| 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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| 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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| D012720 |
Severity of Illness Index |
Levels within a diagnostic group which are established by various measurement criteria applied to the seriousness of a patient's disorder. |
Illness Index Severities,Illness Index Severity |
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| D016891 |
Polycystic Kidney, Autosomal Dominant |
Kidney disorders with autosomal dominant inheritance and characterized by multiple CYSTS in both KIDNEYS with progressive deterioration of renal function. |
Autosomal Dominant Polycystic Kidney,Kidney, Polycystic, Autosomal Dominant,ADPKD,Adult Polycystic Kidney Disease,Adult Polycystic Kidney Disease Type 1,Adult Polycystic Kidney Disease Type 2,Polycystic Kidney Disease 2,Polycystic Kidney Disease, Adult,Polycystic Kidney Disease, Adult Type 2,Polycystic Kidney Disease, Adult, Type II,Polycystic Kidney Disease, Autosomal Dominant,Polycystic Kidney Disease, Type 2,Polycystic Kidney, Type 1 Autosomal Dominant Disease,Polycystic Kidney, Type 2 Autosomal Dominant Disease |
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| 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 |
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| D050396 |
TRPP Cation Channels |
A subgroup of TRP cation channels that are widely expressed in various cell types. Defects are associated with POLYCYSTIC KIDNEY DISEASES. |
Polycystin,Polycystins,Cation Channels, TRPP,Channels, TRPP Cation |
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| D051379 |
Mice |
The common name for the genus Mus. |
Mice, House,Mus,Mus musculus,Mice, Laboratory,Mouse,Mouse, House,Mouse, Laboratory,Mouse, Swiss,Mus domesticus,Mus musculus domesticus,Swiss Mice,House Mice,House Mouse,Laboratory Mice,Laboratory Mouse,Mice, Swiss,Swiss Mouse,domesticus, Mus musculus |
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| D055879 |
Gene Knock-In Techniques |
Techniques used to add in exogenous gene sequence such as mutated genes; REPORTER GENES, to study mechanisms of gene expression; or regulatory control sequences, to study effects of temporal changes to GENE EXPRESSION. |
Gene Knock In,Gene Knock In Techniques,Gene Knock-In,Gene Knock Ins,Gene Knock-In Technique,Gene Knock-Ins,In, Gene Knock,Ins, Gene Knock,Knock In, Gene,Knock Ins, Gene,Knock-In Technique, Gene,Knock-In Techniques, Gene,Knock-In, Gene,Knock-Ins, Gene,Technique, Gene Knock-In,Techniques, Gene Knock-In |
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| D056426 |
Genetic Loci |
Specific regions that are mapped within a GENOME. Genetic loci are usually identified with a shorthand notation that indicates the chromosome number and the position of a specific band along the P or Q arm of the chromosome where they are found. For example the locus 6p21 is found within band 21 of the P-arm of CHROMOSOME 6. Many well known genetic loci are also known by common names that are associated with a genetic function or HEREDITARY DISEASE. |
Genetic Locus,Loci, Genetic,Locus, Genetic |
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| D019943 |
Amino Acid Substitution |
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties. |
Amino Acid Substitutions,Substitution, Amino Acid,Substitutions, Amino Acid |
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