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Nur77
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 exon ... [...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 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 fami ... (), and * Nuclear receptor 4A3 (). References Intracellular receptors Transcription factors {{receptor-stub ... [...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. Four transcript variants encoding four distinct isoforms have been identified for this gene. Additional alternate splice variants may exist, but their full-length nature has not been determined. This protein is thought to be critical to development of the dopaminergic phenotype in the midbrain, as mice without NR4A2 are lacking expression of this phenotype. This is further confirmed by studies showi ... [...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 residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metabolic reactions, DNA replication, Cell signaling, responding to stimuli, providing Cytoskeleton, structure to cells and Fibrous protein, organisms, and Intracellular transport, transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the Nucleic acid sequence, nucleotide sequence of their genes, and which usually results in protein folding into a specific Protein structure, 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 pep ... [...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. A Founding Council was elected at the meeting with a total of 42 scientists from 17 different countries, with Victor A. McKusick serving as founding President. In 2016, HUGO was located at the EWHA Womans University in Seoul, South Korea. In 2020, the ... [...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 example ... [...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 site ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Retinoid
The retinoids are a class of chemical compounds that are natural derivatives of vitamin A or are chemically related to it. Synthetic retinoids are utilized in cosmetic formulations, clinical dermatology, and the treatment of some forms of cancer. Retinoids have many important functions throughout the body, including in vision, regulation of skin proliferation and differentiation, growth of bone tissue, immune function, and male fertility. The biology of retinoids is complex, having well-documented effectiveness in the management of conditions ranging from acute promyelocytic leukemia to acne to photoaging. On the other hand, retinoids may be involved in metabolic dysfunction and, at least in some forms, carcinogenesis. Types Retinoids are divided into four generations based on their molecular structure and receptor selectivity. Structure The basic structure of the hydrophobic retinoid molecule consists of a cyclic end group, a polyene side chain and a polar end group. Th ... [...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 may be an endogenous mammalian RXR-selective agonist. Bexarotene is the only specific activator of the RXRs which does not activate the Retinoic Acid Receptors. There are three retinoic X receptors (RXR): RXR-alpha, RXR-beta, and RXR-gamma, encoded by the , , genes, respectively. RXR heterodimerizes with multiple nuclear receptors including CAR, FXR, LXR, PPAR, PXR, RAR, TR, ER and VDR. RXRs are permissive co-receptors as only one of six alleles is needed for normal development and health. Given this, it is difficult to extrapolate whether the RXR pathway has its own endogenous activity driven by 9-cis retinoic acid species or whether it merely participates in other pathways, predominantly the retinoic nuclear receptor pathway. Genomic knockout of th ... [...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 or multimer 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 while 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 hetero ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Response Element
''Response elements'' are short sequences of DNA within a gene promoter or enhancer region that are able to bind specific transcription factors and regulate transcription of genes. Under conditions of stress, a transcription activator protein binds to the response element and stimulates transcription. If the same response element sequence is located in the control regions of different genes, then these genes will be activated by the same stimuli, thus producing a coordinated response. Hormone response element A hormone response element (HRE) is a short sequence of DNA within the promoter of a gene, that is able to bind to a specific hormone receptor complex and therefore regulate transcription. The sequence is most commonly a pair of inverted repeats separated by three nucleotides, which also indicates that the receptor binds as a dimer. Specifically, HRE responds to steroid hormones, as the activated steroid receptor is the transcription factor binding HRE. This regulates th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
