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000057461 0247_ $$2DOI$$a10.1002/bip.20510
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000057461 084__ $$2WoS$$aBiochemistry & Molecular Biology
000057461 084__ $$2WoS$$aBiophysics
000057461 1001_ $$0P:(DE-Juel1)VDB16784$$aKottke, T.$$b0$$uFZJ
000057461 245__ $$aThe photochemistry of the light-, oxygen-, and voltage sensitive domains in the algal blue light receptor phot
000057461 260__ $$aNew York, NY$$bWiley$$c2006
000057461 300__ $$a373 - 378
000057461 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000057461 440_0 $$011661$$aBiopolymers$$v82$$x0006-3525$$y4
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000057461 520__ $$aPhot proteins are blue light photoreceptors in plants and algae that mainly regulate photomovement responses. They contain two light-, oxygen-, and voltage-sensitive (LOV) domains and a serine/threonine kinase domain. Both LOV domains noncovalently bind a flavin mononucleotide (FMN) as chromophore. Upon blue light illumination, the LOV domains undergo a photocycle, transiently forming a covalent adduct of the FMN moiety with a nearby cysteine residue. The presence of two light-sensitive domains in the photoreceptor raises the question about the differences in properties and function between LOV1 and LOV2. As a model system, the photocycles of the LOV1 and LOV2 domains from phot of the green alga Chlamydomonas reinhardtii have been studied in detail, both separately and in a tandem construct. Here we give an overview about the results on the individual behavior of the domains and their interaction. Furthermore, the current status in the understanding of the role of LOV1 in phot in general is presented.
000057461 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000057461 588__ $$aDataset connected to Web of Science, Pubmed
000057461 650_2 $$2MeSH$$aAnimals
000057461 650_2 $$2MeSH$$aChlamydomonas reinhardtii: chemistry
000057461 650_2 $$2MeSH$$aChlamydomonas reinhardtii: drug effects
000057461 650_2 $$2MeSH$$aChlamydomonas reinhardtii: radiation effects
000057461 650_2 $$2MeSH$$aFlavin Mononucleotide: chemistry
000057461 650_2 $$2MeSH$$aFlavin Mononucleotide: metabolism
000057461 650_2 $$2MeSH$$aFlavoproteins: chemistry
000057461 650_2 $$2MeSH$$aFlavoproteins: metabolism
000057461 650_2 $$2MeSH$$aKinetics
000057461 650_2 $$2MeSH$$aLight
000057461 650_2 $$2MeSH$$aModels, Chemical
000057461 650_2 $$2MeSH$$aOxygen: pharmacology
000057461 650_2 $$2MeSH$$aPhotochemistry: methods
000057461 650_2 $$2MeSH$$aSpectroscopy, Fourier Transform Infrared
000057461 650_7 $$00$$2NLM Chemicals$$aFlavoproteins
000057461 650_7 $$0146-17-8$$2NLM Chemicals$$aFlavin Mononucleotide
000057461 650_7 $$07782-44-7$$2NLM Chemicals$$aOxygen
000057461 650_7 $$2WoSType$$aJ
000057461 65320 $$2Author$$aLOV domain
000057461 65320 $$2Author$$aphototropin
000057461 65320 $$2Author$$aflavoprotein
000057461 65320 $$2Author$$aphotoreceptor
000057461 65320 $$2Author$$aChlamydomonas
000057461 65320 $$2Author$$aflavin
000057461 7001_ $$0P:(DE-HGF)0$$aHegemann, P.$$b1
000057461 7001_ $$0P:(DE-HGF)0$$aDick, B.$$b2
000057461 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b3$$uFZJ
000057461 773__ $$0PERI:(DE-600)1480801-8$$0PERI:(DE-600)1480801-8$$a10.1002/bip.20510$$gVol. 82, p. 373 - 378$$p373 - 378$$q82<373 - 378$$tBiopolymers$$v82$$x0006-3525$$y2006
000057461 8567_ $$uhttp://dx.doi.org/10.1002/bip.20510
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000057461 9141_ $$aNachtrag$$y2006
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000057461 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x1
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