| D007889 |
Leiomyoma |
A benign tumor derived from smooth muscle tissue, also known as a fibroid tumor. They rarely occur outside of the UTERUS and the GASTROINTESTINAL TRACT but can occur in the SKIN and SUBCUTANEOUS TISSUE, probably arising from the smooth muscle of small blood vessels in these tissues. |
Fibroid,Fibroid Tumor,Fibroid Uterus,Fibroids, Uterine,Fibroma, Uterine,Fibromyoma,Leiomyoma, Uterine,Fibroid Tumors,Fibroid, Uterine,Fibroids,Fibromas, Uterine,Fibromyomas,Leiomyomas,Tumor, Fibroid,Tumors, Fibroid,Uterine Fibroid,Uterine Fibroids,Uterine Fibroma,Uterine Fibromas,Uterus, Fibroid |
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| D008970 |
Molecular Weight |
The sum of the weight of all the atoms in a molecule. |
Molecular Weights,Weight, Molecular,Weights, Molecular |
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| D010446 |
Peptide Fragments |
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. |
Peptide Fragment,Fragment, Peptide,Fragments, Peptide |
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| D011485 |
Protein Binding |
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. |
Plasma Protein Binding Capacity,Binding, Protein |
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| 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 |
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| D003094 |
Collagen |
A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH). |
Avicon,Avitene,Collagen Felt,Collagen Fleece,Collagenfleece,Collastat,Dermodress,Microfibril Collagen Hemostat,Pangen,Zyderm,alpha-Collagen,Collagen Hemostat, Microfibril,alpha Collagen |
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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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| D000595 |
Amino Acid Sequence |
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. |
Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein |
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| D000596 |
Amino Acids |
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. |
Amino Acid,Acid, Amino,Acids, Amino |
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| D014357 |
Trypsin |
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4. |
Tripcellim,Trypure,beta-Trypsin,beta Trypsin |
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