Confusing date June 2010 Image Aequorin 1EJ3.png thumb 200px Aequorin ribbon diagram from Protein Data Bank PDB database with prosthetic group coelenterazine in blue Aequorin is a photoprotein isolated from luminescent jellyfish like various Aequorea species, e.g., Aequorea victoria and a variety of other marine organisms. ref cite journal author Shimomura O title A short story of aequorin. journal Biol Bull. volume 189 pages 1 5 year 1995 pmid 7654844 doi 10.2307 1542194 issue 1 publisher Biological Bulletin, Vol. 189, No. 1 jstor 1542194 ref It was originally isolated from the coelenterate by Osamu Shimomura . ref cite journal author Shimomura O, Johnson FH, Saiga Y title Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea journal J Cell Comp Physiol volume 59 pages 223 239 year 1962 pmid 13911999 doi 10.1002 jcp.1030590302 issue 3 ref Structure Aequorin is composed of two distinct units, the apoprotein apoaequorin , with an approximate molecular weight of 22 Atomic mass unit kDa , and the prosthetic group coelenterazine , a luciferin . Mechanism of Action The two components of aequorin reconstitute spontaneously, forming ... and Medicine Since the emitted light can be easily detected with a luminometer , aequorin has become ... cells expressing the aequorin gene can effectively synthesize aequorin However, Recombinant DNA recombinant ..., making aequorin suitable as a calcium in biology Ca sup 2 sup reporter in plants, fungi, and mammalian ... 14 pages 5467 75 year 1995 pmid 8521803 pmc 394660 issue 22 ref Aequorin has a number of advantages ... of aequorin is that the prosthetic group coelenterazine is irreversibly consumed to produce light ... http ca.expasy.org uniprot P07164 Swiss Prot Aequorin entry cite journal author Mith fer A, Mazars C title Aequorin based measurements of intracellular Ca sup 2 sup signatures in plant cells journal ... Oxidoreductases Category Bioluminescence de Aequorin he ja pl Akworyna ru ... more details
Photoproteins refer to bioluminescent proteins from luminous organisms. These proteins do not exhibit a luciferin luciferase reaction, ref http www.britannica.com EBchecked topic 458121 photoprotein Encyclop dia Britannica photoprotein Retrieved on 6 Mars, 2009 ref that is, a normal enzyme Substrate biochemistry substrate reaction. Instead, these proteins display luminescence proportional to the amount of the protein. Such proteins are stable as a luciferin photoprotein complex, often until the addition of another required factor, such as calcium in biology Ca sup 2 sup for the photoprotein aequorin . The term was first used to describe the unusual chemistry of the Chaetopterus luminescent system. ref Shimomura, O. Bioluminescence Chemical Principles and Methods World Scientific Publishing Co., 2006. ref References reflist Category Bioluminescence protein stub ... more details
orphan date March 2010 primarysources date March 2010 iLCD Lighting Cell Display is a device developed by a research team from Universidad Politecnica de Valencia , a Massachusetts Institute of Technology MIT educated Bioengineering bioengineer , undergraduated students of the Universidad Polit ctica de Valencia and Universitat de Val ncia and several members of the faculty and research staff from Universidad de Val ncia Manuel Porcar , UPV Pedro De Cordoba and University of Malaga Emilio Navarro . It is based on yeast cell s expressing aequorin protein sensitive to change in intracellular calcium . Upon electrical stimulation , the transient calcium wave emerges inside the yeast cells and translates into a measurable light signal. Assembly of multiple electrode s over lawn of yeast cells yields Thanks to electronic control and sub second timescale it is one of the first examples of bioelectronic devices capable of bi directional communication between a computer and a living system. It is also one of the first examples of design of simple synthetic biology circuits operating on orders of magnitude faster timescale than those based on gene expression . Fast response to a stimulus is essential in variety of applications such as Biosensor biosensing , medical technology , or as stated before bioelectronics . The project has been awarded a third place in 2009 IGEM iGEM competition References Vilanova C, Hueso A, Palanca C, Marco G, Pitarch M, Otero E, Crespo J, Szablowski J, Rivera S, Dom nguez Escrib L, Navarro E, Montagud A, de C rdoba PF, Gonz lez A, Ari o J, Moya A, Urchuegu a J, Porcar, M. Aequorin expressing yeast emits light under electric control.J Biotechnol. 2011 Mar 20 152 3 93 5. External links http 2009.igem.org Team Valencia home Official website J Biotechnol. 2011 Mar 20 152 3 93 5. Epub 2011 Feb 1. Category Biotechnology ... more details
enzyme Name Renilla luciferin 2 monooxygenase EC number 1.13.12.5 CAS number 61869 41 8 IUBMB EC number 1 13 12 5 GO code 0050248 image 2psj.png width caption Renilla reniformis luciferase with bound coelenterazine. Protein Data Bank PDB 2pdj ref Cite pmid 17980388 ref Renilla luciferin 2 monooxygenase EC number 1.13.12.5 is an enzyme that catalysis catalyzes the chemical reaction Renilla luciferin O sub 2 sub math rightleftharpoons math oxidized Renilla luciferin CO sub 2 sub h The two substrate biochemistry substrates of this enzyme are Coelenterazine and oxygen O sub 2 sub , whereas its 3 product chemistry products are coelenteramide , carbon dioxide CO sub 2 sub , and a photon of blue light. This enzyme was isolated from sea pansy Renilla reniformis , the sea pansy, a Bioluminescence bioluminescent sea pen. The enzyme belongs to the family of oxidoreductase s, specifically those acting on single donors with O sub 2 sub as oxidant and incorporation of two atoms of oxygen into the substrate oxygenases . The oxygen incorporated need not be derived from O with incorporation of one atom of oxygen internal monooxygenases o internal mixed function oxidases . In vivo, the photon emited by Renilla luciferin 2 monooxygenase transferred to green fluorescent protein , causing it to emit green light. The systematic name of this enzyme class is Renilla luciferin oxygen 2 oxidoreductase decarboxylating . Other names in common use include Renilla type luciferase , aequorin , and luciferase Renilla luciferin . References reflist 1 cite journal author Cormier MJ, Hori K, Anderson JM date 1974 title Bioluminescence in coelenterates journal Biochim. Biophys. Acta. volume 346 pages 137&ndash 64 pmid 4154104 issue 2 cite journal author Hori K, Anderson JM, Ward WW, Cormier MJ date 1975 title Renilla luciferin as the substrate for calcium induced photoprotein bioluminescence. Assignment of luciferin tautomers in aequorin and mnemiopsin journal Biochemistry. volume 14 pages 2371&ndash ... more details
, Luc, and aequorin . For other bioreporters, the signal must be activated by an external light source ... . AequorinAequorin is a photoprotein isolated from the bioluminescent jellyfish Aequorea victoria ... of blue light in the 460 470 nm range. Aequorin has been incorporated into human B cell ... NCI Biomedical Imaging Symposium. ref . The B cells are genetically engineered to produce aequorin ... have also been isolated from the sea pansy Renilla reniformis . GFP, like aequorin, produces a blue ... more details
aequorin . The blue light produced is in turn transduced to green by the now famous green fluorescent protein GFP . Both aequorin and GFP are important tools used in biological research. In 1961, Shimomura and Johnson isolated the protein aequorin, and its small molecule cofactor, coelenterazine ... cite journal author Shimomura O title A short story of aequorin journal The Biological bulletin volume ..., Ridgeway and Ashley microinjected aequorin into single muscle fibers of barnacles, and observed transient ... more details
and expression of the cDNA coding for aequorin, a bioluminescent calcium binding protein. Biochem ..., R.O., Longiaru, M., Cormier, M.J., Sequence comparisons of complementary DNAs encoding aequorin isotypes ... and molecular biology of the Ca2 activated photoprotein, aequorin. Photochem. Photobiol. , 49 ..., J.R., Ward, K.B., Preparation and initial characterization of crystals of the photoprotein aequorin ... more details
Anthony J. Trewavas is a professor at the University of Edinburgh ref http www.biology.ed.ac.uk research institutes plant pages staff pages T Trewavas staffpage.htm Staff Page Tony Trewavas ref , best known for his research in the fields of plant physiology and molecular biology . He is the leader of the http homepages.ed.ac.uk ebot40 main.html Edinburgh Molecular Signalling Group , who are investigating the role of calcium in signal transduction during plant development. He is an elected Fellow of the Royal Society of Edinburgh 1993 , the Royal Society of Arts 1995 , the Royal Society of London 1999 , the http www.futurestudies.co.uk Centre for Future Studies 2001 , and received the corresponding membership award from the http www.aspb.org American Society of Plant Biologists in 1999, a prize given to one non US biologist per year. ref cite web url http www.aspb.org committees awards.cfm title American Society of Plant Biologists Awards Winners publisher American Society of Plant Biologists accessdate 2007 07 01 ref He is named by the Institute for Scientific Information as a highly cited author in the field of animal and plant Sciences ISI author number A0597 2002 C . He is a past or present member of the editorial boards of the publications, Trends journals Trends in Plant Science , Botanica Acta , Plant Physiology journal Plant Physiology , What s New in Plant Physiology , Biochemical Journal and Plant, Cell and Environment . His recent research used a flexible confocal fluorescence ratio aiming assembly to image calcium redistribution during contact sensing, stomate stomatal aperture control, pollen tube and rhizoid growth, moss development and photomorphogenesis . Plants were transformed with the gene for the calcium sensitive luminescent protein aequorin , allowing measurements of cytosolic calcium in plants and bacteria. Plants have also been transformed with genes for calmodulin to better assess the role of calcium in development. The group also cloned plan ... more details
chembox Verifiedfields changed verifiedrevid 460106219 ImageFile Coelenterazine.png ImageSize 220px IUPACName 6 4 hydroxyphenyl 2 4 hydroxyphenyl methyl 8 phenylmethyl 7H imidazo 3,2 a pyrazin 3 one OtherNames Coelenterazine, Renilla luciferin Section1 Chembox Identifiers CASNo Ref cascite changed ?? CASNo 55779 48 1 ChEBI Ref ebicite correct EBI ChEBI 2311 StdInChI Ref stdinchicite correct chemspider StdInChI 1S C26H21N3O3 c30 20 10 6 18 7 11 20 15 23 26 32 29 16 24 19 8 12 21 31 13 9 19 27 22 25 29 28 23 14 17 4 2 1 3 5 17 h1 13,16,27,30 31H,14 15H2 StdInChIKey Ref stdinchicite correct chemspider StdInChIKey YHIPILPTUVMWQT UHFFFAOYSA N PubChem 2830 ChemSpiderID Ref chemspidercite correct chemspider ChemSpiderID 2728 SMILES C1 CC C C C1 CC2 C3N C C O N3C C N2 C4 CC C C C4 O CC5 CC C C C5 O InChI InChI 1S C26H21N3O3 c30 20 10 6 18 7 11 20 15 23 26 32 29 16 24 19 8 12 21 31 13 9 19 27 22 25 29 28 23 14 17 4 2 1 3 5 17 h1 13,16,27,30 31H,14 15H2 Section2 Chembox Properties Formula C sub 26 sub H sub 21 sub N sub 3 sub O sub 3 sub MolarMass 423.463 Appearance orange yellow crystals Density MeltingPt 175 178 C BoilingPt Solubility Section3 Chembox Hazards MainHazards FlashPt Autoignition Coelenterazine is the luciferin , the light emitting molecule, found in many aquatic organisms across seven Phylum phyla . ref cite book author Shimomura, O. year 2006 title Bioluminescence Chemical Principles and Methods publisher World Scientific Publishing isbn 9789812568014 ref It is the substrate in many luciferase s and photoprotein s including Renilla reniformis Renilla luciferin 2 monooxygenase luciferase Rluc , Gaussia luciferase Gluc , aequorin , and obelin . History Coelenterazine was simultaneously isolated and characterized by two groups studying the luminescent organisms sea pansy Renilla reniformis and the coelenterate Aequorea victoria , respectively. ref cite journal author Hori K, Charbonneau H, Hart RC, and Cormier MJ title Structure of native Renilla reinformis lucif ... more details
luminescent protein aequorin , was first purified from Aequorea victoria and its properties studied ... Y title Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous ... 13911999 doi 10.1002 jcp.1030590302 ref In A. victoria , GFP fluorescence occurs when aequorin interacts ... and GFP fluorescence in jellyfish is unknown. GFP is co expressed with aequorin in small granules around ... of the blue emission of aequorin , giving the bioluminescence a more green hue. The serine 65 residue ... partner of aequorin, A. victoria appears to evolutionarily prefer the less efficient, dual peaked ... more details
This is a list of articles that describe particular biomolecule s or types of biomolecules. compactTOC8 side yes seealso yes nobreak yes A For substances with an A or prefix such as a amylase amylase , please see the parent page in this case Amylase . A23187 Calcimycin, Calcium Ionophore Abamectin Abietic acid Acetic acid Acetylcholine Actin Actinomycin D Adenosine Adenosine diphosphate ADP Adenosine monophosphate AMP Adenosine triphosphate ATP Adenylate cyclase Adonitol Adrenaline , epinephrine Adrenocorticotropic hormone ACTH Aequorin Aflatoxin Agar Alamethicin Alanine Albumins Aldosterone Aleurone Alpha amanitin Allantoin Allethrin Amanatin, see Alpha amanitin Amino acid Amylase also see a amylase amylase Anabolic steroid Anethole Angiotensinogen Anisomycin Antidiuretic hormone ADH Arabinose Arginine Ascomycin Ascorbic acid vitamin C Asparagine Aspartic acid Asymmetric dimethylarginine Atrial natriuretic peptide ANP Auxin Avidin Azadirachtin A &ndash C sub 35 sub H sub 44 sub O sub 16 sub B Bacteriocin Beauvericin Bicuculline Bilirubin Biopolymer Biotin Vitamin H Brefeldin A Brassinolide Brucine C Cadaverine Caffeine Calciferol Vitamin D calcitonin Calmodulin Calmodulin Calreticulin Camphor Cannabinol Capsaicin Carbohydrase Carbohydrate Carnitine Carrageenan Casein Caspase Cellulase Cellulose C sub 6 sub H sub 10 sub O sub 5 sub sub x sub Cerulenin Cetrimonium bromide Cetrimide C sub 19 sub H sub 42 sub BrN Chelerythrine Chromomycin A3 Chaparonin Chitin a chloralose Chloralose Chlorophyll Cholecystokinin CCK Cholesterol Choline Chondroitin sulfate Cinnamaldehyde Citral Citric acid Citrinin Citronellal Citronellol Citrulline Cobalamin Vitamin B12 vitamin B sub 12 sub Coenzyme Coenzyme Q Colchicine Collagen Coniine Corticosteroid Corticosterone Corticotropin releasing hormone CRH Cortisol Creatine Creatine kinase Crystallin Alpha cyclodextrin Cyclodextrin Cyclodextrin glycosyltransferase Cyclopamine Cyclopiazonic acid Cysteine Cystine Cytidine Cytochala ... more details
PBB geneid 5540 Neuropeptide Y receptor type 4 is a protein that in humans is encoded by the PPYR1 gene . ref name pmid9417917 cite journal author Lutz CM, Richards JE, Scott KL, Sinha S, Yang Feng TL, Frankel WN, Thompson DA title Neuropeptide Y receptor genes mapped in human and mouse receptors with high affinity for pancreatic polypeptide are not clustered with receptors specific for neuropeptide Y and peptide YY journal Genomics volume 46 issue 2 pages 287 90 year 1998 month Feb pmid 9417917 pmc doi 10.1006 geno.1997.5024 ref ref name entrez cite web title Entrez Gene PPYR1 pancreatic polypeptide receptor 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 5540 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text Selective Ligands Agonists Pancreatic polypeptide Neuropeptide Y endogenous agonist, non subtype selective Peptide YY GR 231,118 mixed NPY sub 1 sub antagonist NPY sub 4 sub agonist, CAS 158859 98 4 Antagonists UR AK49 ref name pmid17885919 cite journal author Ziemek R, Schneider E, Kraus A, Cabrele C, Beck Sickinger AG, Bernhardt G, Buschauer A title Determination of affinity and activity of ligands at the human neuropeptide Y Y4 receptor by flow cytometry and aequorin luminescence journal Journal of Receptor and Signal Transduction Research volume 27 issue 4 pages 217 33 year 2007 pmid 17885919 doi 10.1080 10799890701505206 url issn ref See also Neuropeptide Y receptor References reflist External links cite web url http www.iuphar db.org GPCR ReceptorDisplayForward?receptorID 2370 title Neuropeptide Y Receptors Y sub 4 sub accessdate author authorlink coauthors date format work IUPHAR Database of Receptors and Ion Channels publisher International Union of Basic and Clinical Pharmacology pages language archiveurl archivedate quote Further reading refbegin 2 PBB Further reading citations cite journal autho ... more details
Calcium concentration microdomains CCMs are sites in a cell s cytoplasm with a localised high calcium ion Ca sup 2 sup concentration. ref name Serulle cite journal last Serulle first Y. coauthors Sugimori, M., Llinas, R. R. title Imaging synaptosomal calcium concentration microdomains and vesicle fusion by using total internal reflection fluorescent microscopy journal Proceedings of the National Academy of Sciences date 30 January 2007 volume 104 issue 5 pages 1697 1702 doi 10.1073 pnas.0610741104 ref They are found immediately around the intracellular opening of calcium channel s when a calcium channel opens, the Ca sup 2 sup concentration in the adjacent CCM increases up to several hundred Molar concentration micromolar M . ref name Llinas cite journal last Llinas first R coauthors Sugimori, M, Silver, R. title Microdomains of high calcium concentration in a presynaptic terminal journal Science date 1 May 1992 volume 256 issue 5057 pages 677 679 doi 10.1126 science.1350109 pmid 1350109 ref These microdomains take part in calcium signaling , which has a diverse range of potential outcomes. ref name Demuro cite journal last Demuro first A coauthors Parker, I title Imaging single channel calcium microdomains journal Cell calcium date 2006 Nov Dec volume 40 issue 5 6 pages 413 22 pmid 17067668 accessdate 8 May 2011 doi 10.1016 j.ceca.2006.08.006 pmc 1694561 ref Calcium concentration microdomains can be visualised with fluorescence microscopy by using aequorin as a reporter protein. ref name Montero cite journal author Montero M, Brini M, Marsault R, Alvarez J, Sitia R, Pozzan T, Rizzuto R title Monitoring dynamic changes in free Ca sup 2 sup concentration in the endoplasmic reticulum of intact cells journal EMBO J volume 14 pages 5467 75 year 1995 pmid 8521803 pmc 394660 issue 22 ref Ion Channel Process The actions of the Sodium potassium pump Na K ATPase enzyme relate with the creation of calcium signaling microdomains. ref name Tian cite journal last Tian first J. ... more details
George, C. H., Kendall, J. M., Campbell, A. K. and Evans, W. H. year 1998 title Connexin aequorin chimerae ... title Assembly of chimeric connexin aequorin proteins into functional gap junction channels. Reporting ... more details
bioluminescence occurs because of energy transfer from the luminescent molecule aequorin , which ..., M. 1969 Response of aequorin bioluminescence to rapid changes in calcium concentration. Nature ... more details
Biochemistry is the study of the chemistry chemical processes in living organism s. It deals with the structure and function of cellular components such as protein s, carbohydrate s, lipid s, nucleic acid s and other biomolecule s. Articles related to biochemistry include compactTOC8 side yes top yes num yes p NOTOC 0 9 2 amino 5 phosphonovalerate 3 end 5 end A ABC Transporter Genes abl gene acetic acid acetyl CoA acetylcholine acetylcysteine acid acidic fibroblast growth factor acrosin actin action potential activation energy active site active transport adenosine adenosine diphosphate ADP adenosine monophosphate AMP adenosine triphosphate ATP adenovirus adrenergic receptor adrenodoxin aequorin aerobic respiration agonist alanine albumin disambiguation albumin alcohol alcoholic fermentation alicyclic compound aliphatic compound alkali Allosteric site allostery allotrope allotropy alpha adrenergic receptor Alpha helix alpha 1 adrenergic receptor alpha 2 adrenergic receptor alpha beta T cell antigen receptor alpha fetoprotein alpha globulin alpha macroglobulin alpha MSH Ames test amide amine amino amino acid amino acid receptor amino acid sequence amino acid sequence homology aminobutyric acid disambiguation aminobutyric acid ammonia AMPA receptor amyloid anabolism anaerobic respiration analytical chemistry androgen receptor angiotensin angiotensin II angiotensin receptor ankyrin annexin II antibiotic antibody apoenzyme apolipoprotein apoptosis aquaporin archaea arginine argipressin aromatic amine aromatic compound arrestin Arrhenius equation aryl hydrocarbon receptor asparagine aspartic acid atom atomic atomic absorption spectroscopy atomic mass atomic mass unit atomic nucleus atomic number atomic orbital atomic radius Atomic weight ATP synthase ATPase atrial natriuretic factor atrial natriuretic factor receptor Avogadro s number axon B B cell bacteria bacterial conjugation bacterial outer membrane protein bacterial protein bacteriorhodopsin base chemistry base pair ... more details
aequorin Calcium binding protein CaBP &mdash Prevagen neuroprotective ref cite journal author Nelson ... of calcium loaded apo aequorin and apo obelin. journal Protein Sci volume 14 issue 3 pages 663 ... more details
This is part of the List of MeSH codes list of the D codes for MeSH . It is a product of the United States National Library of Medicine . Source for content is http www.nlm.nih.gov mesh filelist.html here . File 2006 MeSH Trees . MeshNumber D12.776 Proteins proteins MeshNumber D12.776.034 Albumins albumins MeshNumber D12.776.034.145 C Reactive Protein c reactive protein MeshNumber D12.776.034.180 Conalbumin conalbumin MeshNumber D12.776.034.398 Lactalbumin lactalbumin MeshNumber D12.776.034.614 Ovalbumin ovalbumin MeshNumber D12.776.034.614.300 Avidin avidin MeshNumber D12.776.034.700 Parvalbumins parvalbumins MeshNumber D12.776.034.756 Ricin ricin MeshNumber D12.776.034.841 Serum Albumin serum albumin MeshNumber D12.776.034.841.350 Methemalbumin methemalbumin MeshNumber D12.776.034.841.450 Prealbumin prealbumin MeshNumber D12.776.034.841.540 Serum Albumin, Bovine serum albumin, bovine MeshNumber D12.776.034.841.665 Serum Albumin, Radio Iodinated serum albumin, radio iodinated MeshNumber D12.776.034.900 Technetium Tc 99m Aggregated Albumin technetium tc 99m aggregated albumin MeshNumber D12.776.037 Algal Proteins algal proteins MeshNumber D12.776.045 Amphibian Proteins amphibian proteins MeshNumber D12.776.045.500 Xenopus Proteins xenopus proteins MeshNumber D12.776.049 Amyloid amyloid MeshNumber D12.776.049.025 Amyloid beta Protein amyloid beta protein MeshNumber D12.776.049.025.150 Amyloid beta Protein Precursor amyloid beta protein precursor MeshNumber D12.776.049.790 Serum Amyloid A Protein serum amyloid a protein MeshNumber D12.776.049.800 Serum Amyloid P Component serum amyloid p component MeshNumber D12.776.053 Antifreeze Proteins antifreeze proteins MeshNumber D12.776.053.100 Antifreeze Proteins, Type I antifreeze proteins, type i MeshNumber D12.776.053.200 Antifreeze Proteins, Type II antifreeze proteins, type ii MeshNumber D12.776.053.350 Antifreeze Proteins, Type III antifreeze proteins, type iii MeshNumber D12.776.053.500 Antifreeze Proteins, Type IV ant ... more details
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