関: YFP

WordNet

cowardly or treacherous; "the little yellow stain of treason"-M.W.Straight; "too yellow to stand and fight"
turn yellow; "The pages of the book began to yellow"
yellow color or pigment; the chromatic color resembling the hue of sunflowers or ripe lemons (同)yellowness
changed to a yellowish color by age; "yellowed parchment" (同)yellowed
of the color intermediate between green and orange in the color spectrum; of something resembling the color of an egg yolk (同)yellowish, xanthous
emitting light during exposure to radiation from an external source
a lighting fixture that uses a fluorescent lamp (同)fluorescent fixture
brilliantly colored and apparently giving off light; "fluorescent colors"
utter or declare in a very loud voice; "You dont have to yell--I can hear you just fine" (同)scream
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
exhibit or undergo fluorescence

PrepTutorEJDIC

『黄色の』 / 皮膚の黄色い / 《俗》おく病な(cowardly) / (新聞が)センセーショナルな,扇情的な / 〈U〉『黄色』 / 〈C〉黄色いもの;卵黄 / 〈U〉〈C〉黄色の絵の具(顔料,染料),黄色の服 / …‘を'黄色にする / 黄色になる
けい光を放つ,けい光性の / けい光灯
(…を求めて)『大声で叫ぶ』《+for+名》;(…に)大声をあげる《+at+名》 / (…に向かって)…‘を'叫んで(大声で)言う《+out+名(+名+out)+at(to)+名》 / 『叫び声』金切り声,わめき
蛋白(たんばく)質
けい光を発する

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/07/08 20:06:57」(JST)

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Yellow Fluorescent Protein (YFP) is a genetic mutant of green fluorescent protein (GFP) originally derived from the jellyfish Aequorea victoria. Its excitation peak is 514 nm and its emission peak is 527 nm. Like the parent GFP, YFP is a useful tool in cell and molecular biology thanks to its properties useful for fluorescence microscopy.

Three improved versions of YFP are Citrine, Venus, and Ypet. They have reduced chloride sensitivity, faster maturation, and increased brightness (defined as the product of the extinction coefficient and quantum yield). Typically, YFP serves as the acceptor for genetically-encoded FRET sensors of which the most likely donor FP is monomeric cyan fluorescent protein (mCFP). The red-shift relative to GFP is caused by a Pi-Pi stacking interaction as a result of the T203Y substitution introduced by mutation, which essentially increases the polarizability of the local chromophore environment as well as providing additional electron density into the chromophore.

"Venus" contains a novel amino acid substitution –F46L– which accelerates the oxidation of the chromophore at 37°C, the rate limiting step of maturation. The protein has other substitutions (F64L/ M153T/ V163A/ S175G), permitting Venus to fold well and giving it relative tolerance to acidosis and Cl^-.^[1]

References

^ Uemura, T.; Kim, H.; Saito, C.; Ebine, K.; Ueda, T.; Schulze-Lefert, P.; Nakano, A. (2012). "Qa-SNAREs localized to the trans-Golgi network regulate multiple transport pathways and extracellular disease resistance in plants". Proceedings of the National Academy of Sciences 109 (5): 1784–9. doi:10.1073/pnas.1115146109. PMC 3277133. PMID 22307646.

External links

Introduction to fluorescent proteins
Tsien, Roger Y.; Llopis, Atsushi; Heim, Juan; McCaffery, Roger; Adams, J. Michael; Ikura, Joseph A.; Tsien, Mitsuhiko (1997). "Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin". Nature 388 (6645): 882–7. doi:10.1038/42264. PMID 9278050.

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English Journal

A Quantitative Protocol for Intensity-Based Live Cell FRET Imaging.

Kaminski CF, Rees EJ, Schierle GS.SourceDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK.
Methods in molecular biology (Clifton, N.J.).Methods Mol Biol.2014;1076:445-54. doi: 10.1007/978-1-62703-649-8_19.
Förster resonance energy transfer (FRET) has become one of the most ubiquitous and powerful methods to quantify protein interactions in molecular biology. FRET refers to the sensitization of an acceptor molecule through transfer of energy from a nearby donor, and it can occur if the emission band o
PMID 24108638

Genetically encoded FRET-based nanosensor for in vivo measurement of leucine.

Mohsin M, Abdin MZ, Nischal L, Kardam H, Ahmad A.SourceMolecular Ecology Laboratory, Department of Botany, Faculty of Science, Hamdard University, New Delhi 110062, India.
Biosensors & bioelectronics.Biosens Bioelectron.2013 Dec 15;50:72-7. doi: 10.1016/j.bios.2013.06.028. Epub 2013 Jun 24.
Besides fundamental role in protein synthesis, leucine has metabolic roles as energy substrates, precursors for synthesis of other amino acids and as a modulator of muscle protein synthesis via the insulin-signaling pathway. Leucine concentration in cell and tissue is temporally dynamic as the metab
PMID 23835220

Functional analysis and tissue-differential expression of four FAD2 genes in amphidiploid Brassica napus derived from Brassica rapa and Brassica oleracea.

Lee KR, In Sohn S, Jung JH, Kim SH, Roh KH, Kim JB, Suh MC, Kim HU.SourceDepartment of Agricultural Biotechnology, National Academy of Agricultural Science, RDA, Suwon 441-707, Republic of Korea.
Gene.Gene.2013 Dec 1;531(2):253-62. doi: 10.1016/j.gene.2013.08.095. Epub 2013 Sep 9.
Fatty acid desaturase 2 (FAD2), which resides in the endoplasmic reticulum (ER), plays a crucial role in producing linoleic acid (18:2) through catalyzing the desaturation of oleic acid (18:1) by double bond formation at the delta 12 position. FAD2 catalyzes the first step needed for the production
PMID 24029080

Japanese Journal

Monitoring the caspase cascade in single apoptotic cells using a three-color fluorescent protein substrate

Sun Fan,Mikuni Shintaro,Kinjo Masataka
Biochemical and Biophysical Research Communications 404(2), 706-710, 2011-01-14
… Fluorescence cross-correlation spectroscopy (FCCS) reveals information about the spatiotemporal coincidence of two spectrally well-defined fluorescent molecules in a small observation area at the level of single-molecule sensitivity. …
NAID 120002834708

Spatial and temporal expression of actin depolymerizing factors ADF7 and ADF10 during male gametophyte development in Arabidopsis thaliana

Daher Firas Bou,van Oostende Chloe,Geitmann Anja
Plant and Cell Physiology 52(7), 1177-1192, 2011-07
NAID 40018902922

Improvement of a Venus-Based Bimolecular Fluorescence Complementation Assay to Visualize bFos-bJun Interaction in Living Cells

NAKAGAWA Chika,INAHATA Kazuto,NISHIMURA Shigenori,SUGIMOTO Kenji
Bioscience, Biotechnology, and Biochemistry 75(7), 1399-1401, 2011
… Bimolecular fluorescence complementation (BiFC) assay makes it possible to visualize protein-protein interactions in living cells. … In this assay, Venus, a bright-yellow variant of green fluorescent protein, is known to produce fluorescent backgrounds due to non-specific interactions. …
NAID 130000940533