about
Evolutionary aspects of emerging Lyme disease in CanadaMolecular mechanisms involved in vascular interactions of the Lyme disease pathogen in a living hostReal-time high resolution 3D imaging of the lyme disease spirochete adhering to and escaping from the vasculature of a living hostIdentification 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.Invariant natural killer T cells act as an extravascular cytotoxic barrier for joint-invading Lyme Borrelia.Vascular binding of a pathogen under shear force through mechanistically distinct sequential interactions with host macromolecules.Biomechanics of Borrelia burgdorferi Vascular InteractionsIdentification of the determinant conferring permissive substrate usage in the telomere resolvase, ResTHyperglycemia Impairs Neutrophil-Mediated Bacterial Clearance in Mice Infected with the Lyme Disease PathogenThe Lyme Disease Pathogen Borrelia burgdorferi Infects Murine Bone and Induces Trabecular Bone Loss.Diet-Induced Obesity Does Not Alter Tigecycline Treatment Efficacy in Murine Lyme Disease.Infection with the Lyme disease pathogen suppresses innate immunity in mice with diet-induced obesity.Rapid upregulation of telomerase activity in human leukemia HL-60 cells treated with clinical doses of the DNA-damaging drug etoposide.Flow-Tolerant Adhesion of a Bacterial Pathogen to Human Endothelial Cells Through Interaction With Biglycan.Interactions between the discoidin domain receptor 1 and β1 integrin regulate attachment to collagenRole of discoidin domain receptor 1 in dysregulation of collagen remodeling by cyclosporin A.An extracellular Leptospira interrogans leucine-rich repeat protein binds human E- and VE-cadherins
P50
Q26795692-8075F70B-0368-4AED-9847-C321A08E7FC1Q27318431-B4E87B9F-E6FB-469D-AFBA-5600C4979EC4Q27318574-FEC433A4-F15D-4FDC-A634-D3CC4357DB12Q29994751-3475DB99-6DEA-49AD-9745-34E4620F08E9Q30152722-27B16F4C-DDFF-415C-809C-CA20DD5AF675Q30416325-B79FC364-0B71-4764-9BC9-81DD2FFF3AE4Q30528723-22A17B86-32BF-4DC7-AC46-CC409292EB0CQ30834956-6B723DA0-EC9E-4596-B4BB-07502FDB2C82Q33475522-7430D099-40B4-4CCF-8BA9-A595D1E53BD3Q36060840-B37733AE-82F0-4A63-BD1C-428F2FA6495FQ37611994-E8D4C09E-7308-4B68-8723-0DD5FC77880DQ37662663-439EE26D-AA67-43A2-A7E0-EBAEC63E8C08Q37740226-7973E926-A744-480E-8AA0-34117F01B7C4Q40728154-9D6DC1BD-F152-46FA-9F51-3C0782C39298Q40842255-46DA2558-449E-4E29-94F5-932AFF11D204Q42628692-8EC228A9-F514-4570-B208-D5E09CB6A8B5Q42829665-E53FDA7B-C9B9-4985-A952-3BFDACA5214AQ91256488-13114631-7CC3-43BF-BB3A-B46F95DEDDD3
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Tara J Moriarty
@ast
Tara J Moriarty
@en
Tara J Moriarty
@es
Tara J Moriarty
@nl
type
label
Tara J Moriarty
@ast
Tara J Moriarty
@en
Tara J Moriarty
@es
Tara J Moriarty
@nl
prefLabel
Tara J Moriarty
@ast
Tara J Moriarty
@en
Tara J Moriarty
@es
Tara J Moriarty
@nl
P108
P106
P1153
55202362800
P2038
Tara_Moriarty
P31
P496
0000-0002-1751-5145