Neuropeptide FF Receptor
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Neuropeptide FF Receptor
The neuropeptide FF receptors are members of the G-protein coupled receptor superfamily of integral membrane proteins which bind the pain modulatory neuropeptides AF and FF. The Neuropeptide FF receptor family is a member of the G protein-coupled receptor superfamily containing two subtypes, NPFF1 and NPFF2, which exhibit a high affinity for Neuropeptide FF (NPFF) peptides. NPFF1 is broadly distributed in the central nervous system with the highest levels found in the limbic system and the hypothalamus. NPFF2 is present in high density, particularly in mammals in the superficial layers of the spinal cord where it is involved in nociception and modulation of opioid functions. These receptors participate to the modulation of opioid receptor function in the brain and spinal cord, and can either reduce or increase opioid receptor function depending which tissue they are released in, reflecting a complex role for neuropeptide FF in pain responses. NPFF receptors are coupled to G prote ...
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Neuropeptide FF Receptor 1
Neuropeptide FF receptor 1, also known as NPFF1 is a human protein, encoded by the NPFFR1 gene In biology, the word gene (from , ; "... Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a b .... See also * Neuropeptide FF receptor References Further reading * * External links * {{G protein-coupled receptors G protein-coupled receptors ...
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Neuropeptide FF Receptor 2
Neuropeptide FF receptor 2, also known as NPFF2 is a human protein encoded by the NPFFR2 gene. See also * Neuropeptide FF receptor The neuropeptide FF receptors are members of the G-protein coupled receptor superfamily of integral membrane proteins which bind the pain modulatory neuropeptides AF and FF. The Neuropeptide FF receptor family is a member of the G protein-coupled ... References Further reading * * * * * * * * * * * External links * G protein-coupled receptors {{transmembranereceptor-stub ...
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G-protein Coupled Receptor
G protein-coupled receptors (GPCRs), also known as seven-(pass)-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptors, and G protein-linked receptors (GPLR), form a large group of protein family, evolutionarily-related proteins that are cell surface receptors that detect molecules outside the cell (biology), cell and activate cellular responses. Coupling with G proteins, they are called seven-transmembrane receptors because they pass through the cell membrane seven times. Text was copied from this source, which is available under Attribution 2.5 Generic (CC BY 2.5) license. Ligands can bind either to extracellular N-terminus and loops (e.g. glutamate receptors) or to the binding site within transmembrane helices (Rhodopsin-like family). They are all activated by agonists although a spontaneous auto-activation of an empty receptor can also be observed. G protein-coupled receptors are found only in eukaryotes, including y ...
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Neuropeptide
Neuropeptides are chemical messengers made up of small chains of amino acids that are synthesized and released by neurons. Neuropeptides typically bind to G protein-coupled receptors (GPCRs) to modulate neural activity and other tissues like the gut, muscles, and heart. There are over 100 known neuropeptides, representing the largest and most diverse class of signaling molecules in the nervous system. Neuropeptides are synthesized from large precursor proteins which are cleaved and post-translationally processed then packaged into dense core vesicles. Neuropeptides are often co-released with other neuropeptides and neurotransmitters in a single neuron, yielding a multitude of effects. Once released, neuropeptides can diffuse widely to affect a broad range of targets. Synthesis Neuropeptides are synthesized from large, inactive precursor proteins called prepropeptides. Prepropeptides contain sequences for a family of distinct peptides and often contain repeated copies of the sa ...
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Opioid Receptor
Opioid receptors are a group of inhibitory G protein-coupled receptors with opioids as ligands. The endogenous opioids are dynorphins, enkephalins, endorphins, endomorphins and nociceptin. The opioid receptors are ~40% identical to somatostatin receptors (SSTRs). Opioid receptors are distributed widely in the brain, in the spinal cord, on peripheral neurons, and digestive tract. Discovery By the mid-1960s, it had become apparent from pharmacologic studies that opiate drugs were likely to exert their actions at specific receptor sites, and that there were likely to be multiple such sites. Early studies had indicated that opiates appeared to accumulate in the brain. The receptors were first identified as specific molecules through the use of binding studies, in which opiates that had been labeled with radioisotopes were found to bind to brain membrane homogenates. The first such study was published in 1971, using 3H-levorphanol. In 1973, Candace Pert and Solomon H. Snyder publis ...
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Neuropeptide AF
Neuropeptides are chemical messengers made up of small chains of amino acids that are synthesized and released by neurons. Neuropeptides typically bind to G protein-coupled receptors (GPCRs) to modulate neural activity and other tissues like the gut, muscles, and heart. There are over 100 known neuropeptides, representing the largest and most diverse class of signaling molecules in the nervous system. Neuropeptides are synthesized from large precursor proteins which are cleaved and post-translationally processed then packaged into dense core vesicles. Neuropeptides are often co-released with other neuropeptides and neurotransmitters in a single neuron, yielding a multitude of effects. Once released, neuropeptides can diffuse widely to affect a broad range of targets. Synthesis Neuropeptides are synthesized from large, inactive precursor proteins called prepropeptides. Prepropeptides contain sequences for a family of distinct peptides and often contain repeated copies of the s ...
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Neuropeptide FF
NPFF Neuropeptide FF (FLFQPQRFa) is a mammalian amidated neuropeptide originally isolated from bovine brain and characterized as a pain-modulating peptide, with anti-opioid activity on morphine-induced analgesia. In humans, Neuropeptide FF peptides are encoded by the ''NPFF'' gene. Two genes encoding two different receptors (NPFF1 and NPFF2) and two precursors (NPFFA and NPFFB) have been cloned in several mammalian species. Function Neuropeptide FF (NPFF) and RFamide related peptides issued from two precursors interact with good affinity with two subtypes of G protein-coupled receptors, namely NPFF1 and NPFF2 subtypes and are involved in several physiological functions such as cardiovascular regulation, hormonal control, macrophage activation, body temperature homeostasis and pain modulation. Processing of the NPFFA precursor at basic proteolytic sites should generate a NPFF-containing peptide with three additional N-terminal amino acids different between species, and a NPSF ...
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Neuropeptide SF
Neuropeptides are chemical messengers made up of small chains of amino acids that are synthesized and released by neurons. Neuropeptides typically bind to G protein-coupled receptors (GPCRs) to modulate neural activity and other tissues like the gut, muscles, and heart. There are over 100 known neuropeptides, representing the largest and most diverse class of signaling molecules in the nervous system. Neuropeptides are synthesized from large precursor proteins which are cleaved and post-translationally processed then packaged into dense core vesicles. Neuropeptides are often co-released with other neuropeptides and neurotransmitters in a single neuron, yielding a multitude of effects. Once released, neuropeptides can diffuse widely to affect a broad range of targets. Synthesis Neuropeptides are synthesized from large, inactive precursor proteins called prepropeptides. Prepropeptides contain sequences for a family of distinct peptides and often contain repeated copies of the s ...
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Neuropeptide VF
Neuropeptides are chemical messengers made up of small chains of amino acids that are synthesized and released by neurons. Neuropeptides typically bind to G protein-coupled receptors (GPCRs) to modulate neural activity and other tissues like the gut, muscles, and heart. There are over 100 known neuropeptides, representing the largest and most diverse class of signaling molecules in the nervous system. Neuropeptides are synthesized from large precursor proteins which are cleaved and post-translationally processed then packaged into dense core vesicles. Neuropeptides are often co-released with other neuropeptides and neurotransmitters in a single neuron, yielding a multitude of effects. Once released, neuropeptides can diffuse widely to affect a broad range of targets. Synthesis Neuropeptides are synthesized from large, inactive precursor proteins called prepropeptides. Prepropeptides contain sequences for a family of distinct peptides and often contain repeated copies of the s ...
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BIBP-3226
BIBP-3226 is a drug used in scientific research which acts as a potent and selective antagonist for both the Neuropeptide Y receptor Y1 and also the neuropeptide FF receptor. It was the first non-peptide antagonist developed for the Y1 receptor and has been widely used to help determine its functions in the body. Activation of Y1 is thought to be involved in functions such as regulation of appetite and anxiety, and BIBP-3226 has anxiogenic and anorectic effects, as well as blocking the Y1-mediated corticotropin releasing hormone release. It has also been used as a lead compound A lead compound (, i.e. a "leading" compound, not to be confused with various compounds of the metallic element lead) in drug discovery is a chemical compound that has pharmacology, pharmacological or biological activity likely to be therapeutical ... to develop a number of newer more potent Y1 antagonists. References Neuropeptide Y antagonists {{nervous-system-drug-stub ...
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Neuropeptide Y Receptor Y1
Neuropeptide Y receptor type 1 is a protein that in humans is encoded by the ''NPY1R'' gene. Selective ligands Agonists * Neuropeptide Y (endogenous agonist, non subtype selective) * Peptide YY Peptide YY (PYY) also known as peptide tyrosine tyrosine is a peptide that in humans is encoded by the gene. Peptide YY is a short (36-amino acid) peptide released from cells in the ileum and colon in response to feeding. In the blood, gut, a ... Antagonists ;Peptide * BVD-10 (selective NPY1 antagonist, CAS# 262418-00-8) * GR-231,118 (mixed NPY1 antagonist / NPY4 agonist, CAS# 158859-98-4) ;Non-peptide * BIBO-3304 (CAS# 191868-14-1) * BIBP-3226 (CAS# 159013-54-4) * PD-160,170 (CAS# 181468-88-2) Available Structures 5ZBH(Neuropeptide Y1 bound to antagonist BMS-193835) 5ZBQ(Neuropeptide Y1 bound to antagonist UR-MK299) See also * Neuropeptide Y receptor References Further reading * * * * * * * * * * * * * * External links * * G protein-c ...
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RF-9 (drug)
The Fournier RF-9 is a two-seat motorglider of conventional sailplane configuration. Originally produced in France, manufacturing was later taken over by ABS Aircraft in Switzerland, and then by Gomolzig in Germany. The pilot and passenger are accommodated side-by-side, and the aircraft's wings are foldable for ease of storage. It first flew in 1977. The licence-built example was known as the Fournier RF-9 ABS but only one, registration D-KHGO (w/nr.9021) was ever constructed. In 1994, ABS Aircraft GmbH left the development of ABS RF-9 though two further kits had been built, and were later constructed by the Polish Aircraft company Polavia. Specifications (RF-9) See also * Fournier RF 4 * Fournier RF 5 The Fournier RF 5 is a two-seat motor glider designed by René Fournier. Design and development The RF 5 is based on the single seater Fournier RF 4, and is a low-winged monoplane of all-wooden construction, with the crew of two sat in a tandem ... {{DEFAULTSORT:Fourn ...
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