| D008854 |
Microscopy, Electron |
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen. |
Electron Microscopy |
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| D009419 |
Nerve Tissue Proteins |
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Proteins, Nerve Tissue,Tissue Proteins, Nerve |
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| D010450 |
Endopeptidases |
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS. |
Endopeptidase,Peptide Peptidohydrolases |
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| D001927 |
Brain Diseases |
Pathologic conditions affecting the BRAIN, which is composed of the intracranial components of the CENTRAL NERVOUS SYSTEM. This includes (but is not limited to) the CEREBRAL CORTEX; intracranial white matter; BASAL GANGLIA; THALAMUS; HYPOTHALAMUS; BRAIN STEM; and CEREBELLUM. |
Intracranial Central Nervous System Disorders,Brain Disorders,CNS Disorders, Intracranial,Central Nervous System Disorders, Intracranial,Central Nervous System Intracranial Disorders,Encephalon Diseases,Encephalopathy,Intracranial CNS Disorders,Brain Disease,Brain Disorder,CNS Disorder, Intracranial,Encephalon Disease,Encephalopathies,Intracranial CNS Disorder |
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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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| D000682 |
Amyloid |
A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease. |
Amyloid Fibril,Amyloid Fibrils,Amyloid Substance,Fibril, Amyloid,Fibrils, Amyloid,Substance, Amyloid |
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| D000686 |
Amyloidosis |
A group of sporadic, familial and/or inherited, degenerative, and infectious disease processes, linked by the common theme of abnormal protein folding and deposition of AMYLOID. As the amyloid deposits enlarge they displace normal tissue structures, causing disruption of function. Various signs and symptoms depend on the location and size of the deposits. |
Amyloidoses |
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| D018622 |
PrP 27-30 Protein |
Protease-resistant core of PrPSc, the abnormal isoform of PRION PROTEINS. PrP 27-30 is produced by limited proteolysis of the N-terminus of PrPSc. |
Scrapie-Associated Fibrils,Fibril-Protein, Scrapie-Associated,Fibrils, Scrapie-Associated,Scrapie Associated Fibril-Protein,Scrapie PrP 27-30 Protein,Scrapie-Associated Fibril-Protein,Associated Fibril-Protein, Scrapie,Fibril Protein, Scrapie Associated,Fibril-Protein, Scrapie Associated,Fibrils, Scrapie Associated,PrP 27 30 Protein,Scrapie Associated Fibril Protein,Scrapie Associated Fibrils,Scrapie PrP 27 30 Protein |
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| D019286 |
Endopeptidase K |
An enzyme that catalyzes the hydrolysis of keratin, and of other proteins with subtilisin-like specificity. It hydrolyses peptide amides. Endopeptidase K is from the mold Tritirachium album Limber. (Enzyme Nomenclature, 1992) EC 3.4.21.64. |
Proteinase K,Protease K,Tritirachium Alkaline Proteinase,Alkaline Proteinase, Tritirachium,Proteinase, Tritirachium Alkaline |
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