| D008958 |
Models, Molecular |
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. |
Molecular Models,Model, Molecular,Molecular Model |
|
| D008969 |
Molecular Sequence Data |
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. |
Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular |
|
| D010744 |
Phosphoric Monoester Hydrolases |
A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. |
Phosphatase,Phosphatases,Phosphohydrolase,Phosphohydrolases,Phosphomonoesterase,Phosphomonoesterases,Phosphoric Monoester Hydrolase,Hydrolase, Phosphoric Monoester,Hydrolases, Phosphoric Monoester,Monoester Hydrolase, Phosphoric |
|
| 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 |
|
| D004260 |
DNA Repair |
The removal of DNA LESIONS and/or restoration of intact DNA strands without BASE PAIR MISMATCHES, intrastrand or interstrand crosslinks, or discontinuities in the DNA sugar-phosphate backbones. |
DNA Damage Response |
|
| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
|
| D000072181 |
Inositol Polyphosphate 5-Phosphatases |
Phosphoinositide phosphatases that catalyze the removal of the 5' phosphate from INOSITOL 1,4,5-TRISPHOSPHATE or myo-inositol 1,3,4,5-tetrakisphosphate, resulting in inositol 1,4-bisphosphate and phosphate. They have important functions in the metabolism of INOSITOL PHOSPHATES and inositol 1,4,5-trisphosphate signaling pathways such as CALCIUM SIGNALING. |
1,4,5-Triphosphate-1,2,4,5-Tetrakisphosphate 5-Phosphatase,Inositol 5-Phosphatase,Inositol Polyphosphate 5-Phosphatase,Inositol Triphosphate 5-Phosphatase,Inositol-1,4,5-Trisphosphate 5'-Phosphatase,Inositol-1,4,5-Trisphosphate 5-Phosphatase,Inositol-Polyphosphate 5-Phosphatase,Ins(1,4,5)P3 5'-Phosphatase,Inositol 5 Phosphatase,Inositol Polyphosphate 5 Phosphatase,Inositol Polyphosphate 5 Phosphatases,Inositol Triphosphate 5 Phosphatase |
|
| 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 |
|
| 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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