Molecular mechanisms involved in vascular interactions of the Lyme disease pathogen in a living host - Test2 - elhamkhani - TriplyDB

Molecular mechanisms involved in vascular interactions of the Lyme disease pathogen in a living host

Molecular mechanisms involved in vascular interactions of the Lyme disease pathogen in a living host

http://www.wikidata.org/entity/Q27318431

about

Lyme disease and pediatric autoimmune neuropsychiatric disorders associated with streptococcal infections (PANDAS): an overview Low-shear force associated with modeled microgravity and spaceflight does not similarly impact the virulence of notable bacterial pathogens Human immunodeficiency virus and heparan sulfate: from attachment to entry inhibition Leptospira interrogans stably infects zebrafish embryos, altering phagocyte behavior and homing to specific tissues Intravital Imaging of Vascular Transmigration by the Lyme Spirochete: Requirement for the Integrin Binding Residues of the B. burgdorferi P66 Protein Multifunctional and Redundant Roles of Borrelia burgdorferi Outer Surface Proteins in Tissue Adhesion, Colonization, and Complement Evasion Spent culture medium from virulent Borrelia burgdorferi increases permeability of individually perfused microvessels of rat mesentery Borrelia burgdorferi BBK32 Inhibits the Classical Pathway by Blocking Activation of the C1 Complement Complex Interaction of variable bacterial outer membrane lipoproteins with brain endothelium Identification of Tp0751 (Pallilysin) as a Treponema pallidum Vascular Adhesin by Heterologous Expression in the Lyme disease Spirochete.The Structure of Treponema pallidum Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fold That Mediates Adhesion to Extracellular Matrix Components and Interactions with Host Cells.Live imaging reveals a biphasic mode of dissemination of Borrelia burgdorferi within ticks.Real-time imaging of trapping and urease-dependent transmigration of Cryptococcus neoformans in mouse brain.Analysis of a Borrelia burgdorferi phosphodiesterase demonstrates a role for cyclic-di-guanosine monophosphate in motility and virulence.Intravital microscopy: a novel tool to study cell biology in living animals Vascular binding of a pathogen under shear force through mechanistically distinct sequential interactions with host macromolecules.The unique paradigm of spirochete motility and chemotaxis.Biomechanics of Borrelia burgdorferi Vascular Interactions Plasma fibronectin stabilizes Borrelia burgdorferi-endothelial interactions under vascular shear stress by a catch-bond mechanism Passage through Ixodes scapularis ticks enhances the virulence of a weakly pathogenic isolate of Borrelia burgdorferi.The cyclic-di-GMP signaling pathway in the Lyme disease spirochete, Borrelia burgdorferi Human complement regulators C4b-binding protein and C1 esterase inhibitor interact with a novel outer surface protein of Borrelia recurrentis.Transposon mutagenesis as an approach to improved understanding of Borrelia pathogenesis and biology Bifunctional role of the Treponema pallidum extracellular matrix binding adhesin Tp0751.Effect of Borrelia burgdorferi OspC at the site of inoculation in mouse skin.Comparative molecular analyses of Borrelia burgdorferi sensu stricto strains B31 and N40D10/E9 and determination of their pathogenicity.Analysis of an ordered, comprehensive STM mutant library in infectious Borrelia burgdorferi: insights into the genes required for mouse infectivity.Spirochetal motility and chemotaxis in the natural enzootic cycle and development of Lyme disease Human coronavirus NL63 utilizes heparan sulfate proteoglycans for attachment to target cells Mapping the ligand-binding region of Borrelia hermsii fibronectin-binding protein Bioluminescent imaging of Borrelia burgdorferi in vivo demonstrates that the fibronectin-binding protein BBK32 is required for optimal infectivity On-Off Kinetics of Engagement of FNI Modules of Soluble Fibronectin by β-Strand Addition.Glycosaminoglycan binding by Borrelia burgdorferi adhesin BBK32 specifically and uniquely promotes joint colonization.Disruption of bbe02 by Insertion of a Luciferase Gene Increases Transformation Efficiency of Borrelia burgdorferi and Allows Live Imaging in Lyme Disease Susceptible C3H Mice.A short-term Borrelia burgdorferi infection model identifies tissue tropisms and bloodstream survival conferred by adhesion proteins.BB0744 Affects Tissue Tropism and Spatial Distribution of Borrelia burgdorferi The role of Borrelia burgdorferi outer surface proteins The early dissemination defect attributed to disruption of decorin-binding proteins is abolished in chronic murine Lyme borreliosis.Motility is crucial for the infectious life cycle of Borrelia burgdorferi.The BBA33 lipoprotein binds collagen and impacts Borrelia burgdorferi pathogenesis.

P2860

Q24626864-6508859D-4AB2-4117-BC2D-A3EC7D2C2E8C Q26829418-4500A130-AD46-4493-A72A-DA28AC8B9D54 Q27004059-55B25DC6-DE8D-4EAC-B799-C201355E1A3C Q27306865-C9E2E881-DCF5-463C-BFAA-9A4963135C35 Q27316620-6584A8A2-963D-472E-BA24-BCFA8CF146A8 Q28067065-390E75F2-BEA0-4ED6-9E92-440F453FAD56 Q28386750-548CC8A5-D6FF-4A0E-8104-62741E5AD225 Q28552790-59A45583-51E6-4088-B1BB-333E2A6BC4D3 Q28748750-896BE846-BFE0-49F5-8CD6-C79D5A68EE5C Q29994751-1C1A2974-5103-4D6A-BC59-85327DB85D0C Q30152722-E31E2E3A-FC47-497D-8F83-9C7D225E5147 Q30492103-FCF7B40C-5F58-4953-AA95-7BBC6BC96677 Q30494253-55DFC8AA-CC81-4978-9E55-E459995525A1 Q30495592-1E8FEF39-773E-4B32-824C-08CCF8D9E83F Q30497996-E10917A6-2051-45D0-BAF9-52AB1601DBA4 Q30528723-537F0C7E-83E5-40F2-8556-EBE131F4DC9E Q30544647-7F01B2FF-9819-43D7-8190-3E115767C07E Q30834956-3F46128E-60BC-45B2-B70D-C34125DD9A66 Q30847374-D11D970E-7B2F-4743-81A7-94A768D4A88B Q33557840-8FFB9123-B241-46B4-8EF5-57F245C552EB Q33579968-C6BEB37F-98B3-48EA-BCBD-564588E38548 Q33598636-194A72D4-14A2-47D2-A2BA-A480EF367DC1 Q33658532-F2FF80EC-6A9B-4358-8DB9-FEB575C9BF67 Q33768367-7FD9F9AF-F1C5-4435-8031-A47E5F10AD75 Q34290663-35574FAC-F0B9-478E-815D-4E444EBB0F07 Q34356943-96D1A396-9C13-4714-A4D1-FEF40F85A8EC Q34469139-B0903AC9-2748-4202-86FA-8A2A53786614 Q34500039-B2FAA6EB-39C3-4E9F-8E39-7E4EE4B94DEB Q34594739-DB13A607-C045-4451-9A03-46F3694473BC Q34651675-1BE9FE12-5C7F-4A0B-94AF-4C70438566BB Q35242498-C948ED6C-D824-4153-B96F-5EBBA9A9F7EC Q35616484-60CA6ABD-3502-485C-9B88-CACE6E898693 Q35625165-04F0D134-6A53-4255-A6B4-891943B837B6 Q35662243-877C5A51-49E2-4D4D-B7E9-4558CF873EFD Q35833788-89D6E25A-CB8F-49A2-AD2F-41A0B28413A3 Q35947346-64817290-1301-47DF-9BB1-FB2154AF628C Q36179733-328798A7-E634-45B6-8784-3D5A5AD888F5 Q36826979-C3077CD7-BA7A-4B26-9FE3-65A2987DAC4C Q36911398-9B3F563D-FD7F-4DB3-A0ED-8BA20FBD19B3 Q37143419-C5C0209E-53E3-4989-A10C-3D29D6DDD4D9

P2860

Molecular mechanisms involved in vascular interactions of the Lyme disease pathogen in a living host

http://www.wikidata.org/entity/Q27318431

description

2008 nî lūn-bûn

@nan

2008 թուականին հրատարակուած գիտական յօդուած

@hyw

2008 թվականին 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

Molecular mechanisms involved ...... ease pathogen in a living host

@ast

Molecular mechanisms involved ...... ease pathogen in a living host

@en

Molecular mechanisms involved ...... ease pathogen in a living host

@nl

type

label

Molecular mechanisms involved ...... ease pathogen in a living host

@ast

Molecular mechanisms involved ...... ease pathogen in a living host

@en

Molecular mechanisms involved ...... ease pathogen in a living host

@nl

prefLabel

Molecular mechanisms involved ...... ease pathogen in a living host

@ast

Molecular mechanisms involved ...... ease pathogen in a living host

@en

Molecular mechanisms involved ...... ease pathogen in a living host

@nl

P1433

Q27318431-1FE936B6-3888-4226-A1A0-3D04EF011A15

P1476

Q27318431-0FBDC4F3-8B47-4DEE-8D78-ED3840DDD242

P2093

Q27318431-1034C549-8065-4F6C-94A6-29F1391B5013

Q27318431-142A92AB-3A57-4194-9729-67C68BAF59BE

Q27318431-2B9CD598-E93A-47F6-B878-C47DE857227E

Q27318431-CEA5BF84-2CE7-4132-9666-2E8E66DFAAA7

Q27318431-DCEDB2BD-B787-43F5-9B19-3BD8E7ECC544

P2860

Q27318431-0189B493-B8C9-467F-AF3F-82FA9173C6E2

Q27318431-091F1FC3-D8ED-4DDD-AC1F-615B17812328

Q27318431-0CC06920-57D2-4408-81B2-BC11E4C5698D

Q27318431-0FAAEC8B-EC8C-4244-970D-6B0D771F7A50

Q27318431-10BAA9CF-8F85-48FB-B026-2644B061FC8E

Q27318431-15F19272-431A-4C50-89DC-32D21E9789E7

Q27318431-266AA5D2-CEFA-4D06-824E-3777038F4529

Q27318431-31EAF4E3-D584-485D-9C7D-16E7660BF580

Q27318431-32E00A5A-87E3-482E-B5E4-B97D27645572

Q27318431-34B6AA3C-8654-42C3-ADF2-2BDA54C9CCE8

P304

Q27318431-9F697D56-2671-4B11-B687-5965E896C70A

P31

Q27318431-8E0A5207-BE5F-458B-9608-EAA27CDA50E1

P3181

Q27318431-9FAB1B01-30CF-4AA5-A373-14F4BA9A1E80

P356

Q27318431-8A036645-6E03-4B1F-974B-5F8473AFE5F5

P407

Q27318431-90249DE5-B48E-41B3-A285-EE26F2FDDAAE

P433

Q27318431-00C4C620-1EED-40BD-BC0B-369DBF092A13

P478

Q27318431-69310A3D-71DA-4E43-98B4-8A7FB7C1526E

P50

Q27318431-B4E87B9F-E6FB-469D-AFBA-5600C4979EC4

P577

Q27318431-45141EBF-0CC0-4DC3-884D-E7B62559A47D

P5875

Q27318431-475C38E7-C85C-4962-BD09-70E98DAF3E61

P698

Q27318431-CB5BCE99-7B73-413F-BD25-BB8A60D684D2

P921

Q27318431-EF7817DD-4D45-4894-965D-E210F34D7C77

P932

Q27318431-32FCF409-C63D-416C-B6B0-D72B8E90589A

P3181

P356

JOURNAL.PPAT.1000169

P1433

P1476

Molecular mechanisms involved ...... ease pathogen in a living host

@en

P2093

Ashley R Dresser

http://www.w3.org/2001/XMLSchema#string

Brandie Millen

http://www.w3.org/2001/XMLSchema#string

George Chaconas

http://www.w3.org/2001/XMLSchema#string

M Ursula Norman

http://www.w3.org/2001/XMLSchema#string

Paul Kubes

http://www.w3.org/2001/XMLSchema#string

P2860

The emergence of Lyme disease

Possibilities for relapsing fever reemergence

Real-time high resolution 3D imaging of the lyme disease spirochete adhering to and escaping from the vasculature of a living host

Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper

Novel adhesin from Pasteurella multocida that binds to the integrin-binding fibronectin FnIII9-10 repeats

BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding

For catch bonds, it all hinges on the interdomain region: Figure 1.

Characterization of a candidate Borrelia burgdorferi beta3-chain integrin ligand identified using a phage display library.

Decorin-binding protein of Borrelia burgdorferi is encoded within a two-gene operon and is protective in the murine model of Lyme borreliosis

Borrelia burgdorferi adhesins identified using in vivo phage display.

P304

e1000169

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

2852557

http://www.w3.org/2001/XMLSchema#string

P356

10.1371/JOURNAL.PPAT.1000169

http://www.w3.org/2001/XMLSchema#string

P407

P433

10

http://www.w3.org/2001/XMLSchema#string

P478

4

http://www.w3.org/2001/XMLSchema#string

P50

Tara J Moriarty

P577

2008-10-03T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

23297863

http://www.w3.org/2001/XMLSchema#string

P698

18833295

http://www.w3.org/2001/XMLSchema#string

P921

P932

2542414

http://www.w3.org/2001/XMLSchema#string