| D010455 |
Peptides |
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. |
Peptide,Polypeptide,Polypeptides |
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| D010861 |
Fimbriae, Bacterial |
Thin, hairlike appendages, 1 to 20 microns in length and often occurring in large numbers, present on the cells of gram-negative bacteria, particularly Enterobacteriaceae and Neisseria. Unlike flagella, they do not possess motility, but being protein (pilin) in nature, they possess antigenic and hemagglutinating properties. They are of medical importance because some fimbriae mediate the attachment of bacteria to cells via adhesins (ADHESINS, BACTERIAL). Bacterial fimbriae refer to common pili, to be distinguished from the preferred use of "pili", which is confined to sex pili (PILI, SEX). |
Bacterial Fimbriae,Bacterial Pili,Common Fimbriae,Common Pili,Pili, Bacterial,Pili, Common,Bacterial Fimbria,Bacterial Pilus,Common Fimbria,Common Pilus,Fimbria, Bacterial,Pilus, Bacterial,Fimbria, Common,Fimbriae, Common,Pilus, Common |
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| D011994 |
Recombinant Proteins |
Proteins prepared by recombinant DNA technology. |
Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
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| D001422 |
Bacterial Adhesion |
Physicochemical property of fimbriated (FIMBRIAE, BACTERIAL) and non-fimbriated bacteria of attaching to cells, tissue, and nonbiological surfaces. It is a factor in bacterial colonization and pathogenicity. |
Adhesion, Bacterial,Adhesions, Bacterial,Bacterial Adhesions |
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| D012471 |
Salivary Proteins and Peptides |
Proteins and peptides found in SALIVA and the SALIVARY GLANDS. Some salivary proteins such as ALPHA-AMYLASES are enzymes, but their composition varies in different individuals. |
Salivary Gland Protein,Salivary Gland Proteins,Salivary Peptide,Salivary Protein,Salivary Proteins,Salivary Peptides,Gland Protein, Salivary,Peptide, Salivary,Protein, Salivary,Protein, Salivary Gland |
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| D013291 |
Streptococcus |
A genus of gram-positive, coccoid bacteria whose organisms occur in pairs or chains. No endospores are produced. Many species exist as commensals or parasites on man or animals with some being highly pathogenic. A few species are saprophytes and occur in the natural environment. |
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| D016966 |
Porphyromonas gingivalis |
A species of gram-negative, anaerobic, rod-shaped bacteria originally classified within the BACTEROIDES genus. This bacterium produces a cell-bound, oxygen-sensitive collagenase and is isolated from the human mouth. |
Bacteroides gingivalis |
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| D055232 |
Proline-Rich Protein Domains |
Protein domains that are enriched in PROLINE. The cyclical nature of proline causes the peptide bonds it forms to have a limited degree of conformational mobility. Therefore the presence of multiple prolines in close proximity to each other can convey a distinct conformational arrangement to a peptide chain. |
Proline-Rich Peptide Domains,Domain, Proline-Rich Peptide,Domain, Proline-Rich Protein,Domains, Proline-Rich Peptide,Domains, Proline-Rich Protein,Peptide Domain, Proline-Rich,Peptide Domains, Proline-Rich,Proline Rich Peptide Domains,Proline Rich Protein Domains,Proline-Rich Peptide Domain,Proline-Rich Protein Domain,Protein Domain, Proline-Rich,Protein Domains, Proline-Rich |
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