Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin.
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Current status of syphilis vaccine development: need, challenges, prospectsVaccinia virus 4c (A26L) protein on intracellular mature virus binds to the extracellular cellular matrix lamininPhysiological osmotic induction of Leptospira interrogans adhesion: LigA and LigB bind extracellular matrix proteins and fibrinogenA newly identified leptospiral adhesin mediates attachment to lamininThe Structure of Treponema pallidum Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fold That Mediates Adhesion to Extracellular Matrix Components and Interactions with Host Cells.The C-terminal variable domain of LigB from Leptospira mediates binding to fibronectin.Bifunctional role of the Treponema pallidum extracellular matrix binding adhesin Tp0751.Biological basis for syphilis.Activation and proteolytic activity of the Treponema pallidum metalloprotease, pallilysin.Progress towards an effective syphilis vaccine: the past, present and future.A novel Treponema pallidum antigen, TP0136, is an outer membrane protein that binds human fibronectinTreponema pallidum subsp. pallidum TP0136 protein is heterogeneous among isolates and binds cellular and plasma fibronectin via its NH2-terminal end.Post-translational modification of LipL32 during Leptospira interrogans infectionSyphilis: using modern approaches to understand an old disease.Heterologous expression of the Treponema pallidum laminin-binding adhesin Tp0751 in the culturable spirochete Treponema phagedenis.Treponema pallidum Lipoprotein TP0435 Expressed in Borrelia burgdorferi Produces Multiple Surface/Periplasmic Isoforms and mediates Adherence.A defined syphilis vaccine candidate inhibits dissemination of Treponema pallidum subspecies pallidum.The multifunctional role of the pallilysin-associated Treponema pallidum protein, Tp0750, in promoting fibrinolysis and extracellular matrix component degradationHuman pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host.Non-proteolytic functions of microbial proteases increase pathological complexity.Treponema pallidum, the syphilis spirochete: making a living as a stealth pathogen.Production of proinflammatory cytokines in the human THP-1 monocyte cell line following induction by Tp0751, a recombinant protein of Treponema pallidum.The Treponema pallidum Outer Membrane.
P2860
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P2860
Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin.
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2005 nî lūn-bûn
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2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի նոյեմբերին հրատարակված գիտական հոդված
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2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin.
@ast
Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin.
@en
Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin.
@nl
type
label
Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin.
@ast
Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin.
@en
Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin.
@nl
prefLabel
Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin.
@ast
Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin.
@en
Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin.
@nl
P2093
P2860
P1476
Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin.
@en
P2093
Caroline E Cameron
Janelle M Y Kuroiwa
Lisa M Tisch
Nathan L Brouwer
P2860
P304
P356
10.1128/IAI.73.11.7485-7494.2005
P407
P577
2005-11-01T00:00:00Z