메뉴 건너뛰기




Volumn 58, Issue 9, 2014, Pages 5552-5566

Signaling of chloroquine-induced stress in the yeast Saccharomyces cerevisiae requires the Hog1 and Slt2 mitogen-activated protein kinase pathways

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; CHLOROQUINE; GLUTAMINE; GLUTATHIONE; GLYCEROL; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; HISTONE; HISTONE DEACETYLASE; LYSINE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE HOG1; MITOGEN ACTIVATED PROTEIN KINASE SLT2; PROTEIN P42; PROTEIN P44; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; SYNAPTOPHYSIN; UNCLASSIFIED DRUG; ANTIMALARIAL AGENT; COPPER ZINC SUPEROXIDE DISMUTASE; HOG1 PROTEIN, S CEREVISIAE; MAPK1 PROTEIN, HUMAN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE P38; P44 PROTEIN, HUMAN; SACCHAROMYCES CEREVISIAE PROTEIN; SLT2 PROTEIN, S CEREVISIAE; TRANSCRIPTION FACTOR;

EID: 84906083461     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.02393-13     Document Type: Article
Times cited : (13)

References (75)
  • 1
    • 0038677510 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization is a critical step of lysosome-initiated apoptosis induced by hydroxychloroquine
    • DOI 10.1038/sj.onc.1206622
    • Boya P, Gonzalez-Polo RA, Poncet D, Andreau K, Vieira HL, Roumier T, Perfettini JL, Kroemer G. 2003. Mitochondrial membrane permeabilization is a critical step of lysosome-initiated apoptosis induced by hydroxychloroquine. Oncogene 22:3927-3936. http://dx.doi.org/10.1038/sj.onc.1206622. (Pubitemid 36819666)
    • (2003) Oncogene , vol.22 , Issue.25 , pp. 3927-3936
    • Boya, P.1    Gonzalez-Polo, R.-A.2    Poncet, D.3    Andreau, K.4    Vieira, H.L.A.5    Roumier, T.6    Perfettini, J.-L.7    Kroemer, G.8
  • 2
    • 33644970102 scopus 로고    scopus 로고
    • Chloroquine inhibits cell growth and induces cell death in A549 lung cancer cells
    • Fan C, Wang W, Zhao B, Zhang S, Miao J. 2006. Chloroquine inhibits cell growth and induces cell death in A549 lung cancer cells. Bioorg. Med. Chem. 14:3218-3222. http://dx.doi.org/10.1016/j.bmc.2005.12.035.
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 3218-3222
    • Fan, C.1    Wang, W.2    Zhao, B.3    Zhang, S.4    Miao, J.5
  • 3
    • 84862815977 scopus 로고    scopus 로고
    • Chloroquine enhances the chemotherapeutic activity of 5-fluorouracil in a colon cancer cell line via cell cycle alteration
    • Choi JH, Yoon JS, Won YW, Park BB, Lee YY. 2012. Chloroquine enhances the chemotherapeutic activity of 5-fluorouracil in a colon cancer cell line via cell cycle alteration. APMIS 120:597-604. http://dx.doi.org/10.1111/j.1600-0463. 2012.02876.x.
    • (2012) APMIS , vol.120 , pp. 597-604
    • Choi, J.H.1    Yoon, J.S.2    Won, Y.W.3    Park, B.B.4    Lee, Y.Y.5
  • 4
    • 0027115531 scopus 로고
    • Malaria. How chloroquine works
    • Wellems TE. 1992. Malaria. How chloroquine works. Nature 355:108-109.
    • (1992) Nature , vol.355 , pp. 108-109
    • Wellems, T.E.1
  • 5
    • 0029977202 scopus 로고    scopus 로고
    • Anti-malarial drugs: Possible mechanisms of action in autoimmune disease and prospects for drug development
    • Fox R. 1996. Anti-malarial drugs: possible mechanisms of action in autoimmune disease and prospects for drug development. Lupus 5(Suppl 1):S4-S10. http://dx.doi.org/10.1177/096120339600500103. (Pubitemid 26196734)
    • (1996) Lupus , vol.5 , Issue.SUPPL. 1
    • Fox, R.1
  • 6
    • 3042837762 scopus 로고    scopus 로고
    • Reactive oxygen species mediate chloroquine-induced expression of chemokines by human astroglial cells
    • DOI 10.1002/glia.20017
    • Park J, Choi K, Jeong E, Kwon D, Benveniste EN, Choi C. 2004. Reactive oxygen species mediate chloroquine-induced expression of chemokines by human astroglial cells. Glia 47:9-20. http://dx.doi.org/10.1002/glia.20017. (Pubitemid 38879701)
    • (2004) GLIA , vol.47 , Issue.1 , pp. 9-20
    • Pare, J.1    Choi, K.2    Jeong, E.3    Kwon, D.4    Benveniste, E.N.5    Choi, C.6
  • 8
    • 18744386931 scopus 로고    scopus 로고
    • PKSP-dependent reduction of phagolysosome fusion and intracellular kill of Aspergillus fumigatus conidia by human monocyte-derived macrophages
    • DOI 10.1046/j.1462-5822.2002.00228.x
    • Jahn B, Langfelder K, Schneider U, Schindel C, Brakhage AA. 2002. PKSP-dependent reduction of phagolysosome fusion and intracellular kill of Aspergillus fumigatus conidia by human monocyte-derived macrophages. Cell. Microbiol. 4:793-803. http://dx.doi.org/10.1046/j.1462-5822.2002.00228.x. (Pubitemid 35469667)
    • (2002) Cellular Microbiology , vol.4 , Issue.12 , pp. 793-803
    • Jahn, B.1    Langfelder, K.2    Schneider, U.3    Schindel, C.4    Brakhage, A.A.5
  • 9
    • 0030824696 scopus 로고    scopus 로고
    • Chloroquine induces human mononuclear phagocytes to inhibit and kill Cryptococcus neoformans by a mechanism independent of iron deprivation
    • Levitz SM, Harrison TS, Tabuni A, Liu X. 1997. Chloroquine induces human mononuclear phagocytes to inhibit and kill Cryptococcus neoformans by a mechanism independent of iron deprivation. J. Clin. Invest. 100:1640-1646. http://dx.doi.org/10.1172/JCI119688. (Pubitemid 27425792)
    • (1997) Journal of Clinical Investigation , vol.100 , Issue.6 , pp. 1640-1646
    • Levitz, S.M.1    Harrison, T.S.2    Tabuni, A.3    Liu, X.4
  • 10
    • 34548460117 scopus 로고    scopus 로고
    • Recycling of chloroquine and its hydroxyl analogue to face bacterial, fungal and viral infections in the 21st century
    • DOI 10.1016/j.ijantimicag.2007.05.015, PII S0924857907002580
    • Rolain JM, Colson P, Raoult D. 2007. Recycling of chloroquine and its hydroxyl analogue to face bacterial, fungal and viral infections in the 21st century. Int. J. Antimicrob. Agents 30:297-308. http://dx.doi.org/10.1016/j. ijantimicag.2007.05.015. (Pubitemid 47364778)
    • (2007) International Journal of Antimicrobial Agents , vol.30 , Issue.4 , pp. 297-308
    • Rolain, J.-M.1    Colson, P.2    Raoult, D.3
  • 12
    • 31344436483 scopus 로고    scopus 로고
    • New insights into the antiviral effects of chloroquine
    • DOI 10.1016/S1473-3099(06)70361-9, PII S1473309906703619
    • Savarino A, Di Trani L, Donatelli I, Cauda R, Cassone A. 2006. New insights into the antiviral effects of chloroquine. Lancet Infect. Dis. 6:67-69. http://dx.doi.org/10.1016/S1473-3099(06)70361-9. (Pubitemid 43138901)
    • (2006) Lancet Infectious Diseases , vol.6 , Issue.2 , pp. 67-69
    • Savarino, A.1    Di, T.L.2    Donatelli, I.3    Cauda, R.4    Cassone, A.5
  • 15
    • 84879572897 scopus 로고    scopus 로고
    • Chloroquine use improves dengue-related symptoms
    • Borges MC, Castro LA, Fonseca BA. 2013. Chloroquine use improves dengue-related symptoms. Mem. Inst. Oswaldo Cruz 108:596-599. http://dx.doi.org/10.1590/S0074-02762013000500010.
    • (2013) Mem. Inst. Oswaldo Cruz , vol.108 , pp. 596-599
    • Borges, M.C.1    Castro, L.A.2    Fonseca, B.A.3
  • 16
    • 57649184991 scopus 로고    scopus 로고
    • Cell growth inhibition, G2/M cell cycle arrest, and apoptosis induced by chloroquine in human breast cancer cell line Bcap-37
    • Jiang PD, Zhao YL, Shi W, Deng XQ, Xie G, Mao YQ, Li ZG, Zheng YZ, Yang SY, Wei YQ. 2008. Cell growth inhibition, G2/M cell cycle arrest, and apoptosis induced by chloroquine in human breast cancer cell line Bcap-37. Cell. Physiol. Biochem. 22:431-440. http://dx.doi.org/10.1159/000185488.
    • (2008) Cell. Physiol. Biochem. , vol.22 , pp. 431-440
    • Jiang, P.D.1    Zhao, Y.L.2    Shi, W.3    Deng, X.Q.4    Xie, G.5    Mao, Y.Q.6    Li, Z.G.7    Zheng, Y.Z.8    Yang, S.Y.9    Wei, Y.Q.10
  • 17
    • 14844347928 scopus 로고    scopus 로고
    • Bacterial topoisomerase inhibitors: Quinolone and pyridone antibacterial agents
    • DOI 10.1021/cr030101q
    • Mitscher LA. 2005. Bacterial topoisomerase inhibitors: quinolone and pyridone antibacterial agents. Chem. Rev. 105:559-592. http://dx.doi.org/10. 1021/cr030101q. (Pubitemid 40351634)
    • (2005) Chemical Reviews , vol.105 , Issue.2 , pp. 559-592
    • Mitscher, L.A.1
  • 19
    • 0036890871 scopus 로고    scopus 로고
    • From genetics and genomics to drug discovery: Yeast rises to the challenge
    • DOI 10.1016/S0165-6147(02)02097-7, PII S0165614702020977
    • Melese T, Hieter P. 2002. From genetics and genomics to drug discovery: yeast rises to the challenge. Trends Pharmacol. Sci. 23:544-547. http://dx.doi.org/10.1016/S0165-6147(02)02097-7. (Pubitemid 35375795)
    • (2002) Trends in Pharmacological Sciences , vol.23 , Issue.12 , pp. 544-547
    • Melese, T.1    Hieter, P.2
  • 20
    • 0036726470 scopus 로고    scopus 로고
    • Yeast and drug discovery
    • DOI 10.1007/s10142-002-0059-1
    • Hughes TR. 2002. Yeast and drug discovery. Funct. Integr. Genomics 2:199-211. http://dx.doi.org/10.1007/s10142-002-0059-1. (Pubitemid 41449154)
    • (2002) Functional and Integrative Genomics , vol.2 , Issue.4-5 , pp. 199-211
    • Hughes, T.R.1
  • 21
    • 84870652808 scopus 로고    scopus 로고
    • Discovering thiamine transporters as targets of chloroquine using a novel functional genomics strategy
    • Huang ZW, Srinivasan S, Zhang JH, Chen KF, Li YX, Li W, Quiocho FA, Pan XW. 2012. Discovering thiamine transporters as targets of chloroquine using a novel functional genomics strategy. PloS Genet. 8:e1003083. http://dx.doi.org/ 10.1371/journal.pgen.1003083.
    • (2012) PloS Genet. , vol.8
    • Huang, Z.W.1    Srinivasan, S.2    Zhang, J.H.3    Chen, K.F.4    Li, Y.X.5    Li, W.6    Quiocho, F.A.7    Pan, X.W.8
  • 22
    • 0036174441 scopus 로고    scopus 로고
    • Relationship between chloroquine toxicity and iron acquisition in Saccharomyces cerevisiae
    • DOI 10.1128/AAC.46.3.787-796.2002
    • Emerson LR, Nau ME, Martin RK, Kyle DE, Vahey M, Wirth DF. 2002. Relationship between chloroquine toxicity and iron acquisition in Saccharomyces cerevisiae. Antimicrob. Agents Chemother. 46:787-796. http://dx.doi.org/10.1128/ AAC.46.3.787-796.2002. (Pubitemid 34157665)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.3 , pp. 787-796
    • Emerson, L.R.1    Nau, M.E.2    Martin, R.K.3    Kyle, D.E.4    Vahey, M.5    Wirth, D.F.6
  • 23
    • 4544352024 scopus 로고    scopus 로고
    • The sensitivities of yeast strains deficient in PDR ABC transporters, to quinoline-ring antimalarial drugs
    • Emerson LR, Skillman BC, Wolfger H, Kuchler K, Wirth DF. 2004. The sensitivities of yeast strains deficient in PDR ABC transporters, to quinoline-ring antimalarial drugs. Ann. Trop. Med. Parasit. 98:643-649. http://dx.doi.org/10.1179/000349804225021523.
    • (2004) Ann. Trop. Med. Parasit. , vol.98 , pp. 643-649
    • Emerson, L.R.1    Skillman, B.C.2    Wolfger, H.3    Kuchler, K.4    Wirth, D.F.5
  • 24
    • 0032910168 scopus 로고    scopus 로고
    • Organization and regulation of mitogen-activated protein kinase signaling pathways
    • DOI 10.1016/S0955-0674(99)80028-3
    • Garrington TP, Johnson GL. 1999. Organization and regulation of mitogen-activated protein kinase signaling pathways. Curr. Opin. Cell Biol. 11:211-218. http://dx.doi.org/10.1016/S0955-0674(99)80028-3. (Pubitemid 29164036)
    • (1999) Current Opinion in Cell Biology , vol.11 , Issue.2 , pp. 211-218
    • Garrington, T.P.1    Johnson, G.L.2
  • 25
    • 0036282743 scopus 로고    scopus 로고
    • Osmotic stress signaling and osmoadaptation in yeasts
    • DOI 10.1128/MMBR.66.2.300-372.2002
    • Hohmann S. 2002. Osmotic stress signaling and osmoadaptation in yeasts. Microbiol. Mol. Biol. Rev. 66:300-372. http://dx.doi.org/10.1128/MMBR.66.2.300- 372.2002. (Pubitemid 34625712)
    • (2002) Microbiology and Molecular Biology Reviews , vol.66 , Issue.2 , pp. 300-372
    • Hohmann, S.1
  • 26
    • 15944365872 scopus 로고    scopus 로고
    • Chloroquine induces the expression of inducible nitric oxide synthase in C6 glioma cells
    • Chen TH, Chang PC, Chang MC, Lin YF, Lee HM. 2005. Chloroquine induces the expression of inducible nitric oxide synthase in C6 glioma cells. Pharmacol. Res. 51:329-336. http://dx.doi.org/10.1016/j.phrs.2004.10.004.
    • (2005) Pharmacol. Res. , vol.51 , pp. 329-336
    • Chen, T.H.1    Chang, P.C.2    Chang, M.C.3    Lin, Y.F.4    Lee, H.M.5
  • 28
    • 84874777959 scopus 로고    scopus 로고
    • Depletion of cellular iron by curcumin leads to alteration in histone acetylation and degradation of Sml1p in Saccharomyces cerevisiae
    • Azad GK, Singh V, Golla U, Tomar RS. 2013. Depletion of cellular iron by curcumin leads to alteration in histone acetylation and degradation of Sml1p in Saccharomyces cerevisiae. PLoS One 8:e59003. http://dx.doi.org/10.1371/journal. pone.0059003.
    • (2013) PLoS One , vol.8
    • Azad, G.K.1    Singh, V.2    Golla, U.3    Tomar, R.S.4
  • 29
    • 83955161230 scopus 로고    scopus 로고
    • Multifunctional Ebselen drug functions through the activation of DNA damage response and alterations in nuclear proteins
    • Azad GK, Balkrishna SJ, Sathish N, Kumar S, Tomar RS. 2012. Multifunctional Ebselen drug functions through the activation of DNA damage response and alterations in nuclear proteins. Biochem. Pharmacol. 83:296-303. http://dx.doi.org/10.1016/j.bcp.2011.10.011.
    • (2012) Biochem. Pharmacol. , vol.83 , pp. 296-303
    • Azad, G.K.1    Balkrishna, S.J.2    Sathish, N.3    Kumar, S.4    Tomar, R.S.5
  • 31
    • 84900355024 scopus 로고    scopus 로고
    • Anti-cancer drug KP1019 induces Hog1 phosphorylation and protein ubiquitylation in Saccharomyces cerevisiae
    • 2 May
    • Singh V, Azad GK, Reddy M A, Baranwal S, Tomar RS. 2 May 2014. Anti-cancer drug KP1019 induces Hog1 phosphorylation and protein ubiquitylation in Saccharomyces cerevisiae. Eur. J. Pharmacol. http://dx.doi.org/10.1016/j. ejphar.2014.04.032.
    • (2014) Eur. J. Pharmacol.
    • Singh, V.1    Azad, G.K.2    Reddy, M.A.3    Baranwal, S.4    Tomar, R.S.5
  • 32
    • 84896071887 scopus 로고    scopus 로고
    • Anti-cancer drug KP1019 modulates epigenetics and induces DNA damage response in Saccharomyces cerevisiae
    • 20 February
    • Singh V, Azad GK, Mandal P, Reddy MA, Tomar RS. 20 February 2014. Anti-cancer drug KP1019 modulates epigenetics and induces DNA damage response in Saccharomyces cerevisiae. FEBS Lett. http://dx.doi.org/10.1016/j.febslet.2014. 02.017.
    • (2014) FEBS Lett.
    • Singh, V.1    Azad, G.K.2    Mandal, P.3    Reddy, M.A.4    Tomar, R.S.5
  • 33
    • 84892549203 scopus 로고    scopus 로고
    • Ebselen induces reactive oxygen species (ROS)-mediated cytotoxicity in Saccharomyces cerevisiae with inhibition of glutamate dehydrogenase being a target
    • 6 January
    • Azad GK, Singh V, Mandal P, Singh P, Golla U, Baranwal S, Chauhan S, Tomar RS. 6 January 2014. Ebselen induces reactive oxygen species (ROS)-mediated cytotoxicity in Saccharomyces cerevisiae with inhibition of glutamate dehydrogenase being a target. FEBS Open Bio http://dx.doi.org/10.1016/j.fob. 2014.01.002.
    • (2014) FEBS Open Bio
    • Azad, G.K.1    Singh, V.2    Mandal, P.3    Singh, P.4    Golla, U.5    Baranwal, S.6    Chauhan, S.7    Tomar, R.S.8
  • 34
    • 84878564641 scopus 로고    scopus 로고
    • Sen1p contributes to genomic integrity by regulating expression of ribonucleotide reductase 1 (RNR1) in Saccharomyces cerevisiae
    • Golla U, Singh V, Azad GK, Singh P, Verma N, Mandal P, Chauhan S, Tomar RS. 2013. Sen1p contributes to genomic integrity by regulating expression of ribonucleotide reductase 1 (RNR1) in Saccharomyces cerevisiae. PLoS One 8:e64798. http://dx.doi.org/10.1371/journal.pone.0064798.
    • (2013) PLoS One , vol.8
    • Golla, U.1    Singh, V.2    Azad, G.K.3    Singh, P.4    Verma, N.5    Mandal, P.6    Chauhan, S.7    Tomar, R.S.8
  • 35
    • 0035710746 scopus 로고    scopus 로고
    • -DeltaDeltaCT method
    • DOI 10.1006/meth.2001.1262
    • Livak KJ, Schmittgen TD. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 25:402-408. http://dx.doi.org/10.1006/meth.2001.1262. (Pubitemid 34164012)
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 36
    • 79961040225 scopus 로고    scopus 로고
    • Analysis of chloroquine resistance transporter (CRT) isoforms and orthologues in S. cerevisiae yeast
    • Baro NK, Pooput C, Roepe PD. 2011. Analysis of chloroquine resistance transporter (CRT) isoforms and orthologues in S. cerevisiae yeast. Biochemistry 50:6701-6710. http://dx.doi.org/10.1021/bi200922g.
    • (2011) Biochemistry , vol.50 , pp. 6701-6710
    • Baro, N.K.1    Pooput, C.2    Roepe, P.D.3
  • 38
    • 84879195625 scopus 로고    scopus 로고
    • Function of resistance conferring Plasmodium falciparum Chloroquine resistance transporter isoforms
    • Baro NK, Callaghan PS, Roepe PD. 2013. Function of resistance conferring Plasmodium falciparum Chloroquine resistance transporter isoforms. Biochemistry 52:4242-4249. http://dx.doi.org/10.1021/bi400557x.
    • (2013) Biochemistry , vol.52 , pp. 4242-4249
    • Baro, N.K.1    Callaghan, P.S.2    Roepe, P.D.3
  • 39
    • 70349319850 scopus 로고    scopus 로고
    • Hydroxychloroquine, chloroquine, and alltrans retinoic acid regulate growth, survival, and histone acetylation in breast cancer cells
    • Rahim R, Strobl JS. 2009. Hydroxychloroquine, chloroquine, and alltrans retinoic acid regulate growth, survival, and histone acetylation in breast cancer cells. Anti-Cancer Drugs 20:736-745. http://dx.doi.org/10.1097/CAD. 0b013e32832f4e50.
    • (2009) Anti-Cancer Drugs , vol.20 , pp. 736-745
    • Rahim, R.1    Strobl, J.S.2
  • 40
    • 0028228109 scopus 로고
    • A two-component system that regulates an osmosensing MAP kinase cascade in yeast
    • DOI 10.1038/369242a0
    • Maeda T, Wurgler-Murphy SM, Saito H. 1994. A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature 369:242-245. http://dx.doi.org/10.1038/369242a0. (Pubitemid 24154803)
    • (1994) Nature , vol.369 , Issue.6477 , pp. 242-245
    • Maeda, T.1    Wurgler-Murphy, S.M.2    Saito, H.3
  • 41
    • 0034696963 scopus 로고    scopus 로고
    • Stimulation of the yeast high osmolarity glycerol (HOG) pathway: Evidence for a signal generated by a change in turgor rather than by water stress
    • DOI 10.1016/S0014-5793(00)01445-9, PII S0014579300014459
    • Tamás MJ, Rep M, Thevelein JM, Hohmann S. 2000. Stimulation of the yeast high osmolarity glycerol (HOG) pathway: evidence for a signal generated by a change in turgor rather than by water stress. FEBS Lett. 472:159-165. http://dx.doi.org/10.1016/S0014-5793(00)01445-9. (Pubitemid 30224606)
    • (2000) FEBS Letters , vol.472 , Issue.1 , pp. 159-165
    • Tamas, M.J.1    Rep, M.2    Thevelein, J.M.3    Hohmann, S.4
  • 42
    • 0034708436 scopus 로고    scopus 로고
    • The transcriptional response of Saccharomyces cerevisiae to osmotic shock. Hot1p and Msn2p/Msn4p are required for the induction of subsets of high osmolarity glycerol pathway-dependent genes
    • DOI 10.1074/jbc.275.12.8290
    • Rep M, Krantz M, Thevelein JM, Hohmann S. 2000. The transcriptional response of Saccharomyces cerevisiae to osmotic shock. Hot1p and Msn2p/Msn4p are required for the induction of subsets of high osmolarity glycerol pathway-dependent genes. J. Biol. Chem. 275:8290-8300. http://dx.doi.org/10. 1074/jbc.275.12.8290. (Pubitemid 30180168)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.12 , pp. 8290-8300
    • Rep, M.1    Krantz, M.2    Thevelein, J.M.3    Hohmann, S.4
  • 43
    • 0032814143 scopus 로고    scopus 로고
    • Osmotic stress-induced gene expression in Saccharomyces cerevisiae requires Msn1p and the novel nuclear factor Hot1p
    • Rep M, Reiser V, Gartner U, Thevelein JM, Hohmann S, Ammerer G, Ruis H. 1999. Osmotic stress-induced gene expression in Saccharomyces cerevisiae requires Msn1p and the novel nuclear factor Hot1p. Mol. Cell. Biol. 19:5474-5485. (Pubitemid 29339905)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.8 , pp. 5474-5485
    • Rep, M.1    Reiser, V.2    Gartner, U.3    Thevelein, J.M.4    Hohmann, S.5    Ammerer, G.6    Ruis, H.7
  • 44
    • 0032189837 scopus 로고    scopus 로고
    • Regulated nucleo/cytoplasmic exchange of HOG1 MAPK requires the importin beta homologs NMD5 and XPO1
    • DOI 10.1093/emboj/17.19.5606
    • Ferrigno P, Posas F, Koepp D, Saito H, Silver PA. 1998. Regulated nucleo/cytoplasmic exchange of HOG1 MAPK requires the importin beta homologs NMD5 and XPO1. EMBO J. 17:5606-5614. http://dx.doi.org/10.1093/emboj/17.19.5606. (Pubitemid 28445972)
    • (1998) EMBO Journal , vol.17 , Issue.19 , pp. 5606-5614
    • Ferrigno, P.1    Posas, F.2    Koepp, D.3    Saito, H.4    Silver, P.A.5
  • 45
    • 33745959274 scopus 로고    scopus 로고
    • The Stress-Activated Hog1 Kinase Is a Selective Transcriptional Elongation Factor for Genes Responding to Osmotic Stress
    • DOI 10.1016/j.molcel.2006.05.031, PII S1097276506003467
    • Proft M, Mas G, de Nadal E, Vendrell A, Noriega N, Struhl K, Posas F. 2006. The stress-activated Hog1 kinase is a selective transcriptional elongation factor for genes responding to osmotic stress. Mol. Cell 23:241-250. http://dx.doi.org/10.1016/j.molcel.2006.05.031. (Pubitemid 44062368)
    • (2006) Molecular Cell , vol.23 , Issue.2 , pp. 241-250
    • Proft, M.1    Mas, G.2    De Nadal, E.3    Vendrell, A.4    Noriega, N.5    Struhl, K.6    Posas, F.7
  • 46
    • 0032933350 scopus 로고    scopus 로고
    • Repressors and upstream repressing sequences of the stress-regulated ENA1 gene in Saccharomyces cerevisiae: bZIP protein Sko1p confers HOG- dependent osmotic regulation
    • Proft M, Serrano R. 1999. Repressors and upstream repressing sequences of the stress-regulated ENA1 gene in Saccharomyces cerevisiae: bZIP protein Sko1p confers HOG-dependent osmotic regulation. Mol. Cell. Biol. 19:537-546. (Pubitemid 29018455)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.1 , pp. 537-546
    • Proft, M.1    Serrano, R.2
  • 47
    • 0035282906 scopus 로고    scopus 로고
    • Regulation of the Sko1 transcriptional repressor by the Hog1 MAP kinase in response to osmotic stress
    • DOI 10.1093/emboj/20.5.1123
    • Proft M, Pascual-Ahuir A, de Nadal E, Arino J, Serrano R, Posas F. 2001. Regulation of the Sko1 transcriptional repressor by the Hog1 MAP kinase in response to osmotic stress.EMBOJ. 20:1123-1133. http://dx.doi.org/10.1093/emboj/ 20.5.1123. (Pubitemid 32186802)
    • (2001) EMBO Journal , vol.20 , Issue.5 , pp. 1123-1133
    • Proft, M.1    Pascual-Ahuir, A.2    De Nadal, E.3    Ario, J.4    Serrano, R.5    Posas, F.6
  • 48
    • 0028302033 scopus 로고
    • GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway
    • Albertyn J, Hohmann S, Thevelein JM, Prior BA. 1994. GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway. Mol. Cell. Biol. 14:4135-4144.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4135-4144
    • Albertyn, J.1    Hohmann, S.2    Thevelein, J.M.3    Prior, B.A.4
  • 50
    • 67449102906 scopus 로고    scopus 로고
    • The high osmotic response and cell wall integrity pathways cooperate to regulate transcriptional responses to zymolyase-induced cell wall stress in Saccharomyces cerevisiae
    • García R, Rodríguez-Peña JM, Bermejo C, Nombela C, Arroyo J. 2009. The high osmotic response and cell wall integrity pathways cooperate to regulate transcriptional responses to zymolyase-induced cell wall stress in Saccharomyces cerevisiae. J. Biol. Chem. 284:10901-10911. http://dx.doi.org/10.1074/jbc.M808693200.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10901-10911
    • García, R.1    Rodríguez-Peña, J.M.2    Bermejo, C.3    Nombela, C.4    Arroyo, J.5
  • 51
    • 84899713980 scopus 로고    scopus 로고
    • Assessment of the biological pathways targeted by isocyanate using N-succinimidyl N-methylcarbamate in budding yeast Saccharomyces cerevisiae
    • Azad GK, Singh V, Tomar RS. 2014. Assessment of the biological pathways targeted by isocyanate using N-succinimidyl N-methylcarbamate in budding yeast Saccharomyces cerevisiae. PLoS One 9:e92993. http://dx.doi.org/10.1371/journal. pone.0092993.
    • (2014) PLoS One , vol.9
    • Azad, G.K.1    Singh, V.2    Tomar, R.S.3
  • 52
    • 0027531645 scopus 로고
    • An osmosensing signal transduction pathway in yeast
    • Brewster JL, de Valoir T, Dwyer ND, Winter E, Gustin MC. 1993. An osmosensing signal transduction pathway in yeast. Science 259: 1760-1763. http://dx.doi.org/10.1126/science.7681220. (Pubitemid 23114664)
    • (1993) Science , vol.259 , Issue.5102 , pp. 1760-1763
    • Brewster, J.L.1    De Valoir, T.2    Dwyer, N.D.3    Winter, E.4    Gustin, M.C.5
  • 53
    • 4644229317 scopus 로고    scopus 로고
    • Rck1 and Rck2 MAPKAP kinases and the HOG pathway are required for oxidative stress resistance
    • DOI 10.1111/j.1365-2958.2004.04238.x
    • Bilsland E, Molin C, Swaminathan S, Ramne A, Sunnerhagen P. 2004. Rck1 and Rck2 MAPKAP kinases and the HOG pathway are required for oxidative stress resistance. Mol. Microbiol. 53:1743-1756. http://dx.doi.org/10.1111/j.1365-2958. 2004.04238.x. (Pubitemid 39265319)
    • (2004) Molecular Microbiology , vol.53 , Issue.6 , pp. 1743-1756
    • Bilsland, E.1    Molin, C.2    Swaminathan, S.3    Ramne, A.4    Sunnerhagen, P.5
  • 54
    • 0038735200 scopus 로고    scopus 로고
    • The Hog1 mitogen-activated protein kinase is essential in the oxidative stress response and chlamydospore formation in Candida albicans
    • DOI 10.1128/EC.2.2.351-361.2003
    • Alonso-Monge R, Navarro-Garcia F, Roman E, Negredo AI, Eisman B, Nombela C, Pla J. 2003. The Hog1 mitogen-activated protein kinase is essential in the oxidative stress response and chlamydospore formation in Candida albicans. Eukaryot. Cell 2:351-361. http://dx.doi.org/10.1128/EC.2.2.351-361.2003. (Pubitemid 36562374)
    • (2003) Eukaryotic Cell , vol.2 , Issue.2 , pp. 351-361
    • Alonso-Monge, R.1    Navarro-Garcia, F.2    Roman, E.3    Negredo, A.I.4    Eisman, B.5    Nombela, C.6    Pla, J.7
  • 55
    • 0036548318 scopus 로고    scopus 로고
    • Heat stress activates the yeast high-osmolarity glycerol mitogen-activated protein kinase pathway, and protein tyrosine phosphatases are essential under heat stress
    • DOI 10.1128/EC.1.2.163-173.2002
    • Winkler A, Arkind C, Mattison CP, Burkholder A, Knoche K, Ota I. 2002. Heat stress activates the yeast high-osmolarity glycerol mitogen-activated protein kinase pathway, and protein tyrosine phosphatases are essential under heat stress. Eukaryot. Cell 1:163-173. http://dx.doi.org/10.1128/EC.1.2.163-173. 2002. (Pubitemid 36562393)
    • (2002) Eukaryotic Cell , vol.1 , Issue.2 , pp. 163-173
    • Winkler, A.1    Arkind, C.2    Mattison, C.P.3    Burkholder, A.4    Knoche, K.5    Ota, I.6
  • 56
    • 1842453025 scopus 로고    scopus 로고
    • Evidence of a New Role for the High-Osmolarity Glycerol Mitogen-Activated Protein Kinase Pathway in Yeast: Regulating Adaptation to Citric Acid Stress
    • DOI 10.1128/MCB.24.8.3307-3323.2004
    • Lawrence CL, Botting CH, Antrobus R, Coote PJ. 2004. Evidence of a new role for the high-osmolarity glycerol mitogen-activated protein kinase pathway in yeast: regulating adaptation to citric acid stress. Mol. Cell. Biol. 24:3307-3323. http://dx.doi.org/10.1128/MCB.24.8.3307-3323.2004. (Pubitemid 38452075)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.8 , pp. 3307-3323
    • Lawrence, C.L.1    Botting, C.H.2    Antrobus, R.3    Coote, P.J.4
  • 57
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • Han J, Lee JD, Bibbs L, Ulevitch RJ. 1994. A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265:808-811. http://dx.doi.org/10.1126/science.7914033. (Pubitemid 24266145)
    • (1994) Science , vol.265 , Issue.5173 , pp. 808-811
    • Man, J.1    Lee, J.-D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 58
    • 1642580754 scopus 로고    scopus 로고
    • The MAPK Hog1 recruits Rpd3 histone deacetylase to activate osmoresponsive genes
    • DOI 10.1038/nature02258
    • De Nadal E, Zapater M, Alepuz PM, Sumoy L, Mas G, Posas F. 2004. The MAPK Hog1 recruits Rpd3 histone deacetylase to activate osmoresponsive genes. Nature 427:370-374. http://dx.doi.org/10.1038/nature02258. (Pubitemid 38133666)
    • (2004) Nature , vol.427 , Issue.6972 , pp. 370-374
    • De Nadal, E.1    Zapater, M.2    Alepuz, P.M.3    Sumoy, L.4    Mas, G.5    Posas, F.6
  • 59
    • 0034610367 scopus 로고    scopus 로고
    • Genomewide studies of histone deacetylase function in yeast
    • Bernstein BE, Tong JK, Schreiber SL. 2000. Genomewide studies of histone deacetylase function in yeast. Proc. Natl. Acad. Sci. U. S. A. 97:13708-13713. http://dx.doi.org/10.1073/pnas.250477697.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 13708-13713
    • Bernstein, B.E.1    Tong, J.K.2    Schreiber, S.L.3
  • 60
    • 0037380209 scopus 로고    scopus 로고
    • Histone acetylation and deacetylation in yeast
    • DOI 10.1038/nrm1075
    • Kurdistani SK, Grunstein M. 2003. Histone acetylation and deacetylation in yeast. Nat. Rev. Mol. Cell Biol. 4:276-284. http://dx.doi.org/10.1038/ nrm1075. (Pubitemid 36383954)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.4 , pp. 276-284
    • Kurdistani, S.K.1    Grunstein, M.2
  • 61
    • 0032960856 scopus 로고    scopus 로고
    • Kinase activity-dependent nuclear export opposes stress-induced nuclear accumulation and retention of Hog1 mitogen-activated protein kinase in the budding yeast Saccharomyces cerevisiae
    • Reiser V, Ruis H, Ammerer G. 1999. Kinase activity-dependent nuclear export opposes stress-induced nuclear accumulation and retention of Hog1 mitogen-activated protein kinase in the budding yeast Saccharomyces cerevisiae. Mol. Biol. Cell 10:1147-1161. http://dx.doi.org/10.1091/mbc.10.4.1147. (Pubitemid 29193737)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.4 , pp. 1147-1161
    • Reiser, V.1    Ruis, H.2    Ammerer, G.3
  • 62
    • 0742288061 scopus 로고    scopus 로고
    • Unique and Redundant Roles for HOG MAPK Pathway Components as Revealed by Whole-Genome Expression Analysis
    • DOI 10.1091/mbc.E03-07-0521
    • O'Rourke SM, Herskowitz I. 2004. Unique and redundant roles for HOG MAPK pathway components as revealed by whole-genome expression analysis. Mol. Biol. Cell 15:532-542. http://dx.doi.org/10.1091/mbc.E03-07-0521. (Pubitemid 38146471)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.2 , pp. 532-542
    • O'Rourke, S.M.1    Herskowitz, I.2
  • 63
    • 0029841921 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and activation of a new mitogen-activated protein (MAP)-kinase cascade in human neutrophils stimulated with various agonists
    • Nahas N, Molski TF, Fernandez GA, Sha'afi RI. 1996. Tyrosine phosphorylation and activation of a new mitogen-activated protein (MAP)-kinase cascade in human neutrophils stimulated with various agonists. Biochem. J. 318(Pt 1):247-253. (Pubitemid 26283653)
    • (1996) Biochemical Journal , vol.318 , Issue.1 , pp. 247-253
    • Nahas, N.1    Molski, T.F.P.2    Fernandez, G.A.3    Sha'afi, R.I.4
  • 65
    • 0028055202 scopus 로고
    • Characterization of the osmotic-stress response in Saccharomyces cerevisiae: Osmotic stress and glucose repression regulate glycerol-3-phosphate dehydrogenase independently
    • DOI 10.1007/BF00712960
    • Albertyn J, Hohmann S, Prior BA. 1994. Characterization of the osmotic-stress response in Saccharomyces cerevisiae: osmotic stress and glucose repression regulate glycerol-3-phosphate dehydrogenase independently. Curr. Genet. 25:12-18. http://dx.doi.org/10.1007/BF00712960. (Pubitemid 24006197)
    • (1994) Current Genetics , vol.25 , Issue.1 , pp. 12-18
    • Albertyn, J.1    Hohmann, S.2    Prior, B.A.3
  • 66
    • 0031474318 scopus 로고    scopus 로고
    • Osmoregulation and glycerol metabolism in the yeast Saccharomyces cerevisiae
    • DOI 10.1016/S0168-6445(97)00058-2, PII S0168644597000582
    • Nevoigt E, Stahl U. 1997. Osmoregulation and glycerol metabolism in the yeast Saccharomyces cerevisiae. FEMS Microbiol. Rev. 21:231-241. http://dx.doi.org/10.1111/j.1574-6976.1997.tb00352.x. (Pubitemid 28018203)
    • (1997) FEMS Microbiology Reviews , vol.21 , Issue.3 , pp. 231-241
    • Nevoigt, E.1    Stahl, U.2
  • 67
    • 0025785813 scopus 로고
    • Osmoregulation in Saccharomyces cerevisiae. Studies on the osmotic induction of glycerol production and glycerol-3-phosphate dehydrogenase (NAD+)
    • André L, Hemming A, Adler L. 1991. Osmoregulation in Saccharomyces cerevisiae. Studies on the osmotic induction of glycerol production and glycerol-3-phosphate dehydrogenase (NAD+). FEBS Lett. 286:13-17.
    • (1991) FEBS Lett. , vol.286 , pp. 13-17
    • André, L.1    Hemming, A.2    Adler, L.3
  • 68
    • 0024614329 scopus 로고
    • Roles of glycerol and glycerol-3-phosphate dehydrogenase (NAD+) in acquired osmotolerance of Saccharomyces cerevisiae
    • Blomberg A, Adler L. 1989. Roles of glycerol and glycerol-3-phosphate dehydrogenase (NAD+) in acquired osmotolerance of Saccharomyces cerevisiae. J. Bacteriol. 171:1087-1092.
    • (1989) J. Bacteriol. , vol.171 , pp. 1087-1092
    • Blomberg, A.1    Adler, L.2
  • 71
    • 1642576083 scopus 로고    scopus 로고
    • Stress-specific activation mechanisms for the "cell integrity"MAPKpathway in Saccharomyces cerevisiae
    • Harrison JC, Bardes EG, Zyla TR, Lew DJ. 2002. Stress-specific activation mechanisms for the "cell integrity"MAPKpathway in Saccharomyces cerevisiae. Mol. Biol. Cell 13:294a-294a. http://dx.doi.org/10.1074/jbc. M306110200.
    • (2002) Mol. Biol. Cell , vol.13
    • Harrison, J.C.1    Bardes, E.G.2    Zyla, T.R.3    Lew, D.J.4
  • 72
    • 1242316941 scopus 로고    scopus 로고
    • Oxidative stress in malaria parasite-infected erythrocytes: Host-parasite interactions
    • DOI 10.1016/j.ijpara.2003.09.011
    • Becker K, Tilley L, Vennerstrom JL, Roberts D, Rogerson S, Ginsburg H. 2004. Oxidative stress in malaria parasite-infected erythrocytes: host-parasite interactions. Int. J. Parasitol. 34:163-189. http://dx.doi.org/10.1016/j.ijpara. 2003.09.011. (Pubitemid 38229822)
    • (2004) International Journal for Parasitology , vol.34 , Issue.2 , pp. 163-189
    • Becker, K.1    Tilley, L.2    Vennerstrom, J.L.3    Roberts, D.4    Rogerson, S.5    Ginsburg, H.6
  • 73
    • 0033560719 scopus 로고    scopus 로고
    • Inhibition of the peroxidative degradation of haem as the basis of action of chloroquine and other quinoline antimalarials
    • DOI 10.1042/0264-6021:3390363
    • Loria P, Miller S, Foley M, Tilley L. 1999. Inhibition of the peroxidative degradation of haem as the basis of action of chloroquine and other quinoline antimalarials. Biochem. J. 339:363-370. http://dx.doi.org/10.1042/ 0264-6021:3390363. (Pubitemid 29209967)
    • (1999) Biochemical Journal , vol.339 , Issue.2 , pp. 363-370
    • Loria, P.1    Miller, S.2    Foley, M.3    Tilley, L.4
  • 74
    • 0015337837 scopus 로고
    • High-resolution autoradiography of malarial parasites treated with 3 H-chloroquine
    • Aikawa M. 1972. High-resolution autoradiography of malarial parasites treated with 3 H-chloroquine. Am. J. Pathol. 67:277-284.
    • (1972) Am. J. Pathol. , vol.67 , pp. 277-284
    • Aikawa, M.1
  • 75
    • 0345652158 scopus 로고
    • Identification of the acidic compartment of Plasmodium falciparum-infected human erythrocytes as the target of the antimalarial drug chloroquine
    • Yayon A, Cabantchik ZI, Ginsburg H. 1984. Identification of the acidic compartment of Plasmodium falciparum-infected human erythrocytes as the target of the antimalarial drug chloroquine. EMBO J. 3:2695-2700.
    • (1984) EMBO J. , vol.3 , pp. 2695-2700
    • Yayon, A.1    Cabantchik, Z.I.2    Ginsburg, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.