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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 receptor, and G protein–linked receptors (GPLR), constitute a large protein family of receptors that detect molecules outside the cell and activate internal signal transduction pathways and, ultimately, cellular responses. Coupling with G proteins, they are called seven-transmembrane receptors because they pass through the cell membrane seven times.[2] G protein–coupled receptors are found only in eukaryotes, including yeast, choanoflagellates,[3] and animals. The ligands that bind and activate these receptors include light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters, and vary in size from small molecules to peptides to large proteins
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Protein Tertiary Structure
Protein tertiary structure
Protein tertiary structure
is the three dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid
Amino acid
side chains may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates
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Nobel Prize
The Nobel Prize
Nobel Prize
(/ˈnoʊbɛl/, Swedish pronunciation: [nʊˈbɛl]; Swedish definite form, singular: Nobelpriset; Norwegian: Nobelprisen) is a set of annual international awards bestowed in several categories by Swedish and Norwegian institutions in recognition of academic, cultural, or scientific advances. The will of the Swedish scientist Alfred Nobel
Alfred Nobel
established the prizes in 1895
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Guanine Nucleotide Exchange Factor
Guanine
Guanine
nucleotide exchange factors (GEFs) are proteins or protein domains that activate monomeric GTPases by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP).[1] A variety of unrelated structural domains have been shown to exhibit guanine nucleotide exchange activity. Some GEFs can activate multiple GTPases while others are specific to a single GTPase.Contents1 Function 2 Mechanism 3 Structure and specificity3.1 CDC25 domain 3.2 DH and PH domains 3.3 DHR2 domain 3.4 Sec7 domain4 Regulation 5 Cancer 6 Examples 7 See also 8 References 9 External linksFunction[edit]Schematic of GEF activation of a GTPase Guanine
Guanine
nucleotide exchange factors (GEFs) are proteins or protein domains involved in the activation of small GTPases
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Guanosine Diphosphate
Guanosine
Guanosine
diphosphate, abbreviated GDP, is a nucleoside diphosphate. It is an ester of pyrophosphoric acid with the nucleoside guanosine. GDP consists of the pyrophosphate group, the pentose sugar ribose, and the nucleobase guanine. GDP is the product of GTP dephosphorylation by GTPases, e.g., the G-proteins that are involved in signal transduction. GDP is converted into GTP with the help of pyruvate kinase and phosphoenolpyruvate. See also[edit]DNA
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Guanosine Triphosphate
Guanosine-5'-triphosphate
Guanosine-5'-triphosphate
(GTP) is a purine nucleoside triphosphate. It is one of the building blocks needed for the synthesis of RNA during the transcription process. Its structure is similar to that of the guanine nucleobase, the only difference being that nucleotides like GTP have a ribose sugar and three phosphates, with the nucleobase attached to the 1' and the triphosphate moiety attached to the 5' carbons of the ribose. It also has the role of a source of energy or an activator of substrates in metabolic reactions, like that of ATP, but more specific
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Gαs
The Gs alpha subunit (Gαs, Gsα, or Gs protein) is a heterotrimeric G protein subunit that activates the cAMP-dependent pathway by activating adenylyl cyclase. It is one of the three main families of G proteins: Gαi/Gαo, Gαq, and Gαs.[1] A mnemonic for remembering this subunit is to look at the first letter (Gαs = Adenylate Cyclase stimulator).Contents1 Receptors 2 Function 3 See also 4 References 5 External linksReceptors[edit] The G protein-coupled receptors
G protein-coupled receptors
that couple to this kind of G-protein include:5-HT receptors types 5-HT4 and 5-HT7 ACTH receptor
ACTH receptor
a.k.a
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Gαi
Gi alpha subunit (Gαi, or Gi/G0 or Gi protein) is a heterotrimeric G protein subunit that inhibits the production of cAMP from ATP.[1] A mnemonic for remembering this subunit is to look at first letter (Gαi = Adenylyl Cyclase inhibitor).Contents1 Receptors 2 Function 3 Types3.1 Gia1 3.2 Gia2 3.3 Gia34 See also 5 References 6 External linksReceptors[edit] The following G protein-coupled receptors
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Gαq
Gq protein (Gαq, or Gq/11) is a heterotrimeric G protein subunit that activates phospholipase C (PLC). PLC in turn hydrolyzes Phosphatidylinositol 4,5-bisphosphate
Phosphatidylinositol 4,5-bisphosphate
(PIP2) to diacyl glycerol (DAG) and inositol trisphosphate (IP3) signal transduction pathway. DAG acts as a second messenger that activates Protein Kinase C (PKC) and IP3 helps in phosphorylation of some proteins.Contents1 Naming 2 Function 3 Examples of GPCR partners 4 Genes 5 See also 6 References 7 External linksNaming[edit] There has been much debate about the naming of the Gαq. In the initial identification of the protein, it was named G alpha 42, because it runs at 42 kDa on SDS-PAGE. Although, already identified by Micheal Strathmann and Mel Simon, shared the sequence this naming it G alpha q. However, the "q" in the name is arbitrarily named and does not stand for anything in particular
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G12/G13 Alpha Subunits
G12/G13 subunits are alpha units of heterotrimeric G proteins that regulate cell processes through the use of guanine nucleotide exchange factors.[1] These two subunits represent a fourth class of G protein alpha subunits.[2] They are not sensitive to pertussis toxin.[3] G proteins G12 and G13 regulate actin cytoskeletal remodeling in cells.[4] G13 is also essential for receptor tyrosine kinase-induced migration of fibroblast and endothelial cells.[5] Genes[edit] GNA12
GNA12
(GNA12), GNA13References[edit]^ Dhanasekaran N, Dermott JM (1996). "Signaling by the G12 class of G proteins". Cell. Signal. 8 (4): 235–45. doi:10.1016/0898-6568(96)00048-4. PMID 8842523.  ^ Strathmann MP, Simon MI (1991). "G alpha 12 and G alpha 13 subunits define a fourth class of G protein alpha subunits". Proc. Natl. Acad. Sci. U.S.A. 88 (13): 5582–6. doi:10.1073/pnas.88.13.5582. PMC 51921 
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Nobel Prize In Chemistry
The Nobel Prize
Nobel Prize
in Chemistry
Chemistry
(Swedish: Nobelpriset i kemi) is awarded annually by the Royal Swedish Academy of Sciences
Royal Swedish Academy of Sciences
to scientists in the various fields of chemistry. It is one of the five Nobel Prizes established by the will of Alfred Nobel
Alfred Nobel
in 1895, awarded for outstanding contributions in chemistry, physics, literature, peace, and physiology or medicine. This award is administered by the Nobel Foundation and awarded by Royal Swedish Academy of Sciences
Royal Swedish Academy of Sciences
on proposal of the Nobel Committee
Nobel Committee
for Chemistry
Chemistry
which consists of five members elected by Academy
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Robert Lefkowitz
Robert Joseph Lefkowitz (born April 15, 1943) is an American physician (internist and cardiologist) and biochemist. He is best known for his groundbreaking discoveries that reveal the inner workings of an important family G protein-coupled receptors, for which he was awarded the 2012 Nobel Prize for Chemistry
Nobel Prize for Chemistry
with Brian Kobilka. He is currently an Investigator with the Howard Hughes Medical Institute
Howard Hughes Medical Institute
as well as a James B. Duke Professor of Medicine and Professor of Biochemistry
Biochemistry
and Chemistry at Duke University.Contents1 Early life 2 Career 3 Personal life 4 Awards 5 References 6 External linksEarly life[edit] Lefkowitz was born on April 15, 1943, in The Bronx, New York to Jewish parents Max and Rose Lefkowitz
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Fluticasone/salmeterol
The combination preparation fluticasone/salmeterol is a formulation containing fluticasone propionate and salmeterol xinafoate, used in the management of asthma and chronic obstructive pulmonary disease (COPD). Patent protection in the US expired in 2010, and European patent protection expired in 2013. However, the availability of a generic form of Advair in the United States may be significantly delayed because the Food and Drug Administration has not determined a standard for the bioequivalence of inhaled steroids in multi-dose inhalers or dry powder inhalers. Fluticasone, a corticosteroid, is the anti-inflammatory component of the combination, while salmeterol, a long acting beta-adrenoceptor agonist (LABA), treats constriction of the airways
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Inverse Agonist
In the field of pharmacology, an inverse agonist is an agent that binds to the same receptor as an agonist but induces a pharmacological response opposite to that agonist. A neutral antagonist has no activity in the absence of an agonist or inverse agonist but can block the activity of either.[1] Inverse agonists have opposite actions to those of agonists but the effects of both of these can be blocked by antagonists.[2] A prerequisite for an inverse agonist response is that the receptor must have a constitutive (also known as intrinsic or basal) level activity in the absence of any ligand
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Human
Homo
Homo
sapiens idaltu White et al., 2003 Homo
Homo
sapiens sapiens Homo
Homo
sapiens population densitySynonyms Species
Species
synonymy[1]aethiopicus Bory de St. Vincent, 1825 americanus Bory de St. Vincent, 1825 arabicus Bory de St. Vincent, 1825 aurignacensis Klaatsch & Hauser, 1910 australasicus Bory de St. Vincent, 1825 cafer Bory de St. Vincent, 1825 capensis Broom, 1917 columbicus Bory de St. Vincent, 1825 cro-magnonensis Gregory, 1921 drennani Kleinschmidt, 1931 eurafricanus (Sergi, 1911) grimaldiensis Gregory, 1921 grimaldii Lapouge, 1906 hottentotus Bory de St. Vincent, 1825 hyperboreus Bory de St. Vincent, 1825 indicus Bory de St. Vincent, 1825 japeticus Bory de St. Vincent, 1825 melaninus Bory de St. Vincent, 1825 monstrosus Linnaeus, 1758 neptunianus Bory de St. Vincent, 1825 palestinus McCown & Keith, 1932 patagonus Bory de St
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