title: Trefoil peptides. Coming up clover.
abstract: Now that information on trefoil domain structure is available from X-ray crystallographic and nuclear magnetic resonance spectroscopy studies, we can begin to understand the functions of these unusual protein motifs.
authors: Histopathology Unit, Imperial Cancer Research Fund, London, UK.
authors: B
authors: B
authors: Otto
authors: N
authors: N
authors: Wright
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009077:Mucins; D009124:Muscle Proteins; D009479:Neuropeptides; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D013552:Swine; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3
chemical_list: D036341:Intercellular Signaling Peptides and Proteins; D009077:Mucins; D009124:Muscle Proteins; D009479:Neuropeptides; D010455:Peptides; C099037:TFF3 protein, rat; D000071164:Trefoil Factor-2; D000071165:Trefoil Factor-3; C034407:pancreatic spasmolytic polypeptide