ENTITY
stringlengths 8
8
| DEFINITION
stringlengths 3
8.47k
⌀ | ALIASES
stringlengths 2
13.6k
⌀ | NAME
stringlengths 2
1.98k
|
|---|---|---|---|
C1335785 | Encoded by human RNR1 Gene, RNA Ribosomal 1 is a ribosomal RNA associated with proteins as structural components of a ribosome where polypeptides are produced by interacting with tRNA and mRNA. (From NCI) | RNA, Ribosomal 1|RNR1|Ribosomal RNA-1 | RNA, Ribosomal 1 |
C1336786 | General transcription factor IIF subunit 1 (517 aa, ~58 kDa) is encoded by the human GTF2F1 gene. This protein plays a role in the modulation of transcription, RNA elongation and RNA splicing. | General Transcription Factor IIF1 74kDa|GTF2F1|General Transcription Factor IIF 74 kDa Subunit|Transcription Initiation Factor IIF Subunit Alpha|Transcription Initiation Factor RAP74|General Transcription Factor IIF Subunit 1|Transcription Initiation Factor IIF Alpha Subunit|TFIIF-Alpha | GT2F1 protein, human |
C1336786 | General transcription factor IIF subunit 1 (517 aa, ~58 kDa) is encoded by the human GTF2F1 gene. This protein plays a role in the modulation of transcription, RNA elongation and RNA splicing. | General Transcription Factor IIF1 74kDa|GTF2F1|General Transcription Factor IIF 74 kDa Subunit|Transcription Initiation Factor IIF Subunit Alpha|Transcription Initiation Factor RAP74|General Transcription Factor IIF Subunit 1|Transcription Initiation Factor IIF Alpha Subunit|TFIIF-Alpha | GT2F1 protein, human |
C0025965 | An enzyme that catalyzes the endonucleolytic cleavage to 3'-phosphomononucleotide and 3'-phospholigonucleotide end-products. It can cause hydrolysis of double- or single-stranded DNA or RNA. (From Enzyme Nomenclature, 1992) EC 3.1.31.1. | Nuclease, Micrococcal|TNase|Micrococcal endonuclease|Micrococcal nuclease (substance)|Nuclease, Thermostable|Thermostable Nuclease|Micrococcal nuclease|Nuclease, Staphylococcal|Thermonuclease|Staphylococcal Nuclease | Micrococcal Nuclease |
C0524550 | A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts). [PMID:10197977] | NER|Nucleotide-Excision Repair|pyrimidine-dimer repair, DNA damage excision|Nucleotide Excision Repairs|Nucleotide Excision Repair|Excision Repair, Nucleotide|nucleotide-excision repair | Nucleotide Excision Repair |
C0028954 | Peptides composed of between two and twelve amino acids. | oligopeptides|Oligopeptides|oligopeptide | Oligopeptides |
C0076934 | Enzymes that recombine DNA segments by a process which involves the formation of a synapse between two DNA helices, the cleavage of single strands from each DNA helix and the ligation of a DNA strand from one DNA helix to the other. The resulting DNA structure is called a Holliday junction which can be resolved by DNA REPLICATION or by HOLLIDAY JUNCTION RESOLVASES. | Transposases|transposase|Transposase | Transposase |
C0225328 | General anatomical term which refers to component of a fiber, e.g. collagen fibril or myofibril. | Fibril (substance)|Fibril|fibril|Fibril, NOS|fibrils | Fibril - cell component |
C0014274 | The transfer of energy of a given form among different scales of motion. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed). It includes the transfer of kinetic energy and the transfer of chemical energy. The transfer of chemical energy from one molecule to another depends on proximity of molecules so it is often used as in techniques to measure distance such as the use of FORSTER RESONANCE ENERGY TRANSFER. | Transfer, Energy|Energy transfer|Energy transfer, function (observable entity)|energy transfer|Energy transfer, function | Energy Transfer |
C1519751 | The process in which one or more ubiquitin groups are added to a protein. [GOC:ai] | Ubiquitination|Protein Ubiquitination|protein ubiquitination|protein ubiquitinylation|Ubiquitinoylation|protein ubiquitylation|ubiquitylation|Ubiquitylation|Ubiquitilation|ubiquitinylation | Ubiquitination |
C0043357 | null | Xiphophorus | Xiphophorus |
C1123023 | The outer covering of the body that protects it from the environment. It is composed of the DERMIS and the EPIDERMIS. | skin|SKIN|integument|skin structure|Piel|Integumental system|Integument|Skin|cutaneous tissue|Skin of body|integumental system|Skin, NOS|skinned|Skin structure|Skin structure (body structure)|skin system|Cutis|skins | Skin |
C0061928 | Proteins that activate the GTPase of specific GTP-BINDING PROTEINS. | GAP Protein|GAP Proteins|guanosinetriphosphatase activating protein|GTPase-Activating Protein|GAP|GTPase-activating protein|GTPase Activating Proteins|GTPase-Activating Proteins|GTPase Activating Protein (GAP)|GTPase Activating Protein|GTPase activating protein | GTPase-Activating Proteins |
C0756801 | null | epsin | epsin |
C0031621 | Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids. | Phosphatidyl inositol (substance)|PtdIns|Inositol Phospholipids|Inositol, Phosphatidyl|Inositide Phospholipids|Phospholipids, Inositide|Inositol Phosphoglycerides|Phosphatidylinositols|Phosphatidyl Inositol|Phosphatidylinositol|phosphatidyl inositol|phosphoinositide|PI|Phosphatidyl inositol|phosphatidylinositol|Phosphoglycerides, Inositol|inositol phospholipid|Phospholipids, Inositol|Phosphoinositides | phosphatidylinositols |
C1331027 | null | Avar | Avar |
C1331027 | null | Avar | Avar |
C0598496 | Any process carried out at the cellular level that results in either long-term transcriptional repression via action on chromatin structure or RNA mediated, post-transcriptional repression of gene expression. [GOC:dos, GOC:dph, GOC:jid, GOC:tb] | Silencing, Gene|gene silencing|silencing gene|Inactivation, Gene|Gene Inactivation|Gene silencing | Gene Silencing |
C0246957 | Cyclin-dependent kinase 4 is a key regulator of G1 PHASE of the CELL CYCLE. It partners with CYCLIN D to phosphorylate RETINOBLASTOMA PROTEIN. CDK4 activity is inhibited by CYCLIN-DEPENDENT KINASE INHIBITOR P16. | Cyclin-Dependent Kinase 4|Cyclin Dependent Kinase 4|Cyclin D-Dependent Kinase CDK4|Cyclin D Dependent Kinase CDK4|Protein Kinase, Cdk4|Cdk4 Cyclin-Dependent Kinase|PSK-J3 Kinase|Cyclin-Dependent Kinase, Cdk4|Cell Division Protein Kinase 4|p34PSK J3 Kinase|cyclin D dependent kinase (CDK4) protein|Cdk4 Protein Kinase|cdk4|Cdk4 Cyclin Dependent Kinase|p34PSK-J3 Kinase|Cdk4 Protein|PSK J3 Kinase|CDK4 | Cyclin-Dependent Kinase 4 |
C0281630 | null | monoclonal antibody 3F8/sargramostim|GM-CSF/MOAB 3F8 | Monoclonal Antibody 3F8/Sargramostim |
C0281630 | null | monoclonal antibody 3F8/sargramostim|GM-CSF/MOAB 3F8 | Monoclonal Antibody 3F8/Sargramostim |
C0285207 | null | AWD-19-166 | AWD 19166 |
C0285207 | null | AWD-19-166 | AWD 19166 |
C1281094 | null | Entire olfactory bulb|Entire olfactory bulb (body structure) | Entire olfactory bulb |
C0020663 | Ventral part of the DIENCEPHALON extending from the region of the OPTIC CHIASM to the caudal border of the MAMMILLARY BODIES and forming the inferior and lateral walls of the THIRD VENTRICLE. | hypothalamus|BRAIN, HYPOTHALAMUS|Preoptico-Hypothalamic Areas|Hypothalamic structure|hypothalamic|Preoptico-hypothalamic region|Preoptico-hypothalamic area|Area, Preoptico-Hypothalamic|HYPOTHALAMUS|Preoptico Hypothalamic Area|Hypothalamus|Hypothalamic|Hypothalamic structure (body structure)|Hypothalamus, NOS|Preoptico-Hypothalamic Area|Areas, Preoptico-Hypothalamic | Hypothalamic structure |
C0023610 | A decapeptide that stimulates the synthesis and secretion of both pituitary gonadotropins, LUTEINIZING HORMONE and FOLLICLE STIMULATING HORMONE. GnRH is produced by neurons in the septum PREOPTIC AREA of the HYPOTHALAMUS and released into the pituitary portal blood, leading to stimulation of GONADOTROPHS in the ANTERIOR PITUITARY GLAND. | Gonadorelin (substance)|Luteinizing hormone releasing factor (LHRF) (LH/RF)|LH Releasing Hormone|Gonadotrophin Releasing Hormone|gonadotropin RH|Gonadotropin releasing hormone|Gonadotrophin releasing factor preparation|Luteinizing hormone releasing factor|Gonadorelina|GRF (gonadotropin releasing factor)|lh-rh|FSH-Releasing Hormone|Gonadotropin Releasing Hormone|gonadotropin releasing factor|gonadotropin-releasing factor|LH-FSH Releasing Hormone|follicle stimulating hormone-releasing factor|Product containing gonadorelin (medicinal product)|Follicle Stimulating Hormone-Releasing Factor|GRH - Gonadotrophin releasing hormone|Gonadorelin-containing product|Product containing gonadotropin releasing factor (product)|Luteotropin-releasing factor|LHFSH Releasing Hormone|Gonadotropin-releasing hormones|gonadotropin releasing hormone|luliberin|grh|Gonadorelin|gonadorelin hormone|LH/RF|LHFSHRH|FRF|LH-FSH releasing hormone|GRF|LHRF preparation|gn-rh|FSH Releasing Hormone|Gonadoliberin|Gonadotropin releasing factor (GRF)|luteinizing hormone releasing hormone|Gonadotropin releasing factor-containing product|Gonadotropin releasing factor|grf|FSHRF preparation|Gonadorelinum|gonadorelinum|FSH/RF|luteinizing hormone-releasing hormone|LH-FSH RH|GnRH|FSH-releasing hormone|GN-RH|gn rh|LH FSH Releasing Hormone|GnRH - Gonadotrophin releasing hormone|LRF|GRF preparation|Gonadoréline|GRH|Hoe- 471|Follicle stimulating hormone releasing factor|gonadotropin-releasing hormone|Gonadotropin releasing factor (substance)|Gonadotropin releasing factor preparation|LH-Releasing Hormone|Luliberin|Follicle stimulating hormone releasing factor (FRF) (FSH/RF)|LFRH|gnrh|Luteinising Hormone-Releasing Factor|LHRH - Luteinising hormone releasing hormone|lhrh|GnRH (gonadotropin releasing hormone)|Releasing Hormone, LHFSH|LH-RF|gonadorelin|LHRH - Luteinizing hormone releasing hormone|LHRF|Luteinizing hormone releasing hormone|Gonadotrophin releasing factor|Luteinizing Hormone-Releasing Hormone|gonadoliberin|Luteinizing hormone releasing factor preparation|GnRH - Gonadotropin releasing hormone|LH-RH|Luteinizing Hormone-Releasing Factor|5-oxoPro-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2 (human or pig)|Gonadotropin-releasing hormone|Gonadotrophin releasing hormone|LHRH|Gn-RH|GRH - Gonadotropin releasing hormone|GONADORELIN|Gonadotropin-Releasing Hormone|Luteinizing Hormone Releasing Hormone|Follicle stimulating hormone releasing factor preparation|gonadotrophin releasing hormone|Luteinising hormone releasing hormone | gonadorelin |
C0031939 | A light-sensitive neuroendocrine organ attached to the roof of the THIRD VENTRICLE of the brain. The pineal gland secretes MELATONIN, other BIOGENIC AMINES and NEUROPEPTIDES. | Corpus Pineale|pineal|Pineal Glands|Epiphysis cerebri|glandula pinealis|PINEAL GLAND|pineal organ|corpus pineale|Pineal gland|PINEAL BODY|epiphysis cerebri|Pineal structure (body structure)|Pineal Body|GLAND, PINEAL|pineal gland|Pineal Gland|Conarium|pineal glands|conarium|Pineal Bodies|pineal body|Glandula pinealis|Pineal body|Corpus pineale|epiphysis|Pineal structure|Gland, Pineal|Epiphysis Cerebri|Pineal | Pineal gland |
C0175723 | device | bands|Band|Band, device (physical object)|Band, device|band | Bands |
C0680022 | One of the persons who compose a social group, especially an individual who has joined and participates in a group organization. | member|Member|members|Member of (attribute)|Member of | member |
C0018595 | Plasma glycoproteins that form a stable complex with hemoglobin to aid the recycling of heme iron. They are encoded in man by a gene on the short arm of chromosome 16. | haptoglobin|haptoglobins|Haptoglobin (substance)|Haptoglobin, NOS|Hp - Haptoglobin|Haptoglobin|Haptoglobins | Haptoglobins |
C0949586 | A species commonly used for molecular biology research and a well known model organism for the vertebrate genome. | Takifugu rubripes|Sphaeroides rubripes|tiger puffer|Tetraodon rubripes|Fugu rubripes|Torafugu | Takifugu rubripes |
C0018595 | Plasma glycoproteins that form a stable complex with hemoglobin to aid the recycling of heme iron. They are encoded in man by a gene on the short arm of chromosome 16. | haptoglobin|haptoglobins|Haptoglobin (substance)|Haptoglobin, NOS|Hp - Haptoglobin|Haptoglobin|Haptoglobins | Haptoglobins |
C0007709 | The clear constricted portion of the chromosome at which the chromatids are joined and by which the chromosome is attached to the spindle during cell division. | Centromeres|Centromere|Centromere (cell structure)|centromeres|centromere | Centromere |
C0019647 | Histone H3 is a core subunit of the eukaryotic nucleosome complex. Histones are basic nuclear proteins responsible for the nucleosome structure of chromatin. Repeating nucleosome units contain two molecules each of Histones H2A, H2B, H3, and H4 that form an octamer complex around which approximately 146 base pairs of DNA is wrapped. Linker Histone H1 interacts with DNA between nucleosome units in mediating chromatin compaction into higher order structures. (NCI) | Histone H3|H3 | Histone H3 |
C0019647 | Histone H3 is a core subunit of the eukaryotic nucleosome complex. Histones are basic nuclear proteins responsible for the nucleosome structure of chromatin. Repeating nucleosome units contain two molecules each of Histones H2A, H2B, H3, and H4 that form an octamer complex around which approximately 146 base pairs of DNA is wrapped. Linker Histone H1 interacts with DNA between nucleosome units in mediating chromatin compaction into higher order structures. (NCI) | Histone H3|H3 | Histone H3 |
C0012934 | Highly repetitive DNA sequences found in HETEROCHROMATIN, mainly near centromeres. They are composed of simple sequences (very short) (see MINISATELLITE REPEATS) repeated in tandem many times to form large blocks of sequence. Additionally, following the accumulation of mutations, these blocks of repeats have been repeated in tandem themselves. The degree of repetition is on the order of 1000 to 10 million at each locus. Loci are few, usually one or two per chromosome. They were called satellites since in density gradients, they often sediment as distinct, satellite bands separate from the bulk of genomic DNA owing to a distinct BASE COMPOSITION. | Satellite DNAs|Satellite DNA|DNAs, Satellite | DNA, Satellite |
C0322859 | null | Aedes aegypti|aedes aegypti|Stegomyia aegypti|Tiger mosquito|tiger mosquito|Aedes aegypti (organism) | Aedes aegypti |
C1514665 | About 8% of human genes have been estimated to carry out transcription from both DNA strands, resulting in significant level of endogenous antisense RNA. In the cytoplasm the antisense RNA leads to formation of long dsRNA, which activates the interferon and RNA-dependent protein kinase antiviral pathway. Most endogenous antisense RNA is made in the nucleus and two responses have been suggested for the nuclear dsRNA. First, the dsRNA may be processed by enzymes of the family of adenosine deaminases that act on RNA (ADAR). The deaminated dsRNAs contain various levels of inosines. dsRNA containing high level of inosines are tightly bound by a protein complex that results in their nuclear retention. dsRNA containing low level of inosines may be able to exit the nucleus. Second, the nuclear dsRNA can lead to gene silencing and heterochromatin formation. (This definition may be outdated - see the DesignNote.) | RNA Interference Pathway|Double Stranded RNA Biosynthesis Pathway|Antisense Pathway|dsRNA Biosynthesis Pathway | RNA Interference Pathway |
C0054755 | Carboxypeptidases that are primarily found the DIGESTIVE SYSTEM that catalyze the release of C-terminal amino acids. Carboxypeptidases A have little or no activity for hydrolysis of C-terminal ASPARTIC ACID; GLUTAMIC ACID; ARGININE; LYSINE; or PROLINE. This enzyme requires ZINC as a cofactor and was formerly listed as EC 3.4.2.1 and EC 3.4.12.2. | Carboxypeptidases A|Carboxypeptidase A (substance)|Carboxypeptidase A|Carboxypolypeptidase | Carboxypeptidase A |
C1336778 | RNA polymerase II transcription of Class II genes involves the TFIID transcription complex comprised of general factors, including TBP, TFIIA, TFIIB, TFIIE, TFIIF, TFIIG/J, and TFIIH, as well as gene-specific factors that include TAFs, which interact with regulatory protein activation domains to enhance transcription. A second group of cofactors includes PC1, PC2, and PC3, which have a strong positive influence on transcription. A third group of factors suppress transcription. The combined action of general and gene-specific regulators encoded by transcription coactivator genes determines appropriate gene expression. (NCI) | Transcription Coactivator/Corepressor Gene|Transcriptional Coregulator Gene | Transcription Coregulator Gene |
C1336778 | RNA polymerase II transcription of Class II genes involves the TFIID transcription complex comprised of general factors, including TBP, TFIIA, TFIIB, TFIIE, TFIIF, TFIIG/J, and TFIIH, as well as gene-specific factors that include TAFs, which interact with regulatory protein activation domains to enhance transcription. A second group of cofactors includes PC1, PC2, and PC3, which have a strong positive influence on transcription. A third group of factors suppress transcription. The combined action of general and gene-specific regulators encoded by transcription coactivator genes determines appropriate gene expression. (NCI) | Transcription Coactivator/Corepressor Gene|Transcriptional Coregulator Gene | Transcription Coregulator Gene |
C1510885 | Loss of the balance between stimulation and inhibition of new blood vessel growth. A required early step in cancer growth and metastasis. | null | Angiogenic Switch |
C0207071 | A neurotrophic factor that promotes the survival of various neuronal cell types and may play an important role in the injury response in the nervous system. | Ciliary neurotrophic factor|CNTF|ciliary neurotrophic factor|Ciliary Neuronotrophic Factor|cntf|Factor, Ciliary Neuronotrophic|Neurotrophic Factor, Ciliary|ciliary neurotrophic factor (CNTF)|Ciliary Neurotrophic Factor|CNTF (ciliary neurotrophic factor)|Factor, Ciliary Neurotrophic|Neuronotrophic Factor, Ciliary | Ciliary Neurotrophic Factor |
C0207071 | A neurotrophic factor that promotes the survival of various neuronal cell types and may play an important role in the injury response in the nervous system. | Ciliary neurotrophic factor|CNTF|ciliary neurotrophic factor|Ciliary Neuronotrophic Factor|cntf|Factor, Ciliary Neuronotrophic|Neurotrophic Factor, Ciliary|ciliary neurotrophic factor (CNTF)|Ciliary Neurotrophic Factor|CNTF (ciliary neurotrophic factor)|Factor, Ciliary Neurotrophic|Neuronotrophic Factor, Ciliary | Ciliary Neurotrophic Factor |
C0381325 | null | PBFI-AM | potassium-binding benzofuran-isophthalate acetoxymethyl ester |
C0381325 | null | PBFI-AM | potassium-binding benzofuran-isophthalate acetoxymethyl ester |
C0022947 | Cyclic esters of hydroxy carboxylic acids, containing a 1-oxacycloalkan-2-one structure. Large cyclic lactones of over a dozen atoms are MACROLIDES. | lactones|Lactone (substance)|Lactones|lactone|Lactone Compound|Lactone|LACTONE | Lactones |
C0907808 | null | null | hypothemycin |
C0010654 | A thiol-containing non-essential amino acid that is oxidized to form CYSTINE. | Cysteine-containing product|L Cysteine|Cysteine (substance)|Cysteine|CYSTEINE|L-Cys|cysteines|L-Cysteine|Product containing cysteine (medicinal product)|(R)-2-Amino-3-sulfanyl-propanoic acid|L-CYSTEINE|Cys|Half Cystine|Free Cysteine|Cisteinum|(2R)-2-amino-3-mercaptopropanoic acid|L-Cystein|(R)-2-Amino-3-mercaptopropanoic acid|L-Zystein|Cysteinum|(2R)-2-amino-3-sulfanylpropanoic acid|l cysteine|Cisteina|l-cysteine|cysteine|cysteine l|cys|L-2-Amino-3-mercaptopropionic acid|Half-Cystine|L-cysteine | cysteine |
C1171350 | null | Kinase Inhibitor|Kinase Inhibitor [EPC] | kinase inhibitor [EPC] |
C0034825 | Glycoprotein molecules on the surface of B- and T-lymphocytes, that react with molecules of antilymphocyte sera, lectins, and other agents which induce blast transformation of lymphocytes. | mitogen receptors|Mitogen receptor (substance)|Mitogen Receptor|Receptor, Mitogen|Mitogen receptor site|Mitogen Receptors|Mitogen receptor | Receptors, Mitogen |
C0929110 | null | Anterior lacrimal crest of maxilla|Anterior lacrimal crest|Crista lacrimalis anterior|Crista lacrimalis anterior maxillae | Anterior lacrimal crest of maxilla |
C0929110 | null | Anterior lacrimal crest of maxilla|Anterior lacrimal crest|Crista lacrimalis anterior|Crista lacrimalis anterior maxillae | Anterior lacrimal crest of maxilla |
C0285890 | Alpha-synuclein (140 aa, ~14 kDa) is encoded by the human SNCA gene. This protein plays a role in the modulation of presynaptic vesicle transport and release. | alpha Synuclein|alpha synuclein|Alpha-synuclein (substance)|Non-A4 Component of Amyloid Precursor|Non-A Beta Component of AD Amyloid|Non-AB Component of AD Amyloid Protein|Alpha-synuclein|Alpha-Synuclein|alpha-synuclein|NACP|SNCA|alpha-Synuclein|Non AB Component of AD Amyloid Protein | alpha-Synuclein |
C0808232 | null | therapy intervention|intervention therapy|therapeutic intervention|interventions therapy|intervention therapeutic|therapeutic interventions | Therapeutic Intervention |
C0242391 | null | Proteins, Cell Membrane|Membrane protein of cell | Cell Membrane Proteins |
C0025979 | The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes. [GOC:jl, ISBN:0395825172, ISBN:0815316194] | Actin Filament|myofilaments|Microfilaments, Actin|Filament, Actin|striated muscle filament|Actin Filaments|microfilaments|Actin cytoskeleton|Filaments, Actin|Microfilament|Filaments of contractile apparatus, NOS|Cytoskeleton, Actin|Microfilament, Actin|Actin filament|Actin Cytoskeletons|Cytoskeletons, Actin|Actin Cytoskeleton|actin filament|Microfilamentum|Filaments of contractile apparatus (cell structure)|microfilament|Actin Microfilaments|Filaments of contractile apparatus|Microfilaments|Actin Microfilament|myofilament|actin cytoskeleton|actin filaments|Myofilaments | Microfilaments |
C1167072 | The outer, i.e. cytoplasm-facing, lipid bilayer of the nuclear envelope; continuous with the endoplasmic reticulum of the cell and sometimes studded with ribosomes. [ISBN:0198547684] | Nuclear Outer Membrane|Membrana nuclearis externa|perinuclear membrane|Outer Nuclear Membrane|Nuclear outer membrane|Outer lipid bilayer of nucleus|nuclear outer membrane|Outer nuclear membrane | Outer nuclear membrane |
C1167428 | An enzyme complex which in eukaryotes is composed of four different chains: alpha, beta, gamma, and delta. The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 8 to 12 subunits. Catalyzes the phosphorylation of proteins to O-phosphoproteins. [EC:2.7.11.17] | calcium/calmodulin-dependent protein kinase complex|calcium- and calmodulin-dependent protein kinase complex location|CAMK2|calcium/calmodulin-dependent protein kinase complex location|calcium- and calmodulin-dependent protein kinase complex | calcium/calmodulin-dependent protein kinase complex location |
C1285654 | null | Ability to remember|Memory performance (observable entity) | Memory performance |
C0012010 | A benzodiazepine with anticonvulsant, anxiolytic, sedative, muscle relaxant, and amnesic properties and a long duration of action. Its actions are mediated by enhancement of GAMMA-AMINOBUTYRIC ACID activity. | diazepam|7-chloro-1,3-dihydro-1-methyl-5-phenyl-2H-1,4-benzodiazepin-2-one|Product containing diazepam (medicinal product)|DIAZEPAM|Diazepam|7-Chloro-1,3-dihydro-1-methyl-5-phenyl-2H-1,4-benzodiazepin-2-one|Methyl diazepinone|2H-1,4-Benzodiazepin-2-one, 7-chloro-1,3-dihydro-1-methyl-5-phenyl-|Diazepam (substance)|Diazepam-containing product | diazepam |
C0219102 | null | 4H-Imidazo(1,5-a)(1,4)benzodiazepine-3-carboxamide, 6-(2-bromophenyl)-8-fluoro-|6-(2-bromophenyl)-8-fluoro-4-H-imidazo(1,5-a)(1-4)benzodiazepine-3-carboxamide | imidazenil |
C0036557 | null | sedatives|Sedatives|sedative|Sedative (substance)|Sedative agent, NOS|Sedative agent|Sedative|Medicinal product acting as sedative (product) | Sedatives |
C0219102 | null | 4H-Imidazo(1,5-a)(1,4)benzodiazepine-3-carboxamide, 6-(2-bromophenyl)-8-fluoro-|6-(2-bromophenyl)-8-fluoro-4-H-imidazo(1,5-a)(1-4)benzodiazepine-3-carboxamide | imidazenil |
C0450429 | A position, site, or point in space where something can be found. | Location (attribute)|location|LOC|locations|Location | Location |
C0917729 | null | Receptors, Ryanodine | Ryanodine Receptors |
C1140999 | null | Contraction, NOS|contractions|contraction|Contraction (finding)|Contraction|Contracted | Contraction (finding) |
C0026609 | Neurons which activate MUSCLE CELLS. | Motor Neurons|Neurons, Motor|motoneurons|motor cell|Motor neurons|Motoneuron|motoneuron|motor neurons|Neuron, Motor|Motor neuron|Motor neuron (cell)|motor neuron|Motoneurons|Motor Neuron | Motor Neurons |
C0013139 | A species of fruit fly frequently used in genetics because of the large size of its chromosomes. | melanogaster, Drosophila|Drosophila melanogaster|drosophila melanogaster|Drosophila melanogasters|Sophophora melanogaster|D. melanogaster | Drosophila melanogaster |
C1570721 | null | nitrolinoleic acid | 10-nitro-9,12-octadecadienoic acid |
C0018988 | Chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N(21),N(22),N(23),N(24)) ferrate(2-) dihydrogen. | Ferriprotoporphyrin IX Chloride|Hemin-containing product|chloro(protoporphyrinato)iron(III)|hemin|Hemin|Hemina|Haemin|Product containing hemin (medicinal product)|Chloride, Ferriprotoporphyrin IX|Hämin|HEMIN|hémine|protohemin|Protohemin|Chlorohemin|Chloride, Ferriheme|Protohemin IX|Ferrate(2-), chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N21,N22,N23,N24)-, dihydrogen, (SP-5-13)-|Haemin-containing product|Ferriheme Chloride|Hemin (substance) | hemin |
C0506947 | Any portion of the aorta including the ascending and descending aorta, and aortic arch or a portion of the aortic orifice of the left ventricle. | Aortic Segment|Aortic segment|Segment of aorta | Segment of aorta |
C0538674 | Heme oxygenase 1 (288 aa, ~33 kDa) is encoded by the human HMOX1 gene. This protein is involved in heme metabolism. | Heme Oxygenase-1|Heme Oxygenase (Decyclizing)|Heme Oxygenase 1|Hemeoxygenase 1|HO1|Oxygenase-1, Heme|HMOX1|EC 1.14.99.3 | Heme Oxygenase-1 |
C0010934 | A compound composed of a two CYCLIC PEPTIDES attached to a phenoxazine that is derived from STREPTOMYCES parvullus. It binds to DNA and inhibits RNA synthesis (transcription), with chain elongation more sensitive than initiation, termination, or release. As a result of impaired mRNA production, protein synthesis also declines after dactinomycin therapy. (From AMA Drug Evaluations Annual, 1993, p2015) | Actinomycin X 1|Meractinomycin|actinomycin IV|2-bis[cyclo(N-methyl-L-valyl-sarcosyl-L-prolyl-D-valyl-L-threonyl)]-1,9 dimethyl-4,6 3H-phenoxazinone-3|Dactinomycin|Actinomycin-[thr-val-pro-sar-meval]|actinomycin d|Dactinomycine|Dactinomycin-containing product|DACTINOMYCIN|Dactinomycin (substance)|ActD|meractinomycin|Dactinomycinum|ACT-D|actinomycin-[thr-val-pro-sar-meval]|actinomycin-C1|2-amino-N,N'-bis(hexadecahydro-2,5,9-trimethyl-6,13-bis(1-methylethyl)-1,4,7,11,14-pentaoxo-1H-pyrrolo(2,1-i)(1,4,7,10,13)oxatetra-azacyclohexadecin-10-yl)-4,6-dimethyl-3-oxo-3H-phenoxazine-1,9-dicarboxamide|Actinomycin IV|actinomycin-d|Actinomycin C1|actinomycin X 1|DACTINomycin|Product containing dactinomycin (medicinal product)|ACTINOMYCIN D|DACT|actinomycin C1|Actinomycin D|actinomycin-D|2-bis[Cyclo(N-methyl-L-valyl-sarcosyl-L-prolyl-D-valyl-L-threonyl)]-1,9 dimethyl-4,6 3H-phenoxazinone-3|actinomycin I1|dactinomycine|Actinomycin A IV|AD|Actinomycin I1|Dactinomicina|actinomycin D|dactinomycin | dactinomycin |
C0166417 | A nuclear transcription factor. Heterodimerization with RETINOID X RECEPTOR ALPHA is important in regulation of GLUCOSE metabolism and CELL GROWTH PROCESSES. It is a target of THIAZOLIDINEDIONES for control of DIABETES MELLITUS. | Peroxisome Proliferator Activated Receptor gamma|Thiazolidinedione Receptor|PPARgamma|PPAR gamma|Receptor, Thiazolidinedione|Peroxisome Proliferator-Activated Receptor gamma | PPAR gamma |
C0221464 | null | Arterial (qualifier value)|Arterial|arterial | Arterial |
C0597639 | null | null | vasoactive agent |
C0205715 | Distinct stack of lamellae seen within chloroplasts. Grana contain the pigments, electron transfer compounds, and enzymes essential to the light-dependent reactions of photosynthesis. [ISBN:0140514031] | granum | Grana |
C1280211 | null | Entire intervertebral disc|Entire intervertebral disc (body structure) | Entire intervertebral disc |
C0004015 | One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter. | l aspartic acid|Asp|(S)-2-aminobutanedioic acid|aspartic acid|2-Aminosuccinic acid|L-Aspartic acid|acid aspartic|L-aspartic acid|ASPARTIC ACID|Aspartic Acid|L Aspartic Acid|(S)-Aminobutanedioic acid|ácido aspártico|Aspartic acid|acids aspartic|L-Aspartic Acid|(S)-2-aminosuccinic acid|Acidum asparticum|Aspartic acid (substance)|l-aspartic acid|L-Asparaginsäure|L-Asp|D | aspartic acid |
C0995550 | null | null | Anabaena sp. |
C0035499 | A purplish-red, light-sensitive pigment found in RETINAL ROD CELLS of most vertebrates. It is a complex consisting of a molecule of ROD OPSIN and a molecule of 11-cis retinal (RETINALDEHYDE). Rhodopsin exhibits peak absorption wavelength at about 500 nm. | Rhodopsins|Rhodopsin|Visual Purple|rhodopsin|visual purple|Visual purple|Rhodopsin (substance) | Rhodopsin |
C0004654 | Rhodopsins found in the PURPLE MEMBRANE of halophilic archaea such as HALOBACTERIUM HALOBIUM. Bacteriorhodopsins function as an energy transducers, converting light energy into electrochemical energy via PROTON PUMPS. | Bacteriorhodopsin|bacteriorhodopsin|Bacteriorhodopsins|Bacteriorhodopsin (substance) | Bacteriorhodopsins |
C1333198 | Protein within the interior of the cell; excludes membrane, mitochondrial, and nuclear proteins. | null | Cytoplasmic Protein |
C0370220 | A preparation consisting of PLATELETS concentrated in a limited volume of PLASMA. This is used in various surgical tissue regeneration procedures where the GROWTH FACTORS in the platelets enhance wound healing and regeneration. | plasma platelet rich|Platelet-rich Plasma|plasma platelets rich|Platelet rich plasma (substance)|Platelet Rich Plasma|PLATELET RICH PLASMA|Platelet rich plasma|plasma rich platelet|Plasma, Platelet-Rich|platelet rich plasma|Platelet-Rich Plasma|PRP | Platelet rich plasma |
C0085262 | A CELL LINE derived from a PHEOCHROMOCYTOMA of the rat ADRENAL MEDULLA. PC12 cells stop dividing and undergo terminal differentiation when treated with NERVE GROWTH FACTOR, making the line a useful model system for NERVE CELL differentiation. | pheochromocytoma 12 cell line|PC12 cell|Cell Lines, Pheochromocytoma|Pheochromocytoma 12 Cell Line|Pheochromocytoma Cell Line|Pheochromocytoma Cell Lines|PC-12|PC12 Cells|Cell Line, Pheochromocytoma|PC12 Cell|pc12 cell|pc12 cells | PC12 Cells |
C0390690 | null | H-cadherin|heart-cadherin|T-cad protein|cadherin 13|T cadherin|truncated-cadherin|T-cadherin | H-Cadherin |
C0390690 | null | H-cadherin|heart-cadherin|T-cad protein|cadherin 13|T cadherin|truncated-cadherin|T-cadherin | H-Cadherin |
C0770114 | null | DNA methyltransferase 3B | DNA Methyltransferase 3B |
C0000546 | A 20-carbon unsaturated fatty acid containing 4 alkyne bonds. It inhibits the enzymatic conversion of arachidonic acid to prostaglandins E(2) and F(2a). | ETYA|5,8,11,14 Eicosatetraynoic Acid|5,8,11,14-Eicosatetraynoic acid | 5,8,11,14-Eicosatetraynoic Acid |
C0206428 | Photosensitive afferent neurons located primarily within the FOVEA CENTRALIS of the MACULA LUTEA. There are three major types of cone cells (red, blue, and green) whose photopigments have different spectral sensitivity curves. Retinal cone cells operate in daylight vision (at photopic intensities) providing color recognition and central visual acuity. | Photoreceptor, Retinal Cone|eye cones|Retinal Cone Photoreceptor Cells|Cone Photoreceptor|Photoreceptor, Cone|Cone Photoreceptor, Retinal|Photoreceptors, Retinal Cone|cones|Retinal Cone Photoreceptor|Retinal Cone Cell|Cones, Retinal|Cone Photoreceptor Cell|Cone Photoreceptors, Retinal|Cone, Retinal|Photoreceptors, Cone|Cones|eye cone|Cones (Retina)|Cone Photoreceptor Cells|Cone Cells, Retinal|Retinal Cone Cells|Cone Cell, Retinal|cones eye|Cone cell|Cone cell of retina|Retina, cone|cells cone|Retinal Cone Photoreceptors|Cone|cone cell|Cell, Retinal Cone|Cells, Retinal Cone|Cell, Cone Photoreceptor|cones retinal|Photoreceptor Cells, Cone|Cone Photoreceptors|Cone Cell|Retinal cone cell|Cells, Cone Photoreceptor|Retinal Cone|Cone of retina (cell structure)|cones retina|Photoreceptor Cell, Cone|Cone of retina|Retinal Cones|retinal cone|Cone (Retina) | Retinal Cone |
C0001388 | An enzyme that forms CMP-acylneuraminic acids, which donate the N-acylneuraminic acid residues to the terminal sugar residue of a ganglioside or glycoprotein. EC 2.7.7.43. | Synthetase, CMP-N-Acetylneuraminic Acid|Cytidylyltransferase, N-Acylneuraminate|CMPsialate pyrophosphorylase|CMP Sialate Synthase|Pyrophosphorylase, CMP Sialate|CMP-Sialic Acid Synthetase|Cytidylyltransferase, Acylneuraminate|Cytidine 5 Monophosphosialate Synthase|Sialate Synthase, CMP|N Acylneuraminate Cytidylyltransferase|Acylneuraminate cytidylyltransferase (substance)|Acylneuraminate cytidylyltransferase|Cytidine 5-Monophosphosialate Synthase|CTP:N-acylneuraminate cytidylyltransferase|Cytidine 5'-Monophosphosialic Acid Synthetase|CMP N Acetylneuraminic Acid Synthetase|Synthetase, CMP-Sialic Acid|CMP Sialic Acid Synthetase|Sialate Pyrophosphorylase, CMP|CMP Sialate Pyrophosphorylase|CMP-N-Acetylneuraminic Acid Synthetase|Synthase, Cytidine 5-Monophosphosialate|CMPsialate synthase|Cytidine 5' Monophosphosialic Acid Synthetase|Synthase, CMP Sialate|N-Acylneuraminate Cytidylyltransferase|Acylneuraminate Cytidylyltransferase | Acylneuraminate Cytidylyltransferase |
C1456459 | The assembly of DNA, histone proteins, other associated proteins, and sometimes RNA, into chromatin structure, beginning with the formation of the basic unit, the nucleosome, followed by organization of the nucleosomes into higher order structures, ultimately giving rise to a complex organization of specific domains within the nucleus. [http://www.infobiogen.fr/services/chromcancer/IntroItems/ChromatinEducEng.html, PMID:20404130] | Chromatin Modeling|Chromatin Assembly|chromatin assembly|establishment of chromatin architecture | Chromatin Modeling |
C0243041 | A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures. | Molecular Chaperone|Chaperone|molecular chaperone|Molecular chaperones|Chaperone, Molecular|Chaperones, Molecular | Molecular Chaperones |
C1156189 | The aggregation, arrangement and bonding together of a nucleosome, the beadlike structural units of eukaryotic chromatin composed of histones and DNA. [GOC:mah] | nucleosome modeling | nucleosome assembly |
C0287990 | Furin (794 aa, ~87 kDa) is encoded by the human FURIN gene. This protein is involved in endopeptidase activity and the secretory pathway. | furin|EC 3.4.21.75|Paired basic amino acid residue cleaving enzyme|Dibasic processing enzyme|Dibasic-Processing Enzyme|Processing Enzyme, Dibasic|Paired Basic Amino Acid Residue-Cleaving Enzyme|PACE Protein|Furin (substance)|SPC1 Proteinase|Furin|Furin Preproprotein|Furin Protein|FURIN|Paired Basic Amino Acid Cleaving Enzyme|Dibasic Processing Enzyme|PACE | paired basic amino acid cleaving enzyme |
C0887838 | The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination. [GOC:vw, ISBN:0815316194] | trans-Golgi network|trans Golgi Network|trans Golgi network|Trans Golgi network|Golgi trans face|Network, trans-Golgi|TGN|Trans-Golgi Network|trans-Golgi Network|Golgi trans-face|Trans face Golgi network | trans-Golgi Network |
C1328825 | null | null | ADAMTS |
C0042172 | null | E Cadherin|E-Cadherin|E-cadherin|e cadherin|Cadherin-1|Cadherin 1|Epithelial-Cadherins|Epithelial Cadherins|e-cadherin|E-Cadherins|E cadherin|E Cadherins|Uvomorulin | E-Cadherin |
C0016790 | Enzymes catalyzing the transfer of fucose from a nucleoside diphosphate fucose to an acceptor molecule which is frequently another carbohydrate, a glycoprotein, or a glycolipid molecule. Elevated activity of some fucosyltransferases in human serum may serve as an indicator of malignancy. The class includes EC 2.4.1.65; EC 2.4.1.68; EC 2.4.1.69; EC 2.4.1.89. | Alpha-Fucosyltransferases|fucosyltransferase|Fucosyltransferase|Fucosyltransferases | Fucosyltransferase |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.