| D003854 |
Deoxyribonucleotides |
A purine or pyrimidine base bonded to a DEOXYRIBOSE containing a bond to a phosphate group. |
Deoxyribonucleotide |
|
| D004789 |
Enzyme Activation |
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. |
Activation, Enzyme,Activations, Enzyme,Enzyme Activations |
|
| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
|
| D000076106 |
SAM Domain and HD Domain-Containing Protein 1 |
A host restriction triphosphorylhydrolase and dNTPase that contains an N-terminal STERILE ALPHA MOTIF and central, conserved ASPARTATE and HISTIDINE (HD) domain. It acts on single-stranded RNA, yielding deoxynucleosides and triphosphate, and functions in anti-viral defense through its dNTPase activity, reducing cellular dNTP levels below what is required for retroviral reverse transcription in DENDRITIC CELLS and MYELOID CELLS. It also has RIBONUCLEASE activity which blocks early replication of retroviruses such as HIV-1. Mutations in the SAMHD1 gene are associated with type 5 Aicardi-Goutieres syndrome (AGS5) and type 2 chilblain LUPUS (CHBL2). |
SAMHD1 Deoxynucleoside Triphosphate Triphosphohydrolase,SAMHD1 Protein,SAMHD1 dNTPase,SAM Domain and HD Domain Containing Protein 1 |
|
| D000494 |
Allosteric Regulation |
The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES. |
Regulation, Allosteric,Allosteric Regulations,Regulations, Allosteric |
|
| D013601 |
T-Lymphocytes |
Lymphocytes responsible for cell-mediated immunity. Two types have been identified - cytotoxic (T-LYMPHOCYTES, CYTOTOXIC) and helper T-lymphocytes (T-LYMPHOCYTES, HELPER-INDUCER). They are formed when lymphocytes circulate through the THYMUS GLAND and differentiate to thymocytes. When exposed to an antigen, they divide rapidly and produce large numbers of new T cells sensitized to that antigen. |
T Cell,T Lymphocyte,T-Cells,Thymus-Dependent Lymphocytes,Cell, T,Cells, T,Lymphocyte, T,Lymphocyte, Thymus-Dependent,Lymphocytes, T,Lymphocytes, Thymus-Dependent,T Cells,T Lymphocytes,T-Cell,T-Lymphocyte,Thymus Dependent Lymphocytes,Thymus-Dependent Lymphocyte |
|
| D055503 |
Protein Multimerization |
The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS. |
Protein Dimerization,Protein Heteromultimerizaton,Protein Multimer Assembly,Protein Trimerization,Assembly, Protein Multimer,Dimerization, Protein,Heteromultimerizaton, Protein,Heteromultimerizatons, Protein,Multimer Assembly, Protein,Multimerization, Protein,Trimerization, Protein |
|
| 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 |
|
| D020125 |
Mutation, Missense |
A mutation in which a codon is mutated to one directing the incorporation of a different amino acid. This substitution may result in an inactive or unstable product. (From A Dictionary of Genetics, King & Stansfield, 5th ed) |
Missense Mutation,Missense Mutations,Mutations, Missense |
|
| D020559 |
Monomeric GTP-Binding Proteins |
A class of monomeric, low molecular weight (20-25 kDa) GTP-binding proteins that regulate a variety of intracellular processes. The GTP bound form of the protein is active and limited by its inherent GTPase activity, which is controlled by an array of GTPase activators, GDP dissociation inhibitors, and guanine nucleotide exchange factors. This enzyme was formerly listed as EC 3.6.1.47 |
G-Proteins, Monomeric,GTP-Binding Proteins, Monomeric,Monomeric G-Protein,Monomeric G-Proteins,Small G-Protein,Small G-Proteins,Small GTPase,Small GTPases,ras-Related GTP-Binding Protein,ras-Related GTPase,ras-Related GTPases,ras-Related G-Proteins,ras-Related GTP-Binding Proteins,G Proteins, Monomeric,G-Protein, Monomeric,G-Protein, Small,G-Proteins, Small,G-Proteins, ras-Related,GTP Binding Proteins, Monomeric,GTP-Binding Protein, ras-Related,GTP-Binding Proteins, ras-Related,GTPase, Small,GTPase, ras-Related,GTPases, Small,GTPases, ras-Related,Monomeric G Protein,Monomeric G Proteins,Monomeric GTP Binding Proteins,Protein, ras-Related GTP-Binding,Proteins, ras-Related GTP-Binding,Small G Protein,Small G Proteins,ras Related G Proteins,ras Related GTP Binding Protein,ras Related GTP Binding Proteins,ras Related GTPase,ras Related GTPases |
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