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Structural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogenic factor from Porphyromonas gingivalis.
Okamoto K, Misumi Y, Kadowaki T, Yoneda M, Yamamoto K, Ikehara Y. Okamoto K, et al. Among authors: kadowaki t. Arch Biochem Biophys. 1995 Feb 1;316(2):917-25. doi: 10.1006/abbi.1995.1123. Arch Biochem Biophys. 1995. PMID: 7864651
Argingipain, so termed due to its peptide cleavage specificity at arginine residue, is a unique extracellular cysteine proteinase produced by the anaerobic rod Porphyromonas gingivalis, which is known as a major pathogenic factor of the progressive periodontal disease (T. …
Argingipain, so termed due to its peptide cleavage specificity at arginine residue, is a unique extracellular cysteine proteinase produced b …
Involvement of arginine-specific cysteine proteinase (Arg-gingipain) in fimbriation of Porphyromonas gingivalis.
Nakayama K, Yoshimura F, Kadowaki T, Yamamoto K. Nakayama K, et al. Among authors: kadowaki t. J Bacteriol. 1996 May;178(10):2818-24. doi: 10.1128/jb.178.10.2818-2824.1996. J Bacteriol. 1996. PMID: 8631669 Free PMC article.
Arginine-specific cysteine proteinase (Arg-gingipain [RGP], a major proteinase secreted from the oral anaerobic bacterium Porphyromonas gingivalis, is encoded by two separate genes (rgpA and rgpB) on the P. gingivalis chromosome and widely implicated as an important virulence fac …
Arginine-specific cysteine proteinase (Arg-gingipain [RGP], a major proteinase secreted from the oral anaerobic bacterium Porphyromonas ging …
1,598 results