Results 91 to 100 of about 670 (133)

TLR5 Gene [PDF]

, 2020
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TLR5 puts the brakes on [PDF]

Nature Reviews Microbiology, 2013
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TLR5 Protects Against Pulmonary Fibrosis [PDF]

A63. MEDIATORS OF LUNG FIBROSIS, 2020
Y. Sakamachi, A. Solis, S. Hussain, C.G. Johnson, Y. Zhang, F.C. Sciurba, I.V. Yang, D.A. Schwartz, E.K. Silverman, S. Garantziotis   +9 more
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Aimed at Subtype Discrimination but Yielding a Shared Marker: Integrative Analysis of Blood Transcriptomes Reveals Upregulated TLR5 as a Potential Biomarker for IBD

Clinical and Experimental Gastroenterology
Arman Mokaram Doust Delkhah Department of Genetics, Mashhad, IranCorrespondence: Arman Mokaram Doust Delkhah, Email arman.mokaram@gmail.comBackground: Despite the similarities, Crohn’s disease (CD) and ulcerative colitis (UC), the two major subtypes of ...
Mokaram Doust Delkhah A
doaj  

Toll-like receptor 5 (TLR5) [PDF]

Science-Business eXchange, 2009
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Toll-like receptor 5 (TLR5) [PDF]

Science-Business eXchange, 2008
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Toll-like receptor 5 (TLR5) [PDF]

Science-Business eXchange, 2013
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Helicobacter pylori flagellin: TLR5 evasion and fusion-based conversion into a TLR5 agonist

Biochemical and Biophysical Research Communications, 2018
Helicobacter pylori is a flagellated bacterium of the Epsilonproteobacteria class that causes peptic ulcers. Flagellin is a primary structural protein that assembles into the flagellar filament. Flagellins from bacteria that belong to the Gammaproteobacteria and Firmicutes groups are detected by Toll-like receptor 5 (TLR5) in the host, triggering the ...
Sung-Il Yoon, Seung Goo Kang, Wan Seok Song   +2 more
exaly   +3 more sources

TLR5: guardian of the gut

Trends in Microbiology, 2001
The human gastrointestinal tract is a dynamic melting pot of commensal bacteria. Although the apical surface of intestinal epithelial cells lining the gut is constantly exposed to proinflammatory bacterial products, this rarely results in an inflammatory response.
Mark Slifka, James D Brien
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TLR5 Tolls for Flagellin

Science Signaling, 2001
Hayashi et al. characterized the transmembrane Toll-like receptor (TLR) 5 protein and identified a physiologically relevant ligand capable of activating TLR5 signaling. Overexpression of chimeric proteins consisting of the intracellular domain of TLR5 fused to the extracellular domain of CD4 (to promote dimerization)
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