| D007527 |
Isoenzymes |
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. |
Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes |
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| D008297 |
Male |
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Males |
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| D008310 |
Malocclusion |
Such malposition and contact of the maxillary and mandibular teeth as to interfere with the highest efficiency during the excursive movements of the jaw that are essential for mastication. (Jablonski, Illustrated Dictionary of Dentistry, 1982) |
Angle's Classification,Crossbite,Tooth Crowding,Cross Bite,Angle Classification,Angles Classification,Bite, Cross,Bites, Cross,Classification, Angle's,Cross Bites,Crossbites,Crowding, Tooth,Crowdings, Tooth,Malocclusions |
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| D008335 |
Mandibular Condyle |
The posterior process on the ramus of the mandible composed of two parts: a superior part, the articular portion, and an inferior part, the condylar neck. |
Condyle, Mandibular,Condyles, Mandibular,Mandibular Condyles |
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| D008810 |
Mice, Inbred C57BL |
One of the first INBRED MOUSE STRAINS to be sequenced. This strain is commonly used as genetic background for transgenic mouse models. Refractory to many tumors, this strain is also preferred model for studying role of genetic variations in development of diseases. |
Mice, C57BL,Mouse, C57BL,Mouse, Inbred C57BL,C57BL Mice,C57BL Mice, Inbred,C57BL Mouse,C57BL Mouse, Inbred,Inbred C57BL Mice,Inbred C57BL Mouse |
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| D009195 |
Peroxidase |
A hemeprotein from leukocytes. Deficiency of this enzyme leads to a hereditary disorder coupled with disseminated moniliasis. It catalyzes the conversion of a donor and peroxide to an oxidized donor and water. EC 1.11.1.7. |
Myeloperoxidase,Hemi-Myeloperoxidase,Hemi Myeloperoxidase |
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| D004195 |
Disease Models, Animal |
Naturally-occurring or experimentally-induced animal diseases with pathological processes analogous to human diseases. |
Animal Disease Model,Animal Disease Models,Disease Model, Animal |
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| D000071681 |
Tartrate-Resistant Acid Phosphatase |
One of several acid phosphatases in humans, other mammals, plants, and a few prokaryotes. The protein fold of tartrate-resistant acid phosphatase (TRAP) resembles that of the catalytic domain of plant purple acid phosphatase and other serine/threonine-protein phosphatases that also contain a metallophosphoesterase domain. One gene produces the various forms which include purple acid phosphatases from spleen and other tissues. Tartrate-resistant acid phosphatase is a biomarker for pathological states in which it is over-expressed. Such conditions include GAUCHER DISEASE; HODGKIN DISEASE; BONE RESORPTION; and NEOPLASM METASTASIS. |
AcPase V,Acid Phosphatase V,TRAP Type 5 AcPase,TRAcP,Tartrate-Resistant Acid Phosphatase Type 5,Type 5 Acid Phosphatase,Uteroferrin,Acid Phosphatase, Tartrate-Resistant,Phosphatase V, Acid,Phosphatase, Tartrate-Resistant Acid,Tartrate Resistant Acid Phosphatase,Tartrate Resistant Acid Phosphatase Type 5,V, AcPase,V, Acid Phosphatase |
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| D000135 |
Acid Phosphatase |
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2. |
Acid beta-Glycerophosphatase,Acid beta Glycerophosphatase |
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| 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 |
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