| 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 |
|
| D009154 |
Mutation |
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. |
Mutations |
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| D009700 |
Nucleoside Deaminases |
Catalyze the hydrolysis of nucleosides with the elimination of ammonia. |
Deaminases, Nucleoside |
|
| D011506 |
Proteins |
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. |
Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene |
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| D012097 |
Repressor Proteins |
Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release. |
Repressor Molecules,Transcriptional Silencing Factors,Proteins, Repressor,Silencing Factors, Transcriptional |
|
| D003564 |
Cytidine Deaminase |
An enzyme that catalyzes the deamination of cytidine, forming uridine. EC 3.5.4.5. |
Cytidine Aminohydrolase,Aminohydrolase, Cytidine,Deaminase, Cytidine |
|
| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
|
| D000071479 |
APOBEC-1 Deaminase |
An APOBEC deaminase catalytic subunit of the apolipoprotein B (APOB) MESSENGER RNA (mRNA) editing enzyme complex that is involved in post-transcriptional editing of a CAA codon for GLYCINE to a UAA STOP CODON in the ApoB mRNA. It also functions in CGA (ARGININE) to UGA STOP CODON editing of NEUROFIBROMIN 1 mRNA and EPIGENETIC PROCESSES. |
APOBEC-1,APOBEC-1 Protein,APOBEC1 Deaminase,APOBEC1 Protein,Apo B mRNA Editing Protein,ApoB mRNA Editing Catalytic Subunit,Apolipoprotein B mRNA Editing Enzyme,Apolipoprotein B mRNA Editing Enzyme, Catalytic Polypeptide 1,HEPR Protein,APOBEC 1 Deaminase,APOBEC 1 Protein,Deaminase, APOBEC-1,Deaminase, APOBEC1 |
|
| D000071480 |
APOBEC-3G Deaminase |
An APOBEC deaminase that functions as an inhibitor of RETROVIRIDAE replication and inhibits the mobility of RETROTRANSPOSONS via deaminase-dependent and independent mechanisms. It is selective for SINGLE-STRANDED DNA and does not deaminate double-stranded DNA or single or DOUBLE-STRANDED RNA. It exhibits potent antiviral activity against VIF PROTEIN deficient HIV-1 through the creation of hypermutations in the VIRAL DNA. It also has anti-viral activity against SIMIAN IMMUNODEFICIENCY VIRUSES and HEPATITIS B VIRUS. |
APOBEC-3G Protein,APOBEC-3G dC-dU Editing Enzyme,APOBEC-Related Cytidine Deaminase,APOBEC-Related Protein,APOBEC3G Deaminase,APOBEC3G Protein,CEM15 Protein,APOBEC 3G Deaminase,APOBEC 3G Protein,APOBEC 3G dC dU Editing Enzyme,APOBEC Related Cytidine Deaminase,APOBEC Related Protein,Cytidine Deaminase, APOBEC-Related,Deaminase, APOBEC-3G,Deaminase, APOBEC3G |
|
| 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 |
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