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NR4A1
The nuclear receptor 4A1 (NR4A1 for "nuclear receptor subfamily 4 group A member 1") also known as Nur77, TR3, and NGFI-B is a protein that in humans is encoded by the ''NR4A1'' gene. Nuclear receptor 4A1 (NR4A1) is a member of the '' NR4A'' nuclear receptor family of intracellular transcription factors. NR4A1 is involved in cell cycle mediation, inflammation and apoptosis. Nuclear receptor 4A1 plays a key role in mediating inflammatory responses in macrophages. In addition, subcellular localization of the NR4A1 protein appears to play a key role in the survival and death of cells. Expression is inducible by phytohemagglutinin in human lymphocytes and by serum stimulation of arrested fibroblasts. Translocation of the protein from the nucleus to mitochondria induces apoptosis. Multiple alternatively spliced variants, encoding the same protein, have been identified. Structure The ''NR4A1'' gene contains seven exons. An amino terminal transactivation domain is encoded in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nuclear Receptor
In the field of molecular biology, nuclear receptors are a class of proteins responsible for sensing steroids, thyroid hormones, vitamins, and certain other molecules. These receptors work with other proteins to regulate the expression of specific genes thereby controlling the development, homeostasis, and metabolism of the organism. Nuclear receptors bind directly to DNA regulating the expression of adjacent genes; hence these receptors are classified as transcription factors. The regulation of gene expression by nuclear receptors often occurs in the presence of a ligand—a molecule that affects the receptor's behavior. Ligand binding to a nuclear receptor results in a conformational change activating the receptor. The result is up- or down-regulation of gene expression. A unique property of nuclear receptors that differentiates them from other classes of receptors is their direct control of genomic DNA. Nuclear receptors play key roles in both embryonic deve ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Celastrol
Celastrol (tripterine) is a chemical compound isolated from the root extracts of '' Tripterygium wilfordii'' (Thunder god vine) and ''Tripterygium regelii'' (Regel's threewingnut). Celastrol is a pentacyclic nortriterpen quinone and belongs to the family of quinone methides. In mice, celastrol is an NR4A1 agonist that alleviates inflammation and induces autophagy. Also in mice, celastrol increase expression of IL1R1, which is the receptor for the cytokine interleukin-1 (IL-1). IL1R1 knock-out mice exposed to celastrol exhibit no leptin-sensitizing or anti-obesity effect. In ''in vitro'' and ''in vivo'' animal experiments, celastrol exhibits antibacterial, antioxidant, anti-inflammatory, anticancer, and insecticidal activities. It has been shown to have obesity-controlling effects in mice by inhibiting negative regulators of leptin. Celastrol has also shown to possess (by inhibition of NF-κB in the hypothalamus) anti-diabetic effects on diabetic nephropathy and improve who ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
NR4A
NR4A (nuclear receptor subfamily 4A) is a family of orphan nuclear receptors which act as transcription factors in neuron development and maintenance. In 2006, it was shown that members of the NR4A family were implicated in the control of skeletal muscle metabolism. Three members have been identified in humans: * Nuclear receptor 4A1 (), * Nuclear receptor 4A2 (), and * Nuclear receptor 4A3 The nuclear receptor 4A3 (NR4A3) (nuclear receptor subfamily 4, group A, member 3) also known as neuron-derived orphan receptor 1 (NOR1) is a protein that in humans is encoded by the ''NR4A3'' gene. NR4A3 is a member of the nuclear receptor famil ... (). References Intracellular receptors Transcription factors {{receptor-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid resid ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nuclear Receptor 4A2
The nuclear receptor 4A2 (NR4A2) (nuclear receptor subfamily 4 group A member 2) also known as nuclear receptor related 1 protein (NURR1) is a protein that in humans is encoded by the ''NR4A2'' gene. NR4A2 is a member of the nuclear receptor family of intracellular transcription factors. NR4A2 plays a key role in the maintenance of the dopaminergic system of the brain. Mutations in this gene have been associated with disorders related to dopaminergic dysfunction, including Parkinson's disease and schizophrenia. Misregulation of this gene may be associated with rheumatoid arthritis Rheumatoid arthritis (RA) is a long-term autoimmune disorder that primarily affects synovial joint, joints. It typically results in warm, swollen, and painful joints. Pain and stiffness often worsen following rest. Most commonly, the wrist and .... Four transcript variants encoding four distinct isoforms have been identified for this gene. Additional alternate splice variants may exist, but their f ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Human Genome Organisation
The Human Genome Organisation (HUGO) is a non-profit organization founded in 1988. HUGO represents an international coordinating scientific body in response to initiatives such as the Human Genome Project. HUGO has four active committees, including the HUGO Gene Nomenclature Committee (HGNC), and the HUGO Committee on Ethics, Law and Society (CELS). History HUGO was established at the first meeting on genome mapping and sequencing at Cold Spring Harbor in 1988. The idea of starting the organization stemmed from South African biologist Sydney Brenner, who is best known for his significant contributions to work on the genetic code and other areas of molecular biology, as well as winning the 2002 Nobel Prize in Physiology or Medicine The Nobel Prize in Physiology or Medicine ( sv, Nobelpriset i fysiologi eller medicin) is awarded yearly by the Nobel Assembly at the Karolinska Institute, Nobel Assembly at the Karolinska Institute for outstanding discoveries in physiology or .... ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sequence Motif
In biology, a sequence motif is a nucleotide or amino-acid sequence pattern that is widespread and usually assumed to be related to biological function of the macromolecule. For example, an ''N''-glycosylation site motif can be defined as ''Asn, followed by anything but Pro, followed by either Ser or Thr, followed by anything but Pro residue''. Overview When a sequence motif appears in the exon of a gene, it may encode the "structural motif" of a protein; that is a stereotypical element of the overall structure of the protein. Nevertheless, motifs need not be associated with a distinctive secondary structure. " Noncoding" sequences are not translated into proteins, and nucleic acids with such motifs need not deviate from the typical shape (e.g. the "B-form" DNA double helix). Outside of gene exons, there exist regulatory sequence motifs and motifs within the " junk", such as satellite DNA. Some of these are believed to affect the shape of nucleic acids (see for exampl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Binding Site
In biochemistry and molecular biology, a binding site is a region on a macromolecule such as a protein that binds to another molecule with specificity. The binding partner of the macromolecule is often referred to as a ligand. Ligands may include other proteins (resulting in a protein-protein interaction), enzyme substrates, second messengers, hormones, or allosteric modulators. The binding event is often, but not always, accompanied by a conformational change that alters the protein's function. Binding to protein binding sites is most often reversible (transient and non-covalent), but can also be covalent reversible or irreversible. Function Binding of a ligand to a binding site on protein often triggers a change in conformation in the protein and results in altered cellular function. Hence binding site on protein are critical parts of signal transduction pathways. Types of ligands include neurotransmitters, toxins, neuropeptides, and steroid hormones. Binding sit ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Retinoid
The retinoids are a class of chemical compounds that are vitamers of vitamin A or are chemically related to it. Retinoids have found use in medicine where they regulate epithelial cell growth. Retinoids have many important functions throughout the body including roles in vision, regulation of cell proliferation and differentiation, growth of bone tissue, immune function, and activation of tumor suppressor genes. Research is also being done into their ability to treat skin cancers. Currently, alitretinoin (9-''cis''-retinoic acid) may be used topically to help treat skin lesions from Kaposi's sarcoma, and tretinoin (all-''trans''- retinoic acid) is used to treat acute promyelocytic leukemia. Types There are four generations of retinoids: * First generation include retinol, retinal, tretinoin (retinoic acid), isotretinoin, and alitretinoin * Second generation include etretinate and its metabolite acitretin * Third generation include adapalene, bexarotene, and tazarote ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Retinoid X Receptor
The retinoid X receptor (RXR) is a type of nuclear receptor that is activated by 9-cis retinoic acid, which is discussed controversially to be of endogenous relevance, and 9-''cis''-13,14-dihydroretinoic acid, which is likely to be the major endogenous mammalian RXR-selective agonist. In a novel review publication, this 9-''cis''-13,14-dihydroretinoic acid was shown to be a metabolite not originating from the known vitamin A (vitamin A1) pathway and its nutritional precursors all-''trans''- retinol ( vitamin A (vitamin A1) or all-''trans''- beta-carotene ( provitamin A (provitamin A1)). An independent pathway for generating this endogenous RXR-ligand 9-''cis''-13,14-dihydroretinoic acid from 9-''cis''-13,14-dihydroretinol present in food source and named vitamin A5 or alternatively via provitamin A5 has been suggested as the first novel vitamin identified since 1948, cobalamin / vitamin B12. There are three retinoic X receptors (RXR): RXR-alpha, RXR-beta, and RXR-gamma, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
COUP-TF
The chicken ovalbumin upstream promoter transcription factor (COUP-TFs) proteins are members of the nuclear receptor family of intracellular transcription factors. There are two variants of the COUP-TFs, labeled as COUP-TFI and COUP-TFII COUP-TFII (COUP transcription factor 2), also known as NR2F2 (nuclear receptor subfamily 2, group F, member 2) is a protein that in humans is encoded by the ''NR2F2'' gene. The COUP acronym stands for chicken ovalbumin upstream promoter. Functio ... encoded by the and genes respectively. COUP-TFs play critical roles in the development of organisms. References External links * * * Intracellular receptors Transcription factors {{gene-15-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heterodimer
In biochemistry, a protein dimer is a macromolecular complex formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word ''dimer'' has roots meaning "two parts", ''di-'' + '' -mer''. A protein dimer is a type of protein quaternary structure. A protein homodimer is formed by two identical proteins. A protein heterodimer is formed by two different proteins. Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains. An exception is dimers that are linked by disulfide bridges such as the homodimeric protein NEMO. Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity. The G protein-coupled cannabinoid receptors have the ability to form both homo- and heterodimers with sever ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
