Lipopeptide structure determines TLR2 dependent cell activation level.
about
International Union of Basic and Clinical Pharmacology. XCVI. Pattern recognition receptors in health and diseaseStructural and functional analysis of a platelet-activating lysophosphatidylcholine of Trypanosoma cruziIdentification of Adjuvantic Activity of Amphotericin B in a Novel, Multiplexed, Poly-TLR/NLR High-Throughput Screen.Brucella abortus uses a stealthy strategy to avoid activation of the innate immune system during the onset of infection.Immunogenecity of modified alkane polymers is mediated through TLR1/2 activation.Staphylococcal peptidoglycan co-localizes with Nod2 and TLR2 and activates innate immune response via both receptors in primary murine keratinocytesBrucella abortus ornithine lipids are dispensable outer membrane components devoid of a marked pathogen-associated molecular pattern.Immunological evaluation of lipopeptide group A streptococcus (GAS) vaccine: structure-activity relationshipExtracellular vesicles modulate host-microbe responses by altering TLR2 activity and phagocytosis.Characterization of a branched lipopeptide candidate vaccine against influenza A/Puerto Rico 8/34 which is recognized by human B and T-cell immune responses.Systematic review of membrane components of gram-positive bacteria responsible as pyrogens for inducing human monocyte/macrophage cytokine release.Mechanisms for the activation of Toll-like receptor 2/4 by saturated fatty acids and inhibition by docosahexaenoic acid.Atherosclerosis induced by endogenous and exogenous toll-like receptor (TLR)1 or TLR6 agonists.Comparison of the immunostimulatory and proinflammatory activities of candidate Gram-positive endotoxins, lipoteichoic acid, peptidoglycan, and lipopeptides, in murine and human cells.Synergistic interactions of TLR2/6 and TLR9 induce a high level of resistance to lung infection in mice.Mycobacterium avium glycopeptidolipids require specific acetylation and methylation patterns for signaling through toll-like receptor 2.Mycoplasma genitalium-encoded MG309 activates NF-kappaB via Toll-like receptors 2 and 6 to elicit proinflammatory cytokine secretion from human genital epithelial cells.Inflammasome-mediated secretion of IL-1β in human monocytes through TLR2 activation; modulation by dietary fatty acids.Novel toll-like receptor 2 ligands for targeted pancreatic cancer imaging and immunotherapy.Toll-Like Receptor 2 Recognizes Orientia tsutsugamushi and Increases Susceptibility to Murine Experimental Scrub TyphusTherapeutic targeting of Toll-like receptors for infectious and inflammatory diseases and cancer.Immune Response Modulation of Conjugated Agonists with Changing Linker LengthRadiation countermeasure agents: an update.An evolutionary strategy for a stealthy intracellular Brucella pathogen.Modulation of γδ T cell responses by TLR ligands.Lipoproteins in bacteria: structures and biosynthetic pathways.TLR2 & Co: a critical analysis of the complex interactions between TLR2 and coreceptors.Toll-like receptors' pathway disturbances are associated with increased susceptibility to infections in humans.Immunostimulation by synthetic lipopeptide-based vaccine candidates: structure-activity relationships.The Interplay between Daptomycin and the Immune System.Soluble human TLR2 ectodomain binds diacylglycerol from microbial lipopeptides and glycolipids.Diacylated lipopeptide from Mycoplasma synoviae mediates TLR15 induced innate immune responses.Synthesis and immunological evaluation of self-assembling and self-adjuvanting tricomponent glycopeptide cancer-vaccine candidates.Identification of full length bovine TLR1 and functional characterization of lipopeptide recognition by bovine TLR2/1 heterodimer.Structure-activity relationships in toll-like receptor 2-agonists leading to simplified monoacyl lipopeptides.Structure-activity relationships in toll-like receptor-2 agonistic diacylthioglycerol lipopeptides.A network of hydrogen bonds on the surface of TLR2 controls ligand positioning and cell signaling.Regulators of G-protein signalling are modulated by bacterial lipopeptides and lipopolysaccharide.Light Guided In-vivo Activation of Innate Immune Cells with Photocaged TLR 2/6 Agonist.Toll-like receptor 2 promiscuity is responsible for the immunostimulatory activity of nucleic acid nanocarriers.
P2860
Q28081406-E713D05A-90BF-48D1-BDD7-1BE85697E4A6Q28541704-1119B540-61D8-4C71-9819-DACD58947BFAQ30388683-B4831014-61B6-47ED-81F6-7B6B74EEA970Q33291121-F3B0C418-BFEF-41C9-BB63-C096779B0CCCQ33344511-65C3DC73-ADA1-43AE-A03B-D90085675940Q33719311-3A58317A-5F72-4544-BA77-17167C795C2FQ33797961-C5B9FC87-0C0C-4D8B-965A-FD5FAEA9BFB2Q34131142-0B10072F-1437-4D31-9F20-19D0F65FF7C0Q35106699-1A7D2B8B-FEB7-418E-BA50-979E1A9D86DAQ35133760-8ED28DAE-71FD-4B16-AFFC-FA44E3A15DB6Q35893715-C1278EA9-03EA-4019-8E72-3F0C3542411BQ35991819-7E832F80-99FD-44EC-8BE8-8E76182720B7Q36213874-B124E3D8-C426-4F92-A35E-376B333BA1DBQ36801478-BF1F171B-8DF4-41CD-89B6-E4004E1B96E1Q36845161-51004F3A-0DF2-414C-AA16-0380A1D5144CQ36981034-697281B4-2C50-4187-B1FF-557C24A04149Q37099478-95192CCF-672E-422D-9DBD-1FE634BED668Q37302656-5AD116FE-9E74-4E10-AA20-A881C1E1DFFBQ37389360-D6168B62-C5FE-4C52-8CA0-A9C018222DBDQ37424974-F147AC5C-CFFE-4F4A-AD4C-4E37420390E5Q37497786-8862C661-C86C-4ADE-BCD0-0B6C21053EA0Q37634354-EFA0DE24-A6BE-42A7-AA5D-18D4A7070E12Q37658857-6A2BC5FB-A323-420C-ACB2-6D1431CDCD33Q37846874-98BD4E9A-22A3-44D8-A3D4-CE09BC9B79CAQ37874203-C520C753-4071-4389-A091-F61324F0A66FQ38055247-EC726681-563A-430B-A782-4F459666F9E5Q38132733-25C96BF1-206A-47E9-B245-7ED3DD313B15Q38140711-C2055F5D-4B9A-4694-8299-D1D12F2352D2Q38153040-856CEABF-EC51-4CF2-BEAB-E88FF1A01224Q38191612-83273B4F-CDD3-4683-9B50-1EC51F9E7C1EQ38421961-88ABE6E5-3B17-4A3F-89C6-EAB0161F4BA1Q39077505-31BAE587-FA1E-4526-8737-34C1019D5189Q39254744-12BF5275-DA81-42F9-8F94-040458D9126CQ39380962-B7D47C2B-B975-496C-907B-8DA3DAA1A5C0Q39539750-EF5A7760-C694-493D-9E74-F97AA7EE5A43Q39725736-EF1FA305-4692-4193-A41B-2A20FE4D2DC2Q39763713-843D8B74-606B-4FF5-9347-58A210CB95AAQ39899161-A58A8E82-3F30-43DA-B093-5EC6E4D12AE4Q41388766-CD7175EA-E7AC-4E21-9D1A-2C058C24473AQ41762712-2666C27F-0D64-4CAD-85E6-1E0B1889FAE8
P2860
Lipopeptide structure determines TLR2 dependent cell activation level.
description
2005 nî lūn-bûn
@nan
2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
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
Lipopeptide structure determines TLR2 dependent cell activation level.
@ast
Lipopeptide structure determines TLR2 dependent cell activation level.
@en
type
label
Lipopeptide structure determines TLR2 dependent cell activation level.
@ast
Lipopeptide structure determines TLR2 dependent cell activation level.
@en
prefLabel
Lipopeptide structure determines TLR2 dependent cell activation level.
@ast
Lipopeptide structure determines TLR2 dependent cell activation level.
@en
P2093
P2860
P1433
P1476
Lipopeptide structure determines TLR2 dependent cell activation level.
@en
P2093
Artur J Ulmer
Günther Jung
Karl-Heinz Wiesmüller
Roland Brock
Ute Buwitt-Beckmann
P2860
P304
P356
10.1111/J.1742-4658.2005.05029.X
P407
P50
P577
2005-12-01T00:00:00Z