A novel receptor - ligand pathway for entry of Francisella tularensis in monocyte-like THP-1 cells: interaction between surface nucleolin and bacterial elongation factor Tu.
about
N-Glycosylation influences the structure and self-association abilities of recombinant nucleolinSubversion of host recognition and defense systems by Francisella sppRSV fusion: time for a new modelNucleolin binds to a subset of selenoprotein mRNAs and regulates their expressionFine tuning inflammation at the front door: macrophage complement receptor 3-mediates phagocytosis and immune suppression for Francisella tularensisAn interbacterial NAD(P)(+) glycohydrolase toxin requires elongation factor Tu for delivery to target cellsAdherence and uptake of Francisella into host cellsTargeting surface nucleolin with a multivalent pseudopeptide delays development of spontaneous melanoma in RET transgenic miceNucleolin, a shuttle protein promoting infection of human monocytes by Francisella tularensis.Immunospecific responses to bacterial elongation factor Tu during Burkholderia infection and immunization.Surface expressed nucleolin is constantly induced in tumor cells to mediate calcium-dependent ligand internalization.Targeting surface nucleolin with multivalent HB-19 and related Nucant pseudopeptides results in distinct inhibitory mechanisms depending on the malignant tumor cell typeImmunoreactive Coxiella burnetii Nine Mile proteins separated by 2D electrophoresis and identified by tandem mass spectrometry.A new twist on plasma membrane repairTLR4-dependent activation of inflammatory cytokine response in macrophages by Francisella elongation factor Tu.The francisella intracellular life cycle: toward molecular mechanisms of intracellular survival and proliferation.Phagocytic receptors dictate phagosomal escape and intracellular proliferation of Francisella tularensis.Francisella tularensis uses cholesterol and clathrin-based endocytic mechanisms to invade hepatocytes.Entry of Francisella tularensis into Murine B Cells: The Role of B Cell Receptors and Complement ReceptorsImmunoproteomic profiling of Rickettsia parkeri and Rickettsia amblyommiiUropathogenic Escherichia coli Releases Extracellular Vesicles That Are Associated with RNANatural IgM mediates complement-dependent uptake of Francisella tularensis by human neutrophils via complement receptors 1 and 3 in nonimmune serum.Anaplasma phagocytophilum Asp14 is an invasin that interacts with mammalian host cells via its C terminus to facilitate infectionDisruption of Francisella tularensis Schu S4 iglI, iglJ, and pdpC genes results in attenuation for growth in human macrophages and in vivo virulence in mice and reveals a unique phenotype for pdpC.Mechanisms of Francisella tularensis intracellular pathogenesis.Pullulanase Is Necessary for the Efficient Intracellular Growth of Francisella tularensis.Discovery and development of the G-rich oligonucleotide AS1411 as a novel treatment for cancerComparative phosphoproteomics reveals components of host cell invasion and post-transcriptional regulation during Francisella infection.Borrelia burgdorferi elongation factor EF-Tu is an immunogenic protein during Lyme borreliosis.Loops and networks in control of Francisella tularensis virulence.Cell-surface nucleolin acts as a central mediator for carcinogenic, anti-carcinogenic, and disease-related ligands.Identification and characterisation of elongation factor Tu, a novel protein involved in Paracoccidioides brasiliensis-host interaction.Host glycosylation pathways and the unfolded protein response contribute to the infection by Francisella.Multifaceted effects of Francisella tularensis on human neutrophil function and lifespan.Complement C3 as a Prompt for Human Macrophage Death during Infection with Francisella tularensis Strain SCHU S4.Elongation factor Tu is a multifunctional and processed moonlighting protein.Exploitation of host cell biology and evasion of immunity by francisella tularensis.Innate Immune Recognition: Implications for the Interaction of Francisella tularensis with the Host Immune System.The Multiple Localized Glyceraldehyde-3-Phosphate Dehydrogenase Contributes to the Attenuation of the Francisella tularensis dsbA Deletion Mutant.Francisella tularensis Confronts the Complement System.
P2860
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P2860
A novel receptor - ligand pathway for entry of Francisella tularensis in monocyte-like THP-1 cells: interaction between surface nucleolin and bacterial elongation factor Tu.
description
2008 nî lūn-bûn
@nan
2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
A novel receptor - ligand path ...... acterial elongation factor Tu.
@ast
A novel receptor - ligand path ...... acterial elongation factor Tu.
@en
type
label
A novel receptor - ligand path ...... acterial elongation factor Tu.
@ast
A novel receptor - ligand path ...... acterial elongation factor Tu.
@en
prefLabel
A novel receptor - ligand path ...... acterial elongation factor Tu.
@ast
A novel receptor - ligand path ...... acterial elongation factor Tu.
@en
P2093
P2860
P356
P1433
P1476
A novel receptor - ligand path ...... acterial elongation factor Tu.
@en
P2093
Ara G Hovanessian
Jean-Paul Briand
Karin Meibom
Marion Dupuis
P2860
P2888
P356
10.1186/1471-2180-8-145
P577
2008-09-12T00:00:00Z
P5875
P6179
1031210727