The Transition from Closed to Open Conformation of Treponema pallidum Outer Membrane-associated Lipoprotein TP0453 Involves Membrane Sensing and Integration by Two Amphipathic Helices
about
The TP0796 Lipoprotein of Treponema pallidum Is a Bimetal-dependent FAD Pyrophosphatase with a Potential Role in Flavin HomeostasisConsensus computational network analysis for identifying candidate outer membrane proteins from Borrelia spirochetes.Characterization of the β-barrel assembly machine accessory lipoproteins from Borrelia burgdorferi.Bipartite Topology of Treponema pallidum Repeat Proteins C/D and I: OUTER MEMBRANE INSERTION, TRIMERIZATION, AND PORIN FUNCTION REQUIRE A C-TERMINAL β-BARREL DOMAINStructural modeling and physicochemical characterization provide evidence that P66 forms a β-barrel in the Borrelia burgdorferi outer membrane.The major outer sheath protein (Msp) of Treponema denticola has a bipartite domain architecture and exists as periplasmic and outer membrane-spanning conformersTprC/D (Tp0117/131), a trimeric, pore-forming rare outer membrane protein of Treponema pallidum, has a bipartite domain structureActivation and proteolytic activity of the Treponema pallidum metalloprotease, pallilysin.Structural characterization and modeling of the Borrelia burgdorferi hybrid histidine kinase Hk1 periplasmic sensor: A system for sensing small molecules associated with tick feeding.Biophysical and bioinformatic analyses implicate the Treponema pallidum Tp34 lipoprotein (Tp0971) in transition metal homeostasisNovel Treponema pallidum Recombinant Antigens for Syphilis Diagnostics: Current Status and Future Prospects.Treponema pallidum, the syphilis spirochete: making a living as a stealth pathogen.The Treponema pallidum Outer Membrane.Identification of the Treponema pallidum subsp. pallidum TP0092 (RpoE) regulon and its implications for pathogen persistence in the host and syphilis pathogenesis.Functional insights from proteome-wide structural modeling of Treponema pallidum subspecies pallidum, the causative agent of syphilis.
P2860
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P2860
The Transition from Closed to Open Conformation of Treponema pallidum Outer Membrane-associated Lipoprotein TP0453 Involves Membrane Sensing and Integration by Two Amphipathic Helices
description
2011 nî lūn-bûn
@nan
2011 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
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2011年论文
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name
The Transition from Closed to ...... ion by Two Amphipathic Helices
@ast
The Transition from Closed to ...... ion by Two Amphipathic Helices
@en
The Transition from Closed to ...... ion by Two Amphipathic Helices
@nl
type
label
The Transition from Closed to ...... ion by Two Amphipathic Helices
@ast
The Transition from Closed to ...... ion by Two Amphipathic Helices
@en
The Transition from Closed to ...... ion by Two Amphipathic Helices
@nl
prefLabel
The Transition from Closed to ...... ion by Two Amphipathic Helices
@ast
The Transition from Closed to ...... ion by Two Amphipathic Helices
@en
The Transition from Closed to ...... ion by Two Amphipathic Helices
@nl
P2093
P2860
P3181
P356
P1476
The Transition from Closed to ...... ion by Two Amphipathic Helices
@en
P2093
Alejandro P Heuck
Amit Luthra
Arvind Anand
Christian H Eggers
Daniel C Desrosiers
Fabian B Romano
Fiona A McArthur
Guangyu Zhu
Justin D Radolf
Melissa J Caimano
P2860
P304
P3181
P356
10.1074/JBC.M111.305284
P407
P577
2011-12-02T00:00:00Z