Pathogen specificity of Treponema pallidum subsp. pallidum integral membrane proteins identified by phase partitioning with Triton X-114
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Structural and Thermodynamic Characterization of the Interaction between Two Periplasmic Treponema pallidum Lipoproteins that are Components of a TPR-Protein-Associated TRAP Transporter (TPAT)Lipid modification of the 17-kilodalton membrane immunogen of Treponema pallidum determines macrophage activation as well as amphiphilicity.Outer membrane ultrastructure explains the limited antigenicity of virulent Treponema pallidumThe tprK gene is heterogeneous among Treponema pallidum strains and has multiple allelesCloning and DNA sequence analysis of an immunogenic glucose-galactose MglB lipoprotein homologue from Brachyspira pilosicoli, the agent of colonic spirochetosis.Biological basis for syphilis.Antigenic composition of Borrelia burgdorferi during infection of SCID mice.Sequence analysis of the 47-kilodalton major integral membrane immunogen of Treponema pallidum.Major integral membrane protein immunogens of Treponema pallidum are proteolipidsActivation of human monocytic cells by Treponema pallidum and Borrelia burgdorferi lipoproteins and synthetic lipopeptides proceeds via a pathway distinct from that of lipopolysaccharide but involves the transcriptional activator NF-kappa B.Similarity between the 38-kilodalton lipoprotein of Treponema pallidum and the glucose/galactose-binding (MglB) protein of Escherichia coli.Molecular cloning and characterization of the 15-kilodalton major immunogen of Treponema pallidumHLA-E-dependent presentation of Mtb-derived antigen to human CD8+ T cellsThe outer membrane, not a coat of host proteins, limits antigenicity of virulent Treponema pallidum.Purification and immunological characterization of a major low-molecular-weight lipoprotein from Borrelia burgdorferi.Immunogenic integral membrane proteins of Borrelia burgdorferi are lipoproteins.Molecular characterization of the pathogen-specific, 34-kilodalton membrane immunogen of Treponema pallidum.Polypeptides of Treponema pallidum: progress toward understanding their structural, functional, and immunologic roles. Treponema Pallidum Polypeptide Research Group.Sensitive detection of Treponema pallidum by using the polymerase chain reaction.
P2860
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P2860
Pathogen specificity of Treponema pallidum subsp. pallidum integral membrane proteins identified by phase partitioning with Triton X-114
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
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name
Pathogen specificity of Trepon ...... partitioning with Triton X-114
@en
type
label
Pathogen specificity of Trepon ...... partitioning with Triton X-114
@en
prefLabel
Pathogen specificity of Trepon ...... partitioning with Triton X-114
@en
P2860
P1476
Pathogen specificity of Trepon ...... partitioning with Triton X-114
@en
P2093
J D Radolf
M V Norgard
P2860
P304
P407
P577
1988-07-01T00:00:00Z