| 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 |
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| D009953 |
Ornithine-Oxo-Acid Transaminase |
A pyridoxal phosphate enzyme that catalyzes the formation of glutamate gamma-semialdehyde and an L-amino acid from L-ornithine and a 2-keto-acid. EC 2.6.1.13. |
Ornithine Aminotransferase,Ornithine Transaminase,L-Ornithine-2-Oxo-Acid Aminotransferase,L-Ornithine-2-Oxoglutarate Aminotransferase,Ornithine Ketoacid Aminotransferase,Ornithine-2-Ketoglutarate Aminotransferase,Ornithine-Keto-Acid-Transaminase,Ornithine-Ketoacid-Transaminase,Pyrroline-5-Carboxylate Synthase,Aminotransferase, L-Ornithine-2-Oxo-Acid,Aminotransferase, L-Ornithine-2-Oxoglutarate,Aminotransferase, Ornithine,Aminotransferase, Ornithine Ketoacid,Aminotransferase, Ornithine-2-Ketoglutarate,Ketoacid Aminotransferase, Ornithine,L Ornithine 2 Oxo Acid Aminotransferase,L Ornithine 2 Oxoglutarate Aminotransferase,Ornithine 2 Ketoglutarate Aminotransferase,Ornithine Keto Acid Transaminase,Ornithine Ketoacid Transaminase,Ornithine Oxo Acid Transaminase,Pyrroline 5 Carboxylate Synthase,Synthase, Pyrroline-5-Carboxylate,Transaminase, Ornithine,Transaminase, Ornithine-Oxo-Acid |
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| D012150 |
Polymorphism, Restriction Fragment Length |
Variation occurring within a species in the presence or length of DNA fragment generated by a specific endonuclease at a specific site in the genome. Such variations are generated by mutations that create or abolish recognition sites for these enzymes or change the length of the fragment. |
RFLP,Restriction Fragment Length Polymorphism,RFLPs,Restriction Fragment Length Polymorphisms |
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| D004247 |
DNA |
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). |
DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
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| 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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| D001483 |
Base Sequence |
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. |
DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA |
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| D012333 |
RNA, Messenger |
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. |
Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated |
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| D015799 |
Gyrate Atrophy |
Progressive, autosomal recessive, diffuse atrophy of the choroid, pigment epithelium, and sensory retina that begins in childhood. |
Gyrate Atrophy of Choroid and Retina,Gyrate Atrophy of the Choroid and Retina,Hyperornithinemia with Gyrate Atrophy of Choroid and Retina,OAT Deficiency,OKT Deficiency,Ornithine Aminotransferase Deficiency,Ornithine Keto Acid Aminotransferase Deficiency,Ornithine Ketoacid Aminotransferase Deficiency,Ornithine-Delta-Aminotransferase Deficiency,Ornithinemia with Gyrate Atrophy,Atrophy, Gyrate,Deficiency, OAT,Deficiency, OKT,Deficiency, Ornithine Aminotransferase,Deficiency, Ornithine-Delta-Aminotransferase,Ornithine Delta Aminotransferase Deficiency |
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