메뉴 건너뛰기




Volumn , Issue , 2014, Pages

Linking peroxiredoxin and vacuolar-ATPase functions in calorie restriction-mediated life span extension

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; FREE RADICAL; GLUCOSE; HYDROGEN PEROXIDE; IRON; PEROXIDE; PEROXIREDOXIN; REACTIVE OXYGEN METABOLITE;

EID: 84896880111     PISSN: 16878876     EISSN: 16878884     Source Type: Journal    
DOI: 10.1155/2014/913071     Document Type: Review
Times cited : (21)

References (122)
  • 1
    • 77950214581 scopus 로고    scopus 로고
    • Lessons on longevity from budding yeast
    • 2-s2.0-77950214581 10.1038/nature08981
    • Kaeberlein M., Lessons on longevity from budding yeast. Nature 2010 464 7288 513 519 2-s2.0-77950214581 10.1038/nature08981
    • (2010) Nature , vol.464 , Issue.7288 , pp. 513-519
    • Kaeberlein, M.1
  • 2
    • 77956244148 scopus 로고    scopus 로고
    • A pathway that links reproductive status to lifespan in Caenorhabditis elegans
    • 2-s2.0-77956244148 10.1111/j.1749-6632.2010.05640.x
    • Kenyon C., A pathway that links reproductive status to lifespan in Caenorhabditis elegans. Annals of the New York Academy of Sciences 2010 1204 156 162 2-s2.0-77956244148 10.1111/j.1749-6632.2010.05640.x
    • (2010) Annals of the New York Academy of Sciences , vol.1204 , pp. 156-162
    • Kenyon, C.1
  • 3
    • 77953790156 scopus 로고    scopus 로고
    • Honoring Clive McCay and 75 years of calorie restriction research
    • 2-s2.0-77953790156 10.3945/jn.110.122804
    • McDonald R. B., Ramsey J. J., Honoring Clive McCay and 75 years of calorie restriction research. Journal of Nutrition 2010 140 7 1205 1210 2-s2.0-77953790156 10.3945/jn.110.122804
    • (2010) Journal of Nutrition , vol.140 , Issue.7 , pp. 1205-1210
    • McDonald, R.B.1    Ramsey, J.J.2
  • 4
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and SIR2 for life-span extension by calorie restriction in saccharomyces cerevisiae
    • 2-s2.0-0034703217 10.1126/science.289.5487.2126
    • Lin S.-J., Defossez P.-A., Guarente L., Requirement of NAD and SIR2 for life-span extension by calorie restriction in saccharomyces cerevisiae. Science 2000 289 5487 2126 2128 2-s2.0-0034703217 10.1126/science.289.5487.2126
    • (2000) Science , vol.289 , Issue.5487 , pp. 2126-2128
    • Lin, S.-J.1    Defossez, P.-A.2    Guarente, L.3
  • 5
    • 0033738362 scopus 로고    scopus 로고
    • An intervention resembling caloric restriction prolongs life span and retards aging in yeast
    • 2-s2.0-0033738362
    • Jiang J. C., Jaruga E., Repnevskaya M. V., Jazwinski S. M., An intervention resembling caloric restriction prolongs life span and retards aging in yeast. FASEB Journal 2000 14 14 2135 2137 2-s2.0-0033738362
    • (2000) FASEB Journal , vol.14 , Issue.14 , pp. 2135-2137
    • Jiang, J.C.1    Jaruga, E.2    Repnevskaya, M.V.3    Jazwinski, S.M.4
  • 7
    • 19344374925 scopus 로고    scopus 로고
    • Sir2-independent life span extension by calorie restriction in yeast
    • 2-s2.0-19344374925 10.1371/journal.pbio.0020296
    • Kaeberlein M., Kirkland K. T., Fields S., Kennedy B. K., Sir2-independent life span extension by calorie restriction in yeast. PLoS Biology 2004 2 9, e296 2-s2.0-19344374925 10.1371/journal.pbio.0020296
    • (2004) PLoS Biology , vol.2 , Issue.9 E296
    • Kaeberlein, M.1    Kirkland, K.T.2    Fields, S.3    Kennedy, B.K.4
  • 8
    • 77951176737 scopus 로고    scopus 로고
    • Extending healthy life span-from yeast to humans
    • 2-s2.0-77951176737 10.1126/science.1172539
    • Fontana L., Partridge L., Longo V. D., Extending healthy life span-from yeast to humans. Science 2010 328 5976 321 326 2-s2.0-77951176737 10.1126/science.1172539
    • (2010) Science , vol.328 , Issue.5976 , pp. 321-326
    • Fontana, L.1    Partridge, L.2    Longo, V.D.3
  • 10
    • 58549084410 scopus 로고    scopus 로고
    • How Saccharomyces responds to nutrients
    • 2-s2.0-58549084410 10.1146/annurev.genet.41.110306.130206
    • Zaman S., Lippman S. I., Zhao X., Broach J. R., How Saccharomyces responds to nutrients. Annual Review of Genetics 2008 42 27 81 2-s2.0-58549084410 10.1146/annurev.genet.41.110306.130206
    • (2008) Annual Review of Genetics , vol.42 , pp. 27-81
    • Zaman, S.1    Lippman, S.I.2    Zhao, X.3    Broach, J.R.4
  • 11
    • 84871011474 scopus 로고    scopus 로고
    • An early age increase in vacuolar pH limits mitochondrial function and lifespan in yeast
    • Hughes A. L., Gottschling D. E., An early age increase in vacuolar pH limits mitochondrial function and lifespan in yeast. Nature 2012 492 7428 261 265
    • (2012) Nature , vol.492 , Issue.7428 , pp. 261-265
    • Hughes, A.L.1    Gottschling, D.E.2
  • 12
    • 80052217019 scopus 로고    scopus 로고
    • 2 resistance elicited by caloric restriction require the peroxiredoxin Tsa1 in Saccharomyces cerevisiae
    • 2-s2.0-80052217019 10.1016/j.molcel.2011.07.027
    • 2 resistance elicited by caloric restriction require the peroxiredoxin Tsa1 in Saccharomyces cerevisiae. Molecular Cell 2011 43 5 823 833 2-s2.0-80052217019 10.1016/j.molcel.2011.07.027
    • (2011) Molecular Cell , vol.43 , Issue.5 , pp. 823-833
    • Molin, M.1    Yang, J.2    Hanzén, S.3    Toledano, M.B.4    Labarre, J.5    Nyström, T.6
  • 13
    • 84859704385 scopus 로고    scopus 로고
    • Leucyl-tRNA synthetase controls TORC1 via the EGO complex
    • 2-s2.0-84859704385 10.1016/j.molcel.2012.02.009
    • Bonfils G., Jaquenoud M., Bontron S., Ostrowicz C., Ungermann C., De Virgilio C., Leucyl-tRNA synthetase controls TORC1 via the EGO complex. Molecular Cell 2012 46 1 105 110 2-s2.0-84859704385 10.1016/j.molcel.2012.02.009
    • (2012) Molecular Cell , vol.46 , Issue.1 , pp. 105-110
    • Bonfils, G.1    Jaquenoud, M.2    Bontron, S.3    Ostrowicz, C.4    Ungermann, C.5    De Virgilio, C.6
  • 14
    • 77955405903 scopus 로고    scopus 로고
    • Cytosolic pH is a second messenger for glucose and regulates the PKA pathway through V-ATPase
    • 2-s2.0-77955405903 10.1038/emboj.2010.138
    • Dechant R., Binda M., Lee S. S., Pelet S., Winderickx J., Peter M., Cytosolic pH is a second messenger for glucose and regulates the PKA pathway through V-ATPase. EMBO Journal 2010 29 15 2515 2526 2-s2.0-77955405903 10.1038/emboj.2010.138
    • (2010) EMBO Journal , vol.29 , Issue.15 , pp. 2515-2526
    • Dechant, R.1    Binda, M.2    Lee, S.S.3    Pelet, S.4    Winderickx, J.5    Peter, M.6
  • 15
    • 80555143078 scopus 로고    scopus 로고
    • MTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H+-ATPase
    • 2-s2.0-80555143078 10.1126/science.1207056
    • Zoncu R., Bar-Peled L., Efeyan A., Wang S., Sancak Y., Sabatini D. M., mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H+-ATPase. Science 2011 334 6056 678 683 2-s2.0-80555143078 10.1126/science.1207056
    • (2011) Science , vol.334 , Issue.6056 , pp. 678-683
    • Zoncu, R.1    Bar-Peled, L.2    Efeyan, A.3    Wang, S.4    Sancak, Y.5    Sabatini, D.M.6
  • 16
    • 84866648366 scopus 로고    scopus 로고
    • Genome-wide analysis of intracellular pH reveals quantitative control of cell division rate by pH(c) in Saccharomyces cerevisiae
    • Orij R., Urbanus M. L., Vizeacoumar F. J., Giaever G., Boone C., Nislow C., Brul S., Smits G. J., Genome-wide analysis of intracellular pH reveals quantitative control of cell division rate by pH(c) in Saccharomyces cerevisiae. Genome Biology 2012 13 9, article R80
    • (2012) Genome Biology , vol.13 , Issue.9 ARTICLE R80
    • Orij, R.1    Urbanus, M.L.2    Vizeacoumar, F.J.3    Giaever, G.4    Boone, C.5    Nislow, C.6    Brul, S.7    Smits, G.J.8
  • 17
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • 2-s2.0-34648813720 10.1038/nrm2256
    • D'Autréaux B., Toledano M. B., ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nature Reviews Molecular Cell Biology 2007 8 10 813 824 2-s2.0-34648813720 10.1038/nrm2256
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.10 , pp. 813-824
    • D'Autréaux, B.1    Toledano, M.B.2
  • 18
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • 2-s2.0-0026795635
    • Stadtman E. R., Protein oxidation and aging. Science 1992 257 5074 1220 1224 2-s2.0-0026795635
    • (1992) Science , vol.257 , Issue.5074 , pp. 1220-1224
    • Stadtman, E.R.1
  • 19
    • 0142213542 scopus 로고    scopus 로고
    • The free radical theory of aging
    • 2-s2.0-0142213542
    • Harman D., The free radical theory of aging. Antioxidants and Redox Signaling 2003 5 5 557 561 2-s2.0-0142213542
    • (2003) Antioxidants and Redox Signaling , vol.5 , Issue.5 , pp. 557-561
    • Harman, D.1
  • 20
    • 34547410267 scopus 로고    scopus 로고
    • Sir2p-dependent protein segregation gives rise to a superior reactive oxygen species management in the progeny of Saccharomyces cerevisiae
    • 2-s2.0-34547410267 10.1073/pnas.0701634104
    • Erjavec N., Nyström T., Sir2p-dependent protein segregation gives rise to a superior reactive oxygen species management in the progeny of Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences of the United States of America 2007 104 26 10877 10881 2-s2.0-34547410267 10.1073/pnas.0701634104
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.26 , pp. 10877-10881
    • Erjavec, N.1    Nyström, T.2
  • 21
    • 0035100306 scopus 로고    scopus 로고
    • Aged mother cells of Saccharomyces cerevisiae show markers of oxidative stress and apoptosis
    • 2-s2.0-0035100306 10.1046/j.1365-2958.2001.02317.x
    • Laun P., Pichova A., Madeo F., Fuchs J., Ellinger A., Kohlwein S., Dawes I., Fröhlich K.-U., Breitenbach M., Aged mother cells of Saccharomyces cerevisiae show markers of oxidative stress and apoptosis. Molecular Microbiology 2001 39 5 1166 1173 2-s2.0-0035100306 10.1046/j.1365-2958.2001. 02317.x
    • (2001) Molecular Microbiology , vol.39 , Issue.5 , pp. 1166-1173
    • Laun, P.1    Pichova, A.2    Madeo, F.3    Fuchs, J.4    Ellinger, A.5    Kohlwein, S.6    Dawes, I.7    Fröhlich, K.-U.8    Breitenbach, M.9
  • 23
    • 80054862809 scopus 로고    scopus 로고
    • Grape seed proanthocyanidin lowers brain oxidative stress in adult and middle-aged rats
    • 2-s2.0-80054862809 10.1016/j.exger.2011.08.006
    • Asha Devi S., Sagar Chandrasekar B. K., Manjula K. R., Ishii N., Grape seed proanthocyanidin lowers brain oxidative stress in adult and middle-aged rats. Experimental Gerontology 2011 46 11 958 964 2-s2.0-80054862809 10.1016/j.exger.2011.08.006
    • (2011) Experimental Gerontology , vol.46 , Issue.11 , pp. 958-964
    • Asha Devi, S.1    Sagar Chandrasekar, B.K.2    Manjula, K.R.3    Ishii, N.4
  • 24
    • 27744510901 scopus 로고    scopus 로고
    • Lipid peroxidation and the aging process
    • Pratico D., Lipid peroxidation and the aging process. Science of Aging Knowledge Environment 2002 2002 50, article re5
    • (2002) Science of Aging Knowledge Environment , vol.2002 , Issue.50 ARTICLE RE5
    • Pratico, D.1
  • 26
    • 79953024462 scopus 로고    scopus 로고
    • Assessment of chronological lifespan dependent molecular damages in yeast lacking mitochondrial antioxidant genes
    • 2-s2.0-79953024462 10.1016/j.bbrc.2010.08.019
    • Demir A. B., Koc A., Assessment of chronological lifespan dependent molecular damages in yeast lacking mitochondrial antioxidant genes. Biochemical and Biophysical Research Communications 2010 400 1 106 110 2-s2.0-79953024462 10.1016/j.bbrc.2010.08.019
    • (2010) Biochemical and Biophysical Research Communications , vol.400 , Issue.1 , pp. 106-110
    • Demir, A.B.1    Koc, A.2
  • 28
    • 0028342438 scopus 로고
    • Oxidative damage, mitochondrial oxidant generation and antioxidant defenses: During aging and in response to food restriction in the mouse
    • 2-s2.0-0028342438 10.1016/0047-6374(94)90104-X
    • Sohal R. S., Kua H.-H., Agarwal S., Forster M. J., Lal H., Oxidative damage, mitochondrial oxidant generation and antioxidant defenses: during aging and in response to food restriction in the mouse. Mechanisms of Ageing and Development 1994 74 1-2 121 133 2-s2.0-0028342438 10.1016/0047-6374(94)90104-X
    • (1994) Mechanisms of Ageing and Development , vol.74 , Issue.1-2 , pp. 121-133
    • Sohal, R.S.1    Kua, H.-H.2    Agarwal, S.3    Forster, M.J.4    Lal, H.5
  • 29
    • 0030038103 scopus 로고    scopus 로고
    • Oxidative stress, caloric restriction, and aging
    • 2-s2.0-0030038103
    • Sohal R. S., Weindruch R., Oxidative stress, caloric restriction, and aging. Science 1996 273 5271 59 63 2-s2.0-0030038103
    • (1996) Science , vol.273 , Issue.5271 , pp. 59-63
    • Sohal, R.S.1    Weindruch, R.2
  • 30
    • 58149157465 scopus 로고    scopus 로고
    • Molecular bases of caloric restriction regulation of neuronal synaptic plasticity
    • 2-s2.0-58149157465 10.1007/s12035-008-8040-1
    • Fontán-Lozano A., López-Lluch G., Delgado-García J. M., Navas P., Carrión A. M., Molecular bases of caloric restriction regulation of neuronal synaptic plasticity. Molecular Neurobiology 2008 38 2 167 177 2-s2.0-58149157465 10.1007/s12035-008-8040-1
    • (2008) Molecular Neurobiology , vol.38 , Issue.2 , pp. 167-177
    • Fontán-Lozano, A.1    López-Lluch, G.2    Delgado-García, J.M.3    Navas, P.4    Carrión, A.M.5
  • 31
    • 40149092156 scopus 로고    scopus 로고
    • Sirt1 protects the heart from aging and stress
    • 2-s2.0-40149092156 10.1515/BC.2008.032
    • Hsu C.-P., Odewale I., Alcendor R. R., Sadoshima J., Sirt1 protects the heart from aging and stress. Biological Chemistry 2008 389 3 221 231 2-s2.0-40149092156 10.1515/BC.2008.032
    • (2008) Biological Chemistry , vol.389 , Issue.3 , pp. 221-231
    • Hsu, C.-P.1    Odewale, I.2    Alcendor, R.R.3    Sadoshima, J.4
  • 32
    • 0036569401 scopus 로고    scopus 로고
    • Carbonyl modified proteins in cellular regulation, aging, and disease
    • 2-s2.0-0036569401 10.1016/S0891-5849(02)00765-7
    • Levine R. L., Carbonyl modified proteins in cellular regulation, aging, and disease. Free Radical Biology and Medicine 2002 32 9 790 796 2-s2.0-0036569401 10.1016/S0891-5849(02)00765-7
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.9 , pp. 790-796
    • Levine, R.L.1
  • 33
    • 0028116159 scopus 로고
    • Effect of age and caloric restriction on DNA oxidative damage in different tissues of C57BL/6 mice
    • 2-s2.0-0028116159 10.1016/0047-6374(94)91595-4
    • Sohal R. S., Agarwal S., Candas M., Forster M. J., Lal H., Effect of age and caloric restriction on DNA oxidative damage in different tissues of C57BL/6 mice. Mechanisms of Ageing and Development 1994 76 2-3 215 224 2-s2.0-0028116159 10.1016/0047-6374(94)91595-4
    • (1994) Mechanisms of Ageing and Development , vol.76 , Issue.2-3 , pp. 215-224
    • Sohal, R.S.1    Agarwal, S.2    Candas, M.3    Forster, M.J.4    Lal, H.5
  • 34
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • 2-s2.0-0034626735 10.1038/35041687
    • Finkel T., Holbrook N. J., Oxidants, oxidative stress and the biology of ageing. Nature 2000 408 6809 239 247 2-s2.0-0034626735 10.1038/35041687
    • (2000) Nature , vol.408 , Issue.6809 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 35
    • 79151477025 scopus 로고    scopus 로고
    • Direct interaction between Tks proteins and the N-terminal proline-rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation
    • 2-s2.0-79151477025 10.1016/j.ejcb.2010.05.007
    • Gianni D., DerMardirossian C., Bokoch G. M., Direct interaction between Tks proteins and the N-terminal proline-rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation. European Journal of Cell Biology 2011 90 2-3 164 171 2-s2.0-79151477025 10.1016/j.ejcb.2010.05.007
    • (2011) European Journal of Cell Biology , vol.90 , Issue.2-3 , pp. 164-171
    • Gianni, D.1    Dermardirossian, C.2    Bokoch, G.M.3
  • 36
    • 34250011458 scopus 로고    scopus 로고
    • Ionizing radiation induces a Yap1-dependent peroxide stress response in yeast
    • 2-s2.0-34250011458 10.1016/j.freeradbiomed.2007.04.007
    • Molin M., Renault J.-P., Lagniel G., Pin S., Toledano M., Labarre J., Ionizing radiation induces a Yap1-dependent peroxide stress response in yeast. Free Radical Biology and Medicine 2007 43 1 136 144 2-s2.0-34250011458 10.1016/j.freeradbiomed.2007.04.007
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.1 , pp. 136-144
    • Molin, M.1    Renault, J.-P.2    Lagniel, G.3    Pin, S.4    Toledano, M.5    Labarre, J.6
  • 38
    • 84885211241 scopus 로고    scopus 로고
    • Role of reactive oxygen species-mediated signaling in aging
    • Labunskyy V. M., Gladyshev V. N., Role of reactive oxygen species-mediated signaling in aging. Antioxidants & Redox Signaling 2013 19 12 1362 1372
    • (2013) Antioxidants & Redox Signaling , vol.19 , Issue.12 , pp. 1362-1372
    • Labunskyy, V.M.1    Gladyshev, V.N.2
  • 39
    • 79959350253 scopus 로고    scopus 로고
    • Extending life span by increasing oxidative stress
    • 2-s2.0-79959350253 10.1016/j.freeradbiomed.2011.05.010
    • Ristow M., Schmeisser S., Extending life span by increasing oxidative stress. Free Radical Biology and Medicine 2011 51 2 327 336 2-s2.0-79959350253 10.1016/j.freeradbiomed.2011.05.010
    • (2011) Free Radical Biology and Medicine , vol.51 , Issue.2 , pp. 327-336
    • Ristow, M.1    Schmeisser, S.2
  • 41
    • 33748775173 scopus 로고    scopus 로고
    • Dual role of peroxiredoxin i in macrophage-derived foam cells
    • 2-s2.0-33748775173 10.1074/jbc.M605026200
    • Conway J. P., Kinter M., Dual role of peroxiredoxin I in macrophage-derived foam cells. Journal of Biological Chemistry 2006 281 38 27991 28001 2-s2.0-33748775173 10.1074/jbc.M605026200
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.38 , pp. 27991-28001
    • Conway, J.P.1    Kinter, M.2
  • 43
    • 77954382142 scopus 로고    scopus 로고
    • 2 mediates endoplasmic reticulum signaling through local ras activation
    • 2-s2.0-77954382142 10.1128/MCB.01445-09
    • 2 mediates endoplasmic reticulum signaling through local ras activation. Molecular and Cellular Biology 2010 30 14 3553 3568 2-s2.0-77954382142 10.1128/MCB.01445-09
    • (2010) Molecular and Cellular Biology , vol.30 , Issue.14 , pp. 3553-3568
    • Wu, R.-F.1    Ma, Z.2    Liu, Z.3    Terada, L.S.4
  • 45
    • 0037130175 scopus 로고    scopus 로고
    • Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration
    • 2-s2.0-0037130175 10.1038/nature00829
    • Lin S.-J., Kaeberlein M., Andalis A. A., Sturtz L. A., Defossez P.-A., Culotta V. C., Fink G. R., Guarente L., Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration. Nature 2002 418 6895 344 348 2-s2.0-0037130175 10.1038/nature00829
    • (2002) Nature , vol.418 , Issue.6895 , pp. 344-348
    • Lin, S.-J.1    Kaeberlein, M.2    Andalis, A.A.3    Sturtz, L.A.4    Defossez, P.-A.5    Culotta, V.C.6    Fink, G.R.7    Guarente, L.8
  • 46
    • 84888134441 scopus 로고    scopus 로고
    • Molecular mechanisms underlying genotype-dependent responses to dietary restriction
    • Schleit J., Johnson S. C., Bennett C. F., Molecular mechanisms underlying genotype-dependent responses to dietary restriction. Aging Cell 2013 12 6 1050 1061
    • (2013) Aging Cell , vol.12 , Issue.6 , pp. 1050-1061
    • Schleit, J.1    Johnson, S.C.2    Bennett, C.F.3
  • 48
    • 34748850786 scopus 로고    scopus 로고
    • Glucose restriction extends caenorhabditis elegans life span by inducing mitochondrial respiration and increasing oxidative stress
    • 2-s2.0-34748850786 10.1016/j.cmet.2007.08.011
    • Schulz T. J., Zarse K., Voigt A., Urban N., Birringer M., Ristow M., Glucose restriction extends caenorhabditis elegans life span by inducing mitochondrial respiration and increasing oxidative stress. Cell Metabolism 2007 6 4 280 293 2-s2.0-34748850786 10.1016/j.cmet.2007.08.011
    • (2007) Cell Metabolism , vol.6 , Issue.4 , pp. 280-293
    • Schulz, T.J.1    Zarse, K.2    Voigt, A.3    Urban, N.4    Birringer, M.5    Ristow, M.6
  • 49
    • 10944237769 scopus 로고    scopus 로고
    • Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine
    • 2-s2.0-10944237769 10.1074/jbc.M409482200
    • Chang T.-S., Jeong W., Hyun A. W., Sun M. L., Park S., Sue G. R., Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. Journal of Biological Chemistry 2004 279 49 50994 51001 2-s2.0-10944237769 10.1074/jbc.M409482200
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 50994-51001
    • Chang, T.-S.1    Jeong, W.2    Hyun, A.W.3    Sun, M.L.4    Park, S.5    Sue, G.R.6
  • 51
    • 0024604234 scopus 로고
    • An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: Genetic characterization and cloning of ahp
    • 2-s2.0-0024604234
    • Storz G., Jacobson F. S., Tartaglia L. A., Morgan R. W., Silveira L. A., Ames B. N., An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp. Journal of Bacteriology 1989 171 4 2049 2055 2-s2.0-0024604234
    • (1989) Journal of Bacteriology , vol.171 , Issue.4 , pp. 2049-2055
    • Storz, G.1    Jacobson, F.S.2    Tartaglia, L.A.3    Morgan, R.W.4    Silveira, L.A.5    Ames, B.N.6
  • 52
    • 13544272571 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins
    • 2-s2.0-13544272571 10.1074/jbc.C400496200
    • Hyun A. W., Jeong W., Chang T.-S., Kwang J. P., Sung J. P., Jeong S. Y., Sue G. R., Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins. Journal of Biological Chemistry 2005 280 5 3125 3128 2-s2.0-13544272571 10.1074/jbc.C400496200
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.5 , pp. 3125-3128
    • Hyun, A.W.1    Jeong, W.2    Chang, T.-S.3    Kwang, J.P.4    Sung, J.P.5    Jeong, S.Y.6    Sue, G.R.7
  • 53
    • 64149085448 scopus 로고    scopus 로고
    • Typical 2-Cys peroxiredoxins - Structures, mechanisms and functions
    • 2-s2.0-64149085448 10.1111/j.1742-4658.2009.06985.x
    • Hall A., Karplus P. A., Poole L. B., Typical 2-Cys peroxiredoxins- structures, mechanisms and functions. FEBS Journal 2009 276 9 2469 2477 2-s2.0-64149085448 10.1111/j.1742-4658.2009.06985.x
    • (2009) FEBS Journal , vol.276 , Issue.9 , pp. 2469-2477
    • Hall, A.1    Karplus, P.A.2    Poole, L.B.3
  • 54
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. Cerevisiae sulphiredoxin
    • 2-s2.0-0242416188 10.1038/nature02075
    • Biteau B., Labarre J., Toledano M. B., ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 2003 425 6961 980 984 2-s2.0-0242416188 10.1038/nature02075
    • (2003) Nature , vol.425 , Issue.6961 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 55
    • 70350398226 scopus 로고    scopus 로고
    • JNK/FOXO-mediated neuronal expression of fly homologue of peroxiredoxin II reduces oxidative stress and extends life span
    • 2-s2.0-70350398226 10.1074/jbc.M109.028027
    • Lee K.-S., Iijima-Ando K., Iijima K., Lee W.-J., Lee J. H., Yu K., Lee D.-S., JNK/FOXO-mediated neuronal expression of fly homologue of peroxiredoxin II reduces oxidative stress and extends life span. Journal of Biological Chemistry 2009 284 43 29454 29461 2-s2.0-70350398226 10.1074/jbc.M109.028027
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.43 , pp. 29454-29461
    • Lee, K.-S.1    Iijima-Ando, K.2    Iijima, K.3    Lee, W.-J.4    Lee, J.H.5    Yu, K.6    Lee, D.-S.7
  • 56
    • 0042568938 scopus 로고    scopus 로고
    • Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression
    • 2-s2.0-0042568938 10.1038/nature01819
    • Neumann C. A., Krause D. S., Carman C. V., Das S., Dubey D. P., Abraham J. L., Bronson R. T., Fujiwara Y., Orkin S. H., Van Etten R. A., Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression. Nature 2003 424 6948 561 565 2-s2.0-0042568938 10.1038/nature01819
    • (2003) Nature , vol.424 , Issue.6948 , pp. 561-565
    • Neumann, C.A.1    Krause, D.S.2    Carman, C.V.3    Das, S.4    Dubey, D.P.5    Abraham, J.L.6    Bronson, R.T.7    Fujiwara, Y.8    Orkin, S.H.9    Van Etten, R.A.10
  • 57
  • 58
    • 84866490309 scopus 로고    scopus 로고
    • Peroxiredoxins, gerontogenes linking aging to genome instability and cancer
    • Nystrom T., Yang J., Molin M., Peroxiredoxins, gerontogenes linking aging to genome instability and cancer. Genes & Development 2012 26 18 2001 2008
    • (2012) Genes & Development , vol.26 , Issue.18 , pp. 2001-2008
    • Nystrom, T.1    Yang, J.2    Molin, M.3
  • 59
    • 14644425402 scopus 로고    scopus 로고
    • A biological network in Saccharomyces cerevisiae prevents the deleterious effects of endogenous oxidative DNA damage
    • 2-s2.0-14644425402 10.1016/j.molcel.2005.02.008
    • Huang M.-E., Kolodner R. D., A biological network in Saccharomyces cerevisiae prevents the deleterious effects of endogenous oxidative DNA damage. Molecular Cell 2005 17 5 709 720 2-s2.0-14644425402 10.1016/j.molcel.2005.02.008
    • (2005) Molecular Cell , vol.17 , Issue.5 , pp. 709-720
    • Huang, M.-E.1    Kolodner, R.D.2
  • 61
    • 0037110454 scopus 로고    scopus 로고
    • 2 receptor and redox-transducer in gene activation
    • 2-s2.0-0037110454 10.1016/S0092-8674(02)01048-6
    • 2 receptor and redox-transducer in gene activation. Cell 2002 111 4 471 481 2-s2.0-0037110454 10.1016/S0092-8674(02)01048-6
    • (2002) Cell , vol.111 , Issue.4 , pp. 471-481
    • Delaunay, A.1    Pflieger, D.2    Barrault, M.-B.3    Vinh, J.4    Toledano, M.B.5
  • 62
    • 63249111293 scopus 로고    scopus 로고
    • A major peroxiredoxin-induced activation of yap 1 transcription factor is mediated by reduction-sensitive disulfide bonds and reveals a low level of transcriptional activation
    • 2-s2.0-63249111293 10.1074/jbc.M807583200
    • Tachibana T., Okazaki S., Murayama A., Naganuma A., Nomoto A., Kuge S., A major peroxiredoxin-induced activation of yap 1 transcription factor is mediated by reduction-sensitive disulfide bonds and reveals a low level of transcriptional activation. Journal of Biological Chemistry 2009 284 7 4464 4472 2-s2.0-63249111293 10.1074/jbc.M807583200
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.7 , pp. 4464-4472
    • Tachibana, T.1    Okazaki, S.2    Murayama, A.3    Naganuma, A.4    Nomoto, A.5    Kuge, S.6
  • 63
    • 2542504409 scopus 로고    scopus 로고
    • Peroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable
    • 2-s2.0-2542504409 10.1074/jbc.M402095200
    • Wong C.-M., Siu K.-L., Jin D.-Y., Peroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable. Journal of Biological Chemistry 2004 279 22 23207 23213 2-s2.0-2542504409 10.1074/jbc.M402095200
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.22 , pp. 23207-23213
    • Wong, C.-M.1    Siu, K.-L.2    Jin, D.-Y.3
  • 64
    • 84879744031 scopus 로고    scopus 로고
    • Boronate-based fluorescent probes: Imaging hydrogen peroxide in living systems
    • Lin V. S., Dickinson B. C., Chang C. J., Boronate-based fluorescent probes: imaging hydrogen peroxide in living systems. Methods in Enzymology 2013 526 19 43
    • (2013) Methods in Enzymology , vol.526 , pp. 19-43
    • Lin, V.S.1    Dickinson, B.C.2    Chang, C.J.3
  • 65
    • 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 2 745 756
    • (2014) Biochim Biophys Acta , vol.1840 , Issue.2 , pp. 745-756
    • Lukyanov, K.A.1    Belousov, V.V.2
  • 66
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • 2-s2.0-19444375216 10.1016/j.freeradbiomed.2005.02.026
    • Sue G. R., Ho Z. C., Kim K., Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radical Biology and Medicine 2005 38 12 1543 1552 2-s2.0-19444375216 10.1016/j.freeradbiomed.2005.02.026
    • (2005) Free Radical Biology and Medicine , vol.38 , Issue.12 , pp. 1543-1552
    • Sue, G.R.1    Ho, Z.C.2    Kim, K.3
  • 69
    • 67651202633 scopus 로고    scopus 로고
    • Peroxiredoxin Tsa1 is the key peroxidase suppressing genome instability and protecting against cell death in Saccharomyces cerevisiae
    • 2-s2.0-67651202633 10.1371/journal.pgen.1000524
    • Iraqui I., Kienda G., Soeur J., Faye G., Baldacci G., Kolodner R. D., Huang M.-E., Peroxiredoxin Tsa1 is the key peroxidase suppressing genome instability and protecting against cell death in Saccharomyces cerevisiae. PLoS Genetics 2009 5 6, article e1000524 2-s2.0-67651202633 10.1371/journal.pgen. 1000524
    • (2009) PLoS Genetics , vol.5 , Issue.6 ARTICLE E1000524
    • Iraqui, I.1    Kienda, G.2    Soeur, J.3    Faye, G.4    Baldacci, G.5    Kolodner, R.D.6    Huang, M.-E.7
  • 70
    • 0037085384 scopus 로고    scopus 로고
    • Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress
    • 2-s2.0-0037085384 10.1074/jbc.M106846200
    • Wong C.-M., Zhou Y., Ng R. W. M., Kung H.-F., Jin D.-Y., Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress. Journal of Biological Chemistry 2002 277 7 5385 5394 2-s2.0-0037085384 10.1074/jbc.M106846200
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.7 , pp. 5385-5394
    • Wong, C.-M.1    Zhou, Y.2    Ng, R.W.M.3    Kung, H.-F.4    Jin, D.-Y.5
  • 72
    • 74849098583 scopus 로고    scopus 로고
    • Peroxiredoxin 1 and its role in cell signaling
    • 2-s2.0-74849098583
    • Neumann C. A., Cao J., Manevich Y., Peroxiredoxin 1 and its role in cell signaling. Cell Cycle 2009 8 24 4072 4078 2-s2.0-74849098583
    • (2009) Cell Cycle , vol.8 , Issue.24 , pp. 4072-4078
    • Neumann, C.A.1    Cao, J.2    Manevich, Y.3
  • 73
    • 79958059617 scopus 로고    scopus 로고
    • Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins
    • 2-s2.0-79958059617 10.1089/ars.2010.3624
    • Hall A., Nelson K., Poole L. B., Karplus P. A., Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins. Antioxidants and Redox Signaling 2011 15 3 795 815 2-s2.0-79958059617 10.1089/ars.2010.3624
    • (2011) Antioxidants and Redox Signaling , vol.15 , Issue.3 , pp. 795-815
    • Hall, A.1    Nelson, K.2    Poole, L.B.3    Karplus, P.A.4
  • 75
    • 79951643450 scopus 로고    scopus 로고
    • 2, and protein chaperones
    • 2-s2.0-79951643450 10.1089/ars.2010.3393
    • 2 and protein chaperones. Antioxidants and Redox Signaling 2011 15 3 781 794 2-s2.0-79951643450 10.1089/ars.2010.3393
    • (2011) Antioxidants and Redox Signaling , vol.15 , Issue.3 , pp. 781-794
    • Rhee, S.G.1    Woo, H.A.2
  • 79
    • 35348972430 scopus 로고    scopus 로고
    • Genetic links between diet and lifespan: Shared mechanisms from yeast to humans
    • 2-s2.0-35348972430 10.1038/nrg2188
    • Bishop N. A., Guarente L., Genetic links between diet and lifespan: shared mechanisms from yeast to humans. Nature Reviews Genetics 2007 8 11 835 844 2-s2.0-35348972430 10.1038/nrg2188
    • (2007) Nature Reviews Genetics , vol.8 , Issue.11 , pp. 835-844
    • Bishop, N.A.1    Guarente, L.2
  • 80
    • 27744511769 scopus 로고    scopus 로고
    • Cell biology: Regulation of yeast replicative life span by TOR and Sch9 response to nutrients
    • 2-s2.0-27744511769 10.1126/science.1115535
    • Kaeberlein M., Powers R. W. III, Steffen K. K., Westman E. A., Hu D., Dang N., Kerr E. O., Kirkland K. T., Fields S., Kennedy B. K., Cell biology: regulation of yeast replicative life span by TOR and Sch9 response to nutrients. Science 2005 310 5751 1193 1196 2-s2.0-27744511769 10.1126/science.1115535
    • (2005) Science , vol.310 , Issue.5751 , pp. 1193-1196
    • Kaeberlein, M.1    Powers III, R.W.2    Steffen, K.K.3    Westman, E.A.4    Hu, D.5    Dang, N.6    Kerr, E.O.7    Kirkland, K.T.8    Fields, S.9    Kennedy, B.K.10
  • 82
    • 34447528668 scopus 로고    scopus 로고
    • Type 5 adenylyl cyclase disruption increases longevity and protects against stress
    • 2-s2.0-34447528668 10.1016/j.cell.2007.05.038
    • Yan L., Vatner D. E., O'Connor J. P., Ivessa A., Ge H., Chen W., Hirotani S., Ishikawa Y., Sadoshima J., Vatner S. F., Type 5 adenylyl cyclase disruption increases longevity and protects against stress. Cell 2007 130 2 247 258 2-s2.0-34447528668 10.1016/j.cell.2007.05.038
    • (2007) Cell , vol.130 , Issue.2 , pp. 247-258
    • Yan, L.1    Vatner, D.E.2    O'Connor, J.P.3    Ivessa, A.4    Ge, H.5    Chen, W.6    Hirotani, S.7    Ishikawa, Y.8    Sadoshima, J.9    Vatner, S.F.10
  • 83
    • 33947688760 scopus 로고    scopus 로고
    • The Drosophila DCO mutation suppresses age-related memory impairment without affecting lifespan
    • 2-s2.0-33947688760 10.1038/nn1863
    • Yamazaki D., Horiuchi J., Nakagami Y., Nagano S., Tamura T., Saitoe M., The Drosophila DCO mutation suppresses age-related memory impairment without affecting lifespan. Nature Neuroscience 2007 10 4 478 484 2-s2.0-33947688760 10.1038/nn1863
    • (2007) Nature Neuroscience , vol.10 , Issue.4 , pp. 478-484
    • Yamazaki, D.1    Horiuchi, J.2    Nakagami, Y.3    Nagano, S.4    Tamura, T.5    Saitoe, M.6
  • 84
    • 17144429302 scopus 로고    scopus 로고
    • Calorie restriction, SIRT1 and metabolism: Understanding longevity
    • 2-s2.0-17144429302 10.1038/nrm1616
    • Bordone L., Guarente L., Calorie restriction, SIRT1 and metabolism: understanding longevity. Nature Reviews Molecular Cell Biology 2005 6 4 298 305 2-s2.0-17144429302 10.1038/nrm1616
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.4 , pp. 298-305
    • Bordone, L.1    Guarente, L.2
  • 85
    • 63749105226 scopus 로고    scopus 로고
    • MTOR and the control of whole body metabolism
    • 2-s2.0-63749105226 10.1016/j.ceb.2009.01.024
    • Polak P., Hall M. N., mTOR and the control of whole body metabolism. Current Opinion in Cell Biology 2009 21 2 209 218 2-s2.0-63749105226 10.1016/j.ceb.2009.01.024
    • (2009) Current Opinion in Cell Biology , vol.21 , Issue.2 , pp. 209-218
    • Polak, P.1    Hall, M.N.2
  • 86
    • 0024554046 scopus 로고
    • Control of Saccharomyces cerevisiae catalase T gene (CTT1) expression by nutrient supply via the RAS-cyclic AMP pathway
    • 2-s2.0-0024554046
    • Bissinger P. H., Wieser R., Hamilton B., Ruis H., Control of Saccharomyces cerevisiae catalase T gene (CTT1) expression by nutrient supply via the RAS-cyclic AMP pathway. Molecular and Cellular Biology 1989 9 3 1309 1315 2-s2.0-0024554046
    • (1989) Molecular and Cellular Biology , vol.9 , Issue.3 , pp. 1309-1315
    • Bissinger, P.H.1    Wieser, R.2    Hamilton, B.3    Ruis, H.4
  • 87
    • 0041589207 scopus 로고    scopus 로고
    • Nuclear thiol peroxidase as a functional Alkyl-hydroperoxide reductase necessary for stationary phase growth of Saccharomyces cerevisiae
    • 2-s2.0-0041589207 10.1074/jbc.M302628200
    • Cha M.-K., Choi Y.-S., Hong S.-K., Kim W.-C., No K. T., Kim I.-H., Nuclear thiol peroxidase as a functional Alkyl-hydroperoxide reductase necessary for stationary phase growth of Saccharomyces cerevisiae. Journal of Biological Chemistry 2003 278 27 24636 24643 2-s2.0-0041589207 10.1074/jbc.M302628200
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 24636-24643
    • Cha, M.-K.1    Choi, Y.-S.2    Hong, S.-K.3    Kim, W.-C.4    No, K.T.5    Kim, I.-H.6
  • 88
    • 0037023725 scopus 로고    scopus 로고
    • Msn2p/Msn4p act as a key transcriptional activator of yeast cytoplasmic thiol peroxidase II
    • 2-s2.0-0037023725 10.1074/jbc.M111341200
    • Hong S.-K., Cha M.-K., Choi Y.-S., Kim W.-C., Kim I.-H., Msn2p/Msn4p act as a key transcriptional activator of yeast cytoplasmic thiol peroxidase II. Journal of Biological Chemistry 2002 277 14 12109 12117 2-s2.0-0037023725 10.1074/jbc.M111341200
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.14 , pp. 12109-12117
    • Hong, S.-K.1    Cha, M.-K.2    Choi, Y.-S.3    Kim, W.-C.4    Kim, I.-H.5
  • 89
    • 0000056465 scopus 로고    scopus 로고
    • Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae
    • 2-s2.0-0000056465 10.1074/jbc.275.8.5723
    • Park S. G., Cha M.-K., Jeong W., Kim I.-H., Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae. Journal of Biological Chemistry 2000 275 8 5723 5732 2-s2.0-0000056465 10.1074/jbc.275.8.5723
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.8 , pp. 5723-5732
    • Park, S.G.1    Cha, M.-K.2    Jeong, W.3    Kim, I.-H.4
  • 91
    • 19344365135 scopus 로고    scopus 로고
    • Ras and Gpa2 mediate one branch of a redundant glucose signaling pathway in yeast
    • 2-s2.0-19344365135 10.1371/journal.pbio.0020128
    • Wang Y., Pierce M., Schneper L., Güldal C. G., Zhang X., Tavazoie S., Broach J. R., Ras and Gpa2 mediate one branch of a redundant glucose signaling pathway in yeast. PLoS Biology 2004 2 5, e128 2-s2.0-19344365135 10.1371/journal.pbio.0020128
    • (2004) PLoS Biology , vol.2 , Issue.5 E128
    • Wang, Y.1    Pierce, M.2    Schneper, L.3    Güldal, C.G.4    Zhang, X.5    Tavazoie, S.6    Broach, J.R.7
  • 92
    • 33645130011 scopus 로고    scopus 로고
    • Glucose signaling in Saccharomyces cerevisiae
    • 2-s2.0-33645130011 10.1128/MMBR.70.1.253-282.2006
    • Santangelo G. M., Glucose signaling in Saccharomyces cerevisiae. Microbiology and Molecular Biology Reviews 2006 70 1 253 282 2-s2.0-33645130011 10.1128/MMBR.70.1.253-282.2006
    • (2006) Microbiology and Molecular Biology Reviews , vol.70 , Issue.1 , pp. 253-282
    • Santangelo, G.M.1
  • 93
    • 76349102304 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae plasma membrane nutrient sensors and their role in PKA signaling
    • 2-s2.0-76349102304 10.1111/j.1567-1364.2009.00587.x
    • Rubio-Texeira M., Van Zeebroeck G., Voordeckers K., Thevelein J. M., Saccharomyces cerevisiae plasma membrane nutrient sensors and their role in PKA signaling. FEMS Yeast Research 2010 10 2 134 149 2-s2.0-76349102304 10.1111/j.1567-1364.2009.00587.x
    • (2010) FEMS Yeast Research , vol.10 , Issue.2 , pp. 134-149
    • Rubio-Texeira, M.1    Van Zeebroeck, G.2    Voordeckers, K.3    Thevelein, J.M.4
  • 94
    • 0025253769 scopus 로고
    • The function of ras genes in Saccharomyces cerevisiae
    • 2-s2.0-0025253769
    • Broach J. R., Deschenes R. J., The function of ras genes in Saccharomyces cerevisiae. Advances in Cancer Research 1990 54 79 139 2-s2.0-0025253769
    • (1990) Advances in Cancer Research , vol.54 , pp. 79-139
    • Broach, J.R.1    Deschenes, R.J.2
  • 95
    • 6344256284 scopus 로고    scopus 로고
    • Activation state of the Ras2 protein and glucose-induced signaling in Saccharomyces cerevisiae
    • 2-s2.0-6344256284 10.1074/jbc.M405136200
    • Colombo S., Ronchetti D., Thevelein J. M., Winderickx J., Martegani E., Activation state of the Ras2 protein and glucose-induced signaling in Saccharomyces cerevisiae. Journal of Biological Chemistry 2004 279 45 46715 46722 2-s2.0-6344256284 10.1074/jbc.M405136200
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.45 , pp. 46715-46722
    • Colombo, S.1    Ronchetti, D.2    Thevelein, J.M.3    Winderickx, J.4    Martegani, E.5
  • 96
    • 0033745888 scopus 로고    scopus 로고
    • Glucose-induced cAMP signalling in yeast requires both a G-protein coupled receptor system for extracellular glucose detection and a separable hexose kinase-dependent sensing process
    • 2-s2.0-0033745888 10.1046/j.1365-2958.2000.02125.x
    • Rolland F., De Winde J. H., Lemaire K., Boles E., Thevelein J. M., Winderickx J., Glucose-induced cAMP signalling in yeast requires both a G-protein coupled receptor system for extracellular glucose detection and a separable hexose kinase-dependent sensing process. Molecular Microbiology 2000 38 2 348 358 2-s2.0-0033745888 10.1046/j.1365-2958.2000.02125.x
    • (2000) Molecular Microbiology , vol.38 , Issue.2 , pp. 348-358
    • Rolland, F.1    De Winde, J.H.2    Lemaire, K.3    Boles, E.4    Thevelein, J.M.5    Winderickx, J.6
  • 97
    • 0024461376 scopus 로고
    • Osteoclastic bone resorption by a polarized vacuolar proton pump
    • 2-s2.0-0024461376
    • Blair H. C., Teitelbaum S. L., Ghiselli R., Gluck S., Osteoclastic bone resorption by a polarized vacuolar proton pump. Science 1989 245 4920 855 857 2-s2.0-0024461376
    • (1989) Science , vol.245 , Issue.4920 , pp. 855-857
    • Blair, H.C.1    Teitelbaum, S.L.2    Ghiselli, R.3    Gluck, S.4
  • 98
    • 0026460154 scopus 로고
    • Activation of vacuolar-type proton pumps by protein kinase C. Role in neutrophil pH regulation
    • 2-s2.0-0026460154
    • Nanda A., Gukovskaya A., Tseng J., Grinstein S., Activation of vacuolar-type proton pumps by protein kinase C. Role in neutrophil pH regulation. Journal of Biological Chemistry 1992 267 32 22740 22746 2-s2.0-0026460154
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.32 , pp. 22740-22746
    • Nanda, A.1    Gukovskaya, A.2    Tseng, J.3    Grinstein, S.4
  • 99
    • 2442560191 scopus 로고    scopus 로고
    • Vacuolar H+-ATPase in human breast cancer cells with distinct metastatic potential: Distribution and functional activity
    • 2-s2.0-2442560191 10.1152/ajpcell.00407.2003
    • Sennoune S. R., Bakunts K., Martínez G. M., Chua-Tuan J. L., Kebir Y., Attaya M. N., Martínez-Zaguilán R., Vacuolar H+-ATPase in human breast cancer cells with distinct metastatic potential: distribution and functional activity. American Journal of Physiology 2004 286 6 C1443 C1452 2-s2.0-2442560191 10.1152/ajpcell.00407.2003
    • (2004) American Journal of Physiology , vol.286 , Issue.6
    • Sennoune, S.R.1    Bakunts, K.2    Martínez, G.M.3    Chua-Tuan, J.L.4    Kebir, Y.5    Attaya, M.N.6    Martínez-Zaguilán, R.7
  • 101
    • 61349192268 scopus 로고    scopus 로고
    • The Ras/cAMP/protein kinase A pathway regulates glucose-dependent assembly of the vacuolar (H+)-ATPase in yeast
    • 2-s2.0-61349192268 10.1074/jbc.M805232200
    • Bond S., Forgac M., The Ras/cAMP/protein kinase A pathway regulates glucose-dependent assembly of the vacuolar (H+)-ATPase in yeast. Journal of Biological Chemistry 2008 283 52 36513 36521 2-s2.0-61349192268 10.1074/jbc.M805232200
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.52 , pp. 36513-36521
    • Bond, S.1    Forgac, M.2
  • 102
    • 50649120655 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane proton pumps collaborate to achieve cytosolic pH homeostasis in yeast
    • 2-s2.0-50649120655 10.1074/jbc.M710470200
    • Martínez-Muñoz G. A., Kane P., Vacuolar and plasma membrane proton pumps collaborate to achieve cytosolic pH homeostasis in yeast. Journal of Biological Chemistry 2008 283 29 20309 20319 2-s2.0-50649120655 10.1074/jbc.M710470200
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.29 , pp. 20309-20319
    • Martínez-Muñoz, G.A.1    Kane, P.2
  • 103
    • 38349193176 scopus 로고    scopus 로고
    • The long physiological reach of the yeast vacuolar H+-ATPase
    • 2-s2.0-38349193176 10.1007/s10863-007-9112-z
    • Kane P. M., The long physiological reach of the yeast vacuolar H+-ATPase. Journal of Bioenergetics and Biomembranes 2007 39 5-6 415 421 2-s2.0-38349193176 10.1007/s10863-007-9112-z
    • (2007) Journal of Bioenergetics and Biomembranes , vol.39 , Issue.5-6 , pp. 415-421
    • Kane, P.M.1
  • 104
    • 62949218373 scopus 로고    scopus 로고
    • The yeast lysosome-like vacuole: Endpoint and crossroads
    • 2-s2.0-62949218373 10.1016/j.bbamcr.2008.08.003
    • Li S. C., Kane P. M., The yeast lysosome-like vacuole: endpoint and crossroads. Biochimica et Biophysica Acta 2009 1793 4 650 663 2-s2.0-62949218373 10.1016/j.bbamcr.2008.08.003
    • (2009) Biochimica et Biophysica Acta , vol.1793 , Issue.4 , pp. 650-663
    • Li, S.C.1    Kane, P.M.2
  • 105
    • 2342487990 scopus 로고    scopus 로고
    • Cells have distinct mechanisms to maintain protection against different reactive oxygen species: Oxidative-stress-response genes
    • 2-s2.0-2342487990 10.1073/pnas.0305888101
    • Thorpe G. W., Fong C. S., Alic N., Higgins V. J., Dawes I. W., Cells have distinct mechanisms to maintain protection against different reactive oxygen species: oxidative-stress-response genes. Proceedings of the National Academy of Sciences of the United States of America 2004 101 17 6564 6569 2-s2.0-2342487990 10.1073/pnas.0305888101
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.17 , pp. 6564-6569
    • Thorpe, G.W.1    Fong, C.S.2    Alic, N.3    Higgins, V.J.4    Dawes, I.W.5
  • 106
    • 61449216130 scopus 로고    scopus 로고
    • In vivo measurement of cytosolic and mitochondrial pH using a pH-sensitive GFP derivative in Saccharomyces cerevisiae reveals a relation between intracellular pH and growth
    • 2-s2.0-61449216130 10.1099/mic.0.022038-0
    • Orij R., Postmus J., Beek A. T., Brul S., Smits G. J., In vivo measurement of cytosolic and mitochondrial pH using a pH-sensitive GFP derivative in Saccharomyces cerevisiae reveals a relation between intracellular pH and growth. Microbiology 2009 155 1 268 278 2-s2.0-61449216130 10.1099/mic.0.022038-0
    • (2009) Microbiology , vol.155 , Issue.1 , pp. 268-278
    • Orij, R.1    Postmus, J.2    Beek, A.T.3    Brul, S.4    Smits, G.J.5
  • 107
    • 0023393237 scopus 로고
    • Regulation of the cAMP level in the yeast Saccharomyces cerevisiae: The glucose-induced cAMP signal is not mediated by a transient drop in the intracellular pH
    • 2-s2.0-0023393237
    • Thevelein J. M., Beullens M., Honshoven F., Hoebeeck G., Detremerie K., Griewel B., den Hollander J. A., Jans A. W., Regulation of the cAMP level in the yeast Saccharomyces cerevisiae: the glucose-induced cAMP signal is not mediated by a transient drop in the intracellular pH. Journal of General Microbiology 1987 133 8 2197 2205 2-s2.0-0023393237
    • (1987) Journal of General Microbiology , vol.133 , Issue.8 , pp. 2197-2205
    • Thevelein, J.M.1    Beullens, M.2    Honshoven, F.3    Hoebeeck, G.4    Detremerie, K.5    Griewel, B.6    Den Hollander, J.A.7    Jans, A.W.8
  • 108
    • 0033800762 scopus 로고    scopus 로고
    • Regulation of yeast H+-ATPase by protein kinases belonging to a family dedicated to activation of plasma membrane transporters
    • 2-s2.0-0033800762 10.1128/MCB.20.20.7654-7661.2000
    • Goossens A., De la Fuente N., Forment J., Serrano R., Portillo F., Regulation of yeast H+-ATPase by protein kinases belonging to a family dedicated to activation of plasma membrane transporters. Molecular and Cellular Biology 2000 20 20 7654 7661 2-s2.0-0033800762 10.1128/MCB.20.20.7654-7661.2000
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.20 , pp. 7654-7661
    • Goossens, A.1    De La Fuente, N.2    Forment, J.3    Serrano, R.4    Portillo, F.5
  • 109
    • 33646161947 scopus 로고    scopus 로고
    • Intracellular acidification delays hormonal G2/M transition and inhibits G2/M transition triggered by thiophosphorylated MAPK in xenopus oocytes
    • 2-s2.0-33646161947 10.1002/jcb.20764
    • Sellier C., Bodart J.-F., Flament S., Baert F., Cannon J., Vilain J.-P., Intracellular acidification delays hormonal G2/M transition and inhibits G2/M transition triggered by thiophosphorylated MAPK in xenopus oocytes. Journal of Cellular Biochemistry 2006 98 2 287 300 2-s2.0-33646161947 10.1002/jcb.20764
    • (2006) Journal of Cellular Biochemistry , vol.98 , Issue.2 , pp. 287-300
    • Sellier, C.1    Bodart, J.-F.2    Flament, S.3    Baert, F.4    Cannon, J.5    Vilain, J.-P.6
  • 110
    • 0029063512 scopus 로고
    • Disassembly and reassembly of the yeast vacuolar H+-ATPase in vivo
    • 2-s2.0-0029063512
    • Kane P. M., Disassembly and reassembly of the yeast vacuolar H+-ATPase in vivo. Journal of Biological Chemistry 1995 270 28 17025 17032 2-s2.0-0029063512
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.28 , pp. 17025-17032
    • Kane, P.M.1
  • 111
    • 0031597366 scopus 로고    scopus 로고
    • Reversible association between the V1 and V0 domains of yeast vacuolar H+-ATPase is an unconventional glucose-induced effect
    • 2-s2.0-0031597366
    • Parra K. J., Kane P. M., Reversible association between the V1 and V0 domains of yeast vacuolar H+-ATPase is an unconventional glucose-induced effect. Molecular and Cellular Biology 1998 18 12 7064 7074 2-s2.0-0031597366
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.12 , pp. 7064-7074
    • Parra, K.J.1    Kane, P.M.2
  • 112
    • 34147107933 scopus 로고    scopus 로고
    • Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress
    • 2-s2.0-34147107933 10.1074/jbc.M608293200
    • Milgrom E., Diab H., Middleton F., Kane P. M., Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress. Journal of Biological Chemistry 2007 282 10 7125 7136 2-s2.0-34147107933 10.1074/jbc.M608293200
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.10 , pp. 7125-7136
    • Milgrom, E.1    Diab, H.2    Middleton, F.3    Kane, P.M.4
  • 113
    • 67549136242 scopus 로고    scopus 로고
    • Mitochondrial dysfunction leads to nuclear genome instability via an iron-sulfur cluster defect
    • 2-s2.0-67549136242 10.1016/j.cell.2009.04.014
    • Veatch J. R., McMurray M. A., Nelson Z. W., Gottschling D. E., Mitochondrial dysfunction leads to nuclear genome instability via an iron-sulfur cluster defect. Cell 2009 137 7 1247 1258 2-s2.0-67549136242 10.1016/j.cell.2009.04.014
    • (2009) Cell , vol.137 , Issue.7 , pp. 1247-1258
    • Veatch, J.R.1    McMurray, M.A.2    Nelson, Z.W.3    Gottschling, D.E.4
  • 114
    • 84877098900 scopus 로고    scopus 로고
    • Defects associated with mitochondrial DNA damage can be mitigated by increased vacuolar pH in Saccharomyces cerevisiae
    • Garipler G., Dunn C. D., Defects associated with mitochondrial DNA damage can be mitigated by increased vacuolar pH in Saccharomyces cerevisiae. Genetics 2013 194 1 285 290
    • (2013) Genetics , vol.194 , Issue.1 , pp. 285-290
    • Garipler, G.1    Dunn, C.D.2
  • 115
    • 84876582502 scopus 로고    scopus 로고
    • Loss of vacuolar H+-ATPase (V-ATPase) activity in yeast generates an iron deprivation signal that is moderated by induction of the peroxiredoxin TSA2
    • Diab H. I., Kane P. M., Loss of vacuolar H+-ATPase (V-ATPase) activity in yeast generates an iron deprivation signal that is moderated by induction of the peroxiredoxin TSA2. The Journal of Biological Chemistry 2013 288 16 11366 11377
    • (2013) The Journal of Biological Chemistry , vol.288 , Issue.16 , pp. 11366-11377
    • Diab, H.I.1    Kane, P.M.2
  • 116
    • 0033582416 scopus 로고    scopus 로고
    • A new antioxidant with alkyl hydroperoxide defense properties in yeast
    • 2-s2.0-0033582416 10.1074/jbc.274.8.4537
    • Lee J., Spector D., Godon C., Labarre J., Toledano M. B., A new antioxidant with alkyl hydroperoxide defense properties in yeast. Journal of Biological Chemistry 1999 274 8 4537 4544 2-s2.0-0033582416 10.1074/jbc.274.8. 4537
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.8 , pp. 4537-4544
    • Lee, J.1    Spector, D.2    Godon, C.3    Labarre, J.4    Toledano, M.B.5
  • 117
    • 77951235682 scopus 로고    scopus 로고
    • Genetic dissection of a mitochondria-vacuole signaling pathway in yeast reveals a link between chronic oxidative stress and vacuolar iron transport
    • 2-s2.0-77951235682 10.1074/jbc.M109.096859
    • Li L., Murdock G., Bagley D., Jia X., Ward D. M., Kaplan J., Genetic dissection of a mitochondria-vacuole signaling pathway in yeast reveals a link between chronic oxidative stress and vacuolar iron transport. Journal of Biological Chemistry 2010 285 14 10232 10242 2-s2.0-77951235682 10.1074/jbc.M109.096859
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.14 , pp. 10232-10242
    • Li, L.1    Murdock, G.2    Bagley, D.3    Jia, X.4    Ward, D.M.5    Kaplan, J.6
  • 119
    • 0030608677 scopus 로고    scopus 로고
    • The ABC transport Atm1p is required for mitochondrial iron homeostasis
    • 2-s2.0-0030608677 10.1016/S0014-5793(97)01414-2
    • Kispal G., Csere P., Guiard B., Lill R., The ABC transport Atm1p is required for mitochondrial iron homeostasis. FEBS Letters 1997 418 3 346 350 2-s2.0-0030608677 10.1016/S0014-5793(97)01414-2
    • (1997) FEBS Letters , vol.418 , Issue.3 , pp. 346-350
    • Kispal, G.1    Csere, P.2    Guiard, B.3    Lill, R.4
  • 120
    • 15444371876 scopus 로고    scopus 로고
    • Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis
    • 2-s2.0-15444371876 10.1074/jbc.M413731200
    • Rutherford J. C., Ojeda L., Balk J., Mühlenhoff U., Lill R., Winge D. R., Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis. Journal of Biological Chemistry 2005 280 11 10135 10140 2-s2.0-15444371876 10.1074/jbc.M413731200
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.11 , pp. 10135-10140
    • Rutherford, J.C.1    Ojeda, L.2    Balk, J.3    Mühlenhoff, U.4    Lill, R.5    Winge, D.R.6
  • 121
    • 74549157678 scopus 로고    scopus 로고
    • Functional genomics of pH homeostasis in Corynebacterium glutamicum revealed novel links between pH response, oxidative stress, iron homeostasis and methionine synthesis
    • 10621,2-s2.0-74549157678 10.1186/1471-2164-10-621
    • Follmann M., Ochrombel I., Krämer R., Trötschel C., Poetsch A., Rückert C., Hüser A., Persicke M., Seiferling D., Kalinowski J., Marin K., Functional genomics of pH homeostasis in Corynebacterium glutamicum revealed novel links between pH response, oxidative stress, iron homeostasis and methionine synthesis. BMC Genomics 2009 10, article 621 2-s2.0-74549157678 10.1186/1471-2164-10-621
    • (2009) BMC Genomics
    • Follmann, M.1    Ochrombel, I.2    Krämer, R.3    Trötschel, C.4    Poetsch, A.5    Rückert, C.6    Hüser, A.7    Persicke, M.8    Seiferling, D.9    Kalinowski, J.10    Marin, K.11
  • 122
    • 78650949287 scopus 로고    scopus 로고
    • Histidine 103 in Fra2 is an iron-sulfur cluster ligand in the [2Fe-2S] Fra2-Grx3 complex and is required for in vivo iron signaling in yeast
    • 2-s2.0-78650949287 10.1074/jbc.M110.184176
    • Li H., Mapolelo D. T., Dingra N. N., Keller G., Riggs-Gelasco P. J., Winge D. R., Johnson M. K., Outten C. E., Histidine 103 in Fra2 is an iron-sulfur cluster ligand in the [2Fe-2S] Fra2-Grx3 complex and is required for in vivo iron signaling in yeast. Journal of Biological Chemistry 2011 286 1 867 876 2-s2.0-78650949287 10.1074/jbc.M110.184176
    • (2011) Journal of Biological Chemistry , vol.286 , Issue.1 , pp. 867-876
    • Li, H.1    Mapolelo, D.T.2    Dingra, N.N.3    Keller, G.4    Riggs-Gelasco, P.J.5    Winge, D.R.6    Johnson, M.K.7    Outten, C.E.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.