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1 ole in degrading bacterial and mitochondrial N-formylated peptides.
2 asin-deficient mice, even in the presence of N-formylated peptides.
3 s Ib molecule with a high propensity to bind N-formylated peptides.
5 in nociceptor neurons, in part via bacterial N-formylated peptides and the pore-forming toxin alpha-h
6 + T cells, which recognize short hydrophobic N-formylated peptides, appear to comprise a substantial
9 ned whether hPepT1 could transport the model n-formylated peptide fMLP and, if so, whether such cellu
10 ed by prior exposure to the chemoattractants N-formylated peptides (fMLP) or a complement cleavage pr
11 f the fifth component of complement (C5a) or n-formylated peptides (formylmethionylleucylphenylalanin
12 complex (MHC) class Ib molecule H2-M3 binds N-formylated peptides from mitochondria and bacteria.
13 he cell surface by addition of high-affinity N-formylated peptides from mitochondria and listeria.
16 , whereas tapasin is critical for loading of N-formylated peptides onto the intracellular pool of M3.
17 e to the classic bacterial chemoattractants, n-formylated peptides, or other soluble bacterial factor
18 ein is catalytically active in deformylating N-formylated peptides, shares many of the properties of
24 le of the mouse with a unique preference for N-formylated peptides, which may come from the N-termini
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