Biomaterial Database

Protein disulfide isomerase and assisted protein folding. 1997

H F Gilbert

Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030, USA. hgilbert@bcm.tmc.edu

UI	MeSH Term	Description	Entries
D008956	Models, Chemical	Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.	Chemical Models,Chemical Model,Model, Chemical
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D002384	Catalysis	The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.	Catalyses
D004220	Disulfides	Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.	Disulfide
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D017510	Protein Folding	Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.	Protein Folding, Globular,Folding, Globular Protein,Folding, Protein,Foldings, Globular Protein,Foldings, Protein,Globular Protein Folding,Globular Protein Foldings,Protein Foldings,Protein Foldings, Globular
D019704	Protein Disulfide-Isomerases	Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.	Protein Disulfide Isomerase,Protein Disulfide-Isomerase,Disulfide Interchange Enzyme,Disulfide Isomerase,Glycosylation Site-Binding Protein,Sulfhydryl-Disulfide Interchange Enzyme,Thiol-Disulfide Transhydrogenase,Trypanothione-Glutathione Thioltransferase,Disulfide Isomerase, Protein,Disulfide-Isomerase, Protein,Disulfide-Isomerases, Protein,Enzyme, Disulfide Interchange,Enzyme, Sulfhydryl-Disulfide Interchange,Glycosylation Site Binding Protein,Interchange Enzyme, Disulfide,Interchange Enzyme, Sulfhydryl-Disulfide,Isomerase, Disulfide,Isomerase, Protein Disulfide,Protein Disulfide Isomerases,Protein, Glycosylation Site-Binding,Site-Binding Protein, Glycosylation,Sulfhydryl Disulfide Interchange Enzyme,Thiol Disulfide Transhydrogenase,Thioltransferase, Trypanothione-Glutathione,Transhydrogenase, Thiol-Disulfide,Trypanothione Glutathione Thioltransferase