768-E4EE2D1D-AA52-4239-8F3B-64D23B1711BDQ35590921-65A29308-0761-4745-B60E-AAC7651A8618Q35606163-BC0F916C-FAEE-4D09-9D6B-1AA252A4E4C5Q35745625-1103AB30-00BD-4A6C-9658-C7CCDF8A2396Q35759822-D7355B64-92C3-4BF1-B2E3-E377B767D53EQ35867533-EAAD5259-4F02-4D89-8CB2-787DF1869397Q36118755-D1D11E7B-BF6A-467B-9056-280A7ED7E9CCQ36250577-1CC71016-0E77-44F3-95A8-7C93F349DCE1Q36631353-D3B48A24-EC67-4DFB-BD34-E676E987F78BQ36873686-48FA08DD-F98D-45D6-B566-B2E30B2DF569Q36964572-E59CA554-902C-47BE-8580-2CDDFD2AA315Q37119044-C489E719-3389-4D93-AE5F-7E80C54FD8D1Q37204377-5592439D-4F10-4EE7-A457-452AC2527285Q37253009-2A21A8D9-21EF-4863-B799-2ECFA78D8B8FQ37257668-E3557C80-2162-465B-A4EE-C4FA272A400FQ37271110-1D3D118C-5E32-4660-8011-2F14F7CAAF80Q38017355-566577C6-809F-4EF8-A06A-030BC54FFFBFQ38167882-2933FF0D-327B-44E4-A008-E33DCF375802Q38254601-53732D77-D8B5-4EAF-9FE7-67E2B2787535Q38736081-8ACD3054-E80F-4449-BDBE-1A7D29E29D22
P2860
Attachment of capsular polysaccharide to the cell wall of Streptococcus pneumoniae type 2 is required for invasive disease.
description
2006 nî lūn-bûn
@nan
2006 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Attachment of capsular polysac ...... required for invasive disease.
@ast
Attachment of capsular polysac ...... required for invasive disease.
@en
Attachment of capsular polysac ...... required for invasive disease.
@nl
type
label
Attachment of capsular polysac ...... required for invasive disease.
@ast
Attachment of capsular polysac ...... required for invasive disease.
@en
Attachment of capsular polysac ...... required for invasive disease.
@nl
prefLabel
Attachment of capsular polysac ...... required for invasive disease.
@ast
Attachment of capsular polysac ...... required for invasive disease.
@en
Attachment of capsular polysac ...... required for invasive disease.
@nl
P2093
P2860
P356
P1476
Attachment of capsular polysac ...... required for invasive disease.
@en
P2093
James C Paton
Judy K Morona
Renato Morona
P2860
P304
P356
10.1073/PNAS.0602148103
P407
P577
2006-05-17T00:00:00Z