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Volumn 73, Issue , 2014, Pages 43-49

Imaging dynamic redox processes with genetically encoded probes

Author keywords

CpYFP; Genetically encoded redox probes; Hydrogen peroxide; RoGFP; Superoxide

Indexed keywords

AMINO TERMINAL SEQUENCE; BIOSENSOR; CELL COMPARTMENTALIZATION; CRYSTAL STRUCTURE; DISULFIDE BOND; GENE MUTATION; GENE PROBE; GENETIC CODE; MOLECULAR IMAGING; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTON TRANSPORT; QUANTUM YIELD; REVIEW; SENSITIVITY AND SPECIFICITY; SIGNAL TRANSDUCTION; STRUCTURAL HOMOLOGY; ANIMAL; HUMAN; METABOLISM;

EID: 84901842374     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2013.12.023     Document Type: Review
Times cited : (56)

References (64)
  • 1
    • 84866929338 scopus 로고    scopus 로고
    • Redox signaling in cardiac physiology and pathology
    • Burgoyne J.R., Mongue-Din H., Eaton P., Shah A.M. Redox signaling in cardiac physiology and pathology. Circ Res 2012, 111:1091-1106.
    • (2012) Circ Res , vol.111 , pp. 1091-1106
    • Burgoyne, J.R.1    Mongue-Din, H.2    Eaton, P.3    Shah, A.M.4
  • 2
    • 84870918882 scopus 로고    scopus 로고
    • Redox control of cardiac rhythm
    • Kapelko V.I. Redox control of cardiac rhythm. Biochemistry (Mosc) 2012, 77:1248-1257.
    • (2012) Biochemistry (Mosc) , vol.77 , pp. 1248-1257
    • Kapelko, V.I.1
  • 3
    • 84878725609 scopus 로고    scopus 로고
    • Oxidative stress in atrial fibrillation: an emerging role of NADPH oxidase
    • Youn J.Y., Zhang J., Zhang Y., Chen H., Liu D., Ping P., et al. Oxidative stress in atrial fibrillation: an emerging role of NADPH oxidase. J Mol Cell Cardiol 2013, 62:72-79.
    • (2013) J Mol Cell Cardiol , vol.62 , pp. 72-79
    • Youn, J.Y.1    Zhang, J.2    Zhang, Y.3    Chen, H.4    Liu, D.5    Ping, P.6
  • 4
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • Finkel T. Signal transduction by reactive oxygen species. J Cell Biol 2011, 194:7-15.
    • (2011) J Cell Biol , vol.194 , pp. 7-15
    • Finkel, T.1
  • 5
    • 84872687926 scopus 로고    scopus 로고
    • Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis
    • Morgan B., Ezerina D., Amoako T.N., Riemer J., Seedorf M., Dick T.P. Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis. Nat Chem Biol 2013, 9:119-125.
    • (2013) Nat Chem Biol , vol.9 , pp. 119-125
    • Morgan, B.1    Ezerina, D.2    Amoako, T.N.3    Riemer, J.4    Seedorf, M.5    Dick, T.P.6
  • 6
    • 82955227412 scopus 로고    scopus 로고
    • In vivo mapping of hydrogen peroxide and oxidized glutathione reveals chemical and regional specificity of redox homeostasis
    • Albrecht S.C., Barata A.G., Grosshans J., Teleman A.A., Dick T.P. In vivo mapping of hydrogen peroxide and oxidized glutathione reveals chemical and regional specificity of redox homeostasis. Cell Metab 2011, 14:819-829.
    • (2011) Cell Metab , vol.14 , pp. 819-829
    • Albrecht, S.C.1    Barata, A.G.2    Grosshans, J.3    Teleman, A.A.4    Dick, T.P.5
  • 7
    • 0035502932 scopus 로고    scopus 로고
    • Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein
    • Ostergaard H., Henriksen A., Hansen F.G., Winther J.R. Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein. EMBO J 2001, 20:5853-5862.
    • (2001) EMBO J , vol.20 , pp. 5853-5862
    • Ostergaard, H.1    Henriksen, A.2    Hansen, F.G.3    Winther, J.R.4
  • 8
    • 84902982320 scopus 로고    scopus 로고
    • Multi-parametric optical analysis of mitochondrial redox signals during neuronal physiology and pathology in vivo
    • in press
    • Breckwoldt M.O., Pfister F., Bradley P.M., Marinković P., Williams P.R., Brill M.S., et al. Multi-parametric optical analysis of mitochondrial redox signals during neuronal physiology and pathology in vivo. Nat Med 2014, in press.
    • (2014) Nat Med
    • Breckwoldt, M.O.1    Pfister, F.2    Bradley, P.M.3    Marinković, P.4    Williams, P.R.5    Brill, M.S.6
  • 9
    • 77954356493 scopus 로고    scopus 로고
    • Fluorescent protein-based redox probes
    • Meyer A.J., Dick T.P. Fluorescent protein-based redox probes. Antioxid Redox Signal 2010, 13:621-650.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 621-650
    • Meyer, A.J.1    Dick, T.P.2
  • 12
    • 84890120295 scopus 로고    scopus 로고
    • Genetically encoded fluorescent redox sensors
    • Lukyanov K.A., Belousov V.V. Genetically encoded fluorescent redox sensors. Biochim Biophys Acta 2014, 1840:745-756.
    • (2014) Biochim Biophys Acta , vol.1840 , pp. 745-756
    • Lukyanov, K.A.1    Belousov, V.V.2
  • 13
    • 84856910091 scopus 로고    scopus 로고
    • Assessment of physiological redox state with novel FRET protein probes
    • Oku M., Sakai Y. Assessment of physiological redox state with novel FRET protein probes. Antioxid Redox Signal 2012, 16:698-704.
    • (2012) Antioxid Redox Signal , vol.16 , pp. 698-704
    • Oku, M.1    Sakai, Y.2
  • 15
    • 33646677239 scopus 로고    scopus 로고
    • Measuring intracellular redox conditions using GFP-based sensors
    • Bjornberg O., Ostergaard H., Winther J.R. Measuring intracellular redox conditions using GFP-based sensors. Antioxid Redox Signal 2006, 8:354-361.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 354-361
    • Bjornberg, O.1    Ostergaard, H.2    Winther, J.R.3
  • 16
    • 0842344106 scopus 로고    scopus 로고
    • Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators
    • Hanson G.T., Aggeler R., Oglesbee D., Cannon M., Capaldi R.A., Tsien R.Y., et al. Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators. J Biol Chem 2004, 279:13044-13053.
    • (2004) J Biol Chem , vol.279 , pp. 13044-13053
    • Hanson, G.T.1    Aggeler, R.2    Oglesbee, D.3    Cannon, M.4    Capaldi, R.A.5    Tsien, R.Y.6
  • 17
    • 2542455473 scopus 로고    scopus 로고
    • Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators
    • Dooley C.T., Dore T.M., Hanson G.T., Jackson W.C., Remington S.J., Tsien R.Y. Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators. J Biol Chem 2004, 279:22284-22293.
    • (2004) J Biol Chem , vol.279 , pp. 22284-22293
    • Dooley, C.T.1    Dore, T.M.2    Hanson, G.T.3    Jackson, W.C.4    Remington, S.J.5    Tsien, R.Y.6
  • 18
    • 3543095148 scopus 로고    scopus 로고
    • Monitoring disulfide bond formation in the eukaryotic cytosol
    • Ostergaard H., Tachibana C., Winther J.R. Monitoring disulfide bond formation in the eukaryotic cytosol. J Cell Biol 2004, 166:337-345.
    • (2004) J Cell Biol , vol.166 , pp. 337-345
    • Ostergaard, H.1    Tachibana, C.2    Winther, J.R.3
  • 19
    • 36349007756 scopus 로고    scopus 로고
    • Redox-sensitive GFP in Arabidopsis thaliana is a quantitative biosensor for the redox potential of the cellular glutathione redox buffer
    • Meyer A.J., Brach T., Marty L., Kreye S., Rouhier N., Jacquot J.P., et al. Redox-sensitive GFP in Arabidopsis thaliana is a quantitative biosensor for the redox potential of the cellular glutathione redox buffer. Plant J 2007, 52:973-986.
    • (2007) Plant J , vol.52 , pp. 973-986
    • Meyer, A.J.1    Brach, T.2    Marty, L.3    Kreye, S.4    Rouhier, N.5    Jacquot, J.P.6
  • 20
  • 25
    • 84880689673 scopus 로고    scopus 로고
    • Spatial and temporal analysis of NADPH oxidase-generated hydrogen peroxide signals by novel fluorescent reporter proteins
    • Enyedi B., Zana M., Donko A., Geiszt M. Spatial and temporal analysis of NADPH oxidase-generated hydrogen peroxide signals by novel fluorescent reporter proteins. Antioxid Redox Signal 2013, 19:523-534.
    • (2013) Antioxid Redox Signal , vol.19 , pp. 523-534
    • Enyedi, B.1    Zana, M.2    Donko, A.3    Geiszt, M.4
  • 26
    • 78650078746 scopus 로고    scopus 로고
    • A highly selective fluorescent probe for visualization of organic hydroperoxides in living cells
    • Zhao B.S., Liang Y., Song Y., Zheng C., Hao Z., Chen P.R. A highly selective fluorescent probe for visualization of organic hydroperoxides in living cells. J Am Chem Soc 2010, 132:17065-17067.
    • (2010) J Am Chem Soc , vol.132 , pp. 17065-17067
    • Zhao, B.S.1    Liang, Y.2    Song, Y.3    Zheng, C.4    Hao, Z.5    Chen, P.R.6
  • 27
    • 80053902441 scopus 로고    scopus 로고
    • Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor
    • Hung Y.P., Albeck J.G., Tantama M., Yellen G. Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor. Cell Metab 2011, 14:545-554.
    • (2011) Cell Metab , vol.14 , pp. 545-554
    • Hung, Y.P.1    Albeck, J.G.2    Tantama, M.3    Yellen, G.4
  • 28
    • 33144474685 scopus 로고    scopus 로고
    • Mechanistic insight provided by glutaredoxin within a fusion to redox-sensitive yellow fluorescent protein
    • Bjornberg O., Ostergaard H., Winther J.R. Mechanistic insight provided by glutaredoxin within a fusion to redox-sensitive yellow fluorescent protein. Biochemistry 2006, 45:2362-2371.
    • (2006) Biochemistry , vol.45 , pp. 2362-2371
    • Bjornberg, O.1    Ostergaard, H.2    Winther, J.R.3
  • 31
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • Choi H., Kim S., Mukhopadhyay P., Cho S., Woo J., Storz G., et al. Structural basis of the redox switch in the OxyR transcription factor. Cell 2001, 105:103-113.
    • (2001) Cell , vol.105 , pp. 103-113
    • Choi, H.1    Kim, S.2    Mukhopadhyay, P.3    Cho, S.4    Woo, J.5    Storz, G.6
  • 32
    • 84890124303 scopus 로고
    • Kinetic and mechanistic considerations to assess the biological fate of peroxynitrite
    • Carballal S., Bartesaghi S., Radi R. Kinetic and mechanistic considerations to assess the biological fate of peroxynitrite. Biochim Biophys Acta 1840, 2014:768-780.
    • (1840) Biochim Biophys Acta , vol.2014 , pp. 768-780
    • Carballal, S.1    Bartesaghi, S.2    Radi, R.3
  • 33
    • 84855948520 scopus 로고    scopus 로고
    • Dynamic measurements of mitochondrial hydrogen peroxide concentration and glutathione redox state in rat pancreatic beta-cells using ratiometric fluorescent proteins: confounding effects of pH with HyPer but not roGFP1
    • Roma L.P., Duprez J., Takahashi H.K., Gilon P., Wiederkehr A., Jonas J.C. Dynamic measurements of mitochondrial hydrogen peroxide concentration and glutathione redox state in rat pancreatic beta-cells using ratiometric fluorescent proteins: confounding effects of pH with HyPer but not roGFP1. Biochem J 2012, 441:971-978.
    • (2012) Biochem J , vol.441 , pp. 971-978
    • Roma, L.P.1    Duprez, J.2    Takahashi, H.K.3    Gilon, P.4    Wiederkehr, A.5    Jonas, J.C.6
  • 34
    • 0033613235 scopus 로고    scopus 로고
    • Circular permutation and receptor insertion within green fluorescent proteins
    • Baird G.S., Zacharias D.A., Tsien R.Y. Circular permutation and receptor insertion within green fluorescent proteins. Proc Natl Acad Sci U S A 1999, 96:11241-11246.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11241-11246
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 35
    • 79952412095 scopus 로고    scopus 로고
    • Dynamic regulation of the mitochondrial proton gradient during cytosolic calcium elevations
    • Poburko D., Santo-Domingo J., Demaurex N. Dynamic regulation of the mitochondrial proton gradient during cytosolic calcium elevations. J Biol Chem 2011, 286:11672-11684.
    • (2011) J Biol Chem , vol.286 , pp. 11672-11684
    • Poburko, D.1    Santo-Domingo, J.2    Demaurex, N.3
  • 36
    • 84863996302 scopus 로고    scopus 로고
    • Perspectives on: SGP symposium on mitochondrial physiology and medicine: the renaissance of mitochondrial pH
    • Santo-Domingo J., Demaurex N. Perspectives on: SGP symposium on mitochondrial physiology and medicine: the renaissance of mitochondrial pH. J Gen Physiol 2012, 139:415-423.
    • (2012) J Gen Physiol , vol.139 , pp. 415-423
    • Santo-Domingo, J.1    Demaurex, N.2
  • 37
    • 82455174380 scopus 로고    scopus 로고
    • Selective ion changes during spontaneous mitochondrial transients in intact astrocytes
    • Azarias G., Chatton J.Y. Selective ion changes during spontaneous mitochondrial transients in intact astrocytes. PLoS One 2011, 6:e28505.
    • (2011) PLoS One , vol.6
    • Azarias, G.1    Chatton, J.Y.2
  • 38
    • 47549096022 scopus 로고    scopus 로고
    • Superoxide flashes in single mitochondria
    • Wang W., Fang H., Groom L., Cheng A., Zhang W., Liu J., et al. Superoxide flashes in single mitochondria. Cell 2008, 134:279-290.
    • (2008) Cell , vol.134 , pp. 279-290
    • Wang, W.1    Fang, H.2    Groom, L.3    Cheng, A.4    Zhang, W.5    Liu, J.6
  • 39
    • 84862795098 scopus 로고    scopus 로고
    • Superoxide flashes: elemental events of mitochondrial ROS signaling in the heart
    • Wang X., Jian C., Zhang X., Huang Z., Xu J., Hou T., et al. Superoxide flashes: elemental events of mitochondrial ROS signaling in the heart. J Mol Cell Cardiol 2012, 52:940-948.
    • (2012) J Mol Cell Cardiol , vol.52 , pp. 940-948
    • Wang, X.1    Jian, C.2    Zhang, X.3    Huang, Z.4    Xu, J.5    Hou, T.6
  • 41
    • 79960209663 scopus 로고    scopus 로고
    • The circularly permuted yellow fluorescent protein cpYFP that has been used as a superoxide probe is highly responsive to pH but not superoxide in mitochondria: implications for the existence of superoxide 'flashes'
    • Schwarzlander M., Logan D.C., Fricker M.D., Sweetlove L.J. The circularly permuted yellow fluorescent protein cpYFP that has been used as a superoxide probe is highly responsive to pH but not superoxide in mitochondria: implications for the existence of superoxide 'flashes'. Biochem J 2011, 437:381-387.
    • (2011) Biochem J , vol.437 , pp. 381-387
    • Schwarzlander, M.1    Logan, D.C.2    Fricker, M.D.3    Sweetlove, L.J.4
  • 42
    • 84870803043 scopus 로고    scopus 로고
    • Mitochondria-targeted cpYFP: pH or superoxide sensor?
    • Quatresous E., Legrand C., Pouvreau S. Mitochondria-targeted cpYFP: pH or superoxide sensor?. J Gen Physiol 2012, 140:567-570.
    • (2012) J Gen Physiol , vol.140 , pp. 567-570
    • Quatresous, E.1    Legrand, C.2    Pouvreau, S.3
  • 44
    • 84880213863 scopus 로고    scopus 로고
    • OPA1 promotes pH flashes that spread between contiguous mitochondria without matrix protein exchange
    • Santo-Domingo J., Giacomello M., Poburko D., Scorrano L., Demaurex N. OPA1 promotes pH flashes that spread between contiguous mitochondria without matrix protein exchange. EMBO J 2013, 32:1927-1940.
    • (2013) EMBO J , vol.32 , pp. 1927-1940
    • Santo-Domingo, J.1    Giacomello, M.2    Poburko, D.3    Scorrano, L.4    Demaurex, N.5
  • 45
    • 84876213335 scopus 로고    scopus 로고
    • Respective contribution of mitochondrial superoxide and pH to mitochondria-targeted circularly permuted yellow fluorescent protein (mt-cpYFP) flash activity
    • Wei-LaPierre L., Gong G., Gerstner B.J., Ducreux S., Yule D.I., Pouvreau S., et al. Respective contribution of mitochondrial superoxide and pH to mitochondria-targeted circularly permuted yellow fluorescent protein (mt-cpYFP) flash activity. J Biol Chem 2013, 288:10567-10577.
    • (2013) J Biol Chem , vol.288 , pp. 10567-10577
    • Wei-LaPierre, L.1    Gong, G.2    Gerstner, B.J.3    Ducreux, S.4    Yule, D.I.5    Pouvreau, S.6
  • 46
    • 84880274705 scopus 로고    scopus 로고
    • Superoxide constitutes a major signal of mitochondrial superoxide flash
    • Zhang X., Huang Z., Hou T., Xu J., Wang Y., Shang W., et al. Superoxide constitutes a major signal of mitochondrial superoxide flash. Life Sci 2013, 93:178-186.
    • (2013) Life Sci , vol.93 , pp. 178-186
    • Zhang, X.1    Huang, Z.2    Hou, T.3    Xu, J.4    Wang, Y.5    Shang, W.6
  • 47
    • 33646698671 scopus 로고    scopus 로고
    • Hydrogen peroxide: a signaling messenger
    • Stone J.R., Yang S. Hydrogen peroxide: a signaling messenger. Antioxid Redox Signal 2006, 8:243-270.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 243-270
    • Stone, J.R.1    Yang, S.2
  • 48
    • 16544369973 scopus 로고    scopus 로고
    • Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path
    • Lee C., Lee S.M., Mukhopadhyay P., Kim S.J., Lee S.C., Ahn W.S., et al. Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path. Nat Struct Mol Biol 2004, 11:1179-1185.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1179-1185
    • Lee, C.1    Lee, S.M.2    Mukhopadhyay, P.3    Kim, S.J.4    Lee, S.C.5    Ahn, W.S.6
  • 49
    • 0034674055 scopus 로고    scopus 로고
    • 2 gradients across biomembranes
    • 2 gradients across biomembranes. FEBS Lett 2000, 475:121-126.
    • (2000) FEBS Lett , vol.475 , pp. 121-126
    • Antunes, F.1    Cadenas, E.2
  • 50
    • 34249703509 scopus 로고    scopus 로고
    • The high reactivity of peroxiredoxin 2 with H(2)O(2) is not reflected in its reaction with other oxidants and thiol reagents
    • Peskin A.V., Low F.M., Paton L.N., Maghzal G.J., Hampton M.B., Winterbourn C.C. The high reactivity of peroxiredoxin 2 with H(2)O(2) is not reflected in its reaction with other oxidants and thiol reagents. J Biol Chem 2007, 282:11885-11892.
    • (2007) J Biol Chem , vol.282 , pp. 11885-11892
    • Peskin, A.V.1    Low, F.M.2    Paton, L.N.3    Maghzal, G.J.4    Hampton, M.B.5    Winterbourn, C.C.6
  • 52
    • 33947204162 scopus 로고    scopus 로고
    • Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte
    • Low F.M., Hampton M.B., Peskin A.V., Winterbourn C.C. Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte. Blood 2007, 109:2611-2617.
    • (2007) Blood , vol.109 , pp. 2611-2617
    • Low, F.M.1    Hampton, M.B.2    Peskin, A.V.3    Winterbourn, C.C.4
  • 54
    • 84877953147 scopus 로고    scopus 로고
    • Real-time imaging of NADPH oxidase activity in living cells using a novel fluorescent protein reporter
    • Pal R., Basu Thakur P., Li S., Minard C., Rodney G.G. Real-time imaging of NADPH oxidase activity in living cells using a novel fluorescent protein reporter. PLoS One 2013, 8:e63989.
    • (2013) PLoS One , vol.8
    • Pal, R.1    Basu Thakur, P.2    Li, S.3    Minard, C.4    Rodney, G.G.5
  • 55
    • 33644872102 scopus 로고    scopus 로고
    • The oxidation of 2',7'-dichlorofluorescin to reactive oxygen species: a self-fulfilling prophesy?
    • Bonini M.G., Rota C., Tomasi A., Mason R.P. The oxidation of 2',7'-dichlorofluorescin to reactive oxygen species: a self-fulfilling prophesy?. Free Radic Biol Med 2006, 40:968-975.
    • (2006) Free Radic Biol Med , vol.40 , pp. 968-975
    • Bonini, M.G.1    Rota, C.2    Tomasi, A.3    Mason, R.P.4
  • 56
    • 84862215205 scopus 로고    scopus 로고
    • Reaction-based genetically encoded fluorescent hydrogen sulfide sensors
    • Chen S., Chen Z.J., Ren W., Ai H.W. Reaction-based genetically encoded fluorescent hydrogen sulfide sensors. J Am Chem Soc 2012, 134:9589-9592.
    • (2012) J Am Chem Soc , vol.134 , pp. 9589-9592
    • Chen, S.1    Chen, Z.J.2    Ren, W.3    Ai, H.W.4
  • 57
    • 84885584704 scopus 로고    scopus 로고
    • Genetically encoded fluorescent probe for the selective detection of peroxynitrite
    • Chen Z.J., Ren W., Wright Q.E., Ai H.W. Genetically encoded fluorescent probe for the selective detection of peroxynitrite. J Am Chem Soc 2013, 135:14940-14943.
    • (2013) J Am Chem Soc , vol.135 , pp. 14940-14943
    • Chen, Z.J.1    Ren, W.2    Wright, Q.E.3    Ai, H.W.4
  • 61
    • 84859164120 scopus 로고    scopus 로고
    • Toxicity of 6-hydroxydopamine: live cell imaging of cytoplasmic redox flux
    • Dooley C.T., Li L., Misler J.A., Thompson J.H. Toxicity of 6-hydroxydopamine: live cell imaging of cytoplasmic redox flux. Cell Biol Toxicol 2012, 28:89-101.
    • (2012) Cell Biol Toxicol , vol.28 , pp. 89-101
    • Dooley, C.T.1    Li, L.2    Misler, J.A.3    Thompson, J.H.4
  • 62
    • 84861232254 scopus 로고    scopus 로고
    • Determination of the in vivo redox potential by one-wavelength spectro-microscopy of roGFP
    • Wierer S., Peter S., Elgass K., Mack H.G., Bieker S., Meixner A.J., et al. Determination of the in vivo redox potential by one-wavelength spectro-microscopy of roGFP. Anal Bioanal Chem 2012, 403:737-744.
    • (2012) Anal Bioanal Chem , vol.403 , pp. 737-744
    • Wierer, S.1    Peter, S.2    Elgass, K.3    Mack, H.G.4    Bieker, S.5    Meixner, A.J.6
  • 63
    • 84876716167 scopus 로고    scopus 로고
    • Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox
    • Avezov E., Cross B.C., Kaminski Schierle G.S., Winters M., Harding H.P., Melo E.P., et al. Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox. J Cell Biol 2013, 201:337-349.
    • (2013) J Cell Biol , vol.201 , pp. 337-349
    • Avezov, E.1    Cross, B.C.2    Kaminski Schierle, G.S.3    Winters, M.4    Harding, H.P.5    Melo, E.P.6
  • 64
    • 84877986773 scopus 로고    scopus 로고
    • Endoplasmic reticulum: reduced and oxidized glutathione revisited
    • Birk J., Meyer M., Aller I., Hansen H.G., Odermatt A., Dick T.P., et al. Endoplasmic reticulum: reduced and oxidized glutathione revisited. J Cell Sci 2013, 126:1604-1617.
    • (2013) J Cell Sci , vol.126 , pp. 1604-1617
    • Birk, J.1    Meyer, M.2    Aller, I.3    Hansen, H.G.4    Odermatt, A.5    Dick, T.P.6


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