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Volumn 5, Issue 2, 2015, Pages 318-342

Oxidative stress in fungi: Its function in signal transduction, interaction with plant hosts, and lignocellulose degradation

Author keywords

Hydrogen peroxide; Hydroxyl radical; Integral membrane reductases; Lignin degradation; Mitochondria; NADPH oxidase; Oxidative stress; Peroxiredoxin; Protein disulfide isomerase; Superoxide radical anion

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 1; ADENOSINE TRIPHOSPHATE; ARABIDOPSIS PROTEIN; CATALASE; CHAPERONIN; EPIDERMAL GROWTH FACTOR RECEPTOR; FLAVINE ADENINE NUCLEOTIDE; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; LIGNIN PEROXIDASE; LIGNOCELLULOSE; MANGANESE PEROXIDASE; MITOGEN ACTIVATED PROTEIN KINASE; PEROXIREDOXIN; PEROXIREDOXIN 1; PEROXIREDOXIN 2; PEROXIREDOXIN 3; PEROXIREDOXIN 4; PEROXIREDOXIN 5; PEROXIREDOXIN 6; PROTEIN DISULFIDE ISOMERASE; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE 1B; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; SUPEROXIDE DISMUTASE; THYROXINE; UNINDEXED DRUG; LIGNIN; OXIDOREDUCTASE; REACTIVE OXYGEN METABOLITE;

EID: 85012109011     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom5020318     Document Type: Review
Times cited : (77)

References (91)
  • 2
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • Winterbourn, C.C. Reconciling the chemistry and biology of reactive oxygen species. Nat. Chem. Biol. 2008, 4, 278-286.
    • (2008) Nat. Chem. Biol , vol.4 , pp. 278-286
    • Winterbourn, C.C.1
  • 3
    • 0030667206 scopus 로고    scopus 로고
    • A yeast mutant showing diagnostic markers of early and late apoptosis
    • Madeo, F.; Frohlich, E.; Frohlich, K.U. A yeast mutant showing diagnostic markers of early and late apoptosis. J. Cell Biol. 1997, 139, 729-734.
    • (1997) J. Cell Biol , vol.139 , pp. 729-734
    • Madeo, F.1    Frohlich, E.2    Frohlich, K.U.3
  • 5
    • 78650598564 scopus 로고    scopus 로고
    • Adaptive response to oxidative stress: Bacteria, fungi, plants and animals
    • Lushchak, V.I. Adaptive response to oxidative stress: Bacteria, fungi, plants and animals. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2011, 153, 175-190.
    • (2011) Comp. Biochem. Physiol. C Toxicol. Pharmacol , vol.153 , pp. 175-190
    • Lushchak, V.I.1
  • 8
    • 10444257943 scopus 로고    scopus 로고
    • Yeast signaling pathways in the oxidative stress response
    • Ikner, A.; Shiozaki, K. Yeast signaling pathways in the oxidative stress response. Mutat. Res. 2005, 569, 13-27.
    • (2005) Mutat. Res , vol.569 , pp. 13-27
    • Ikner, A.1    Shiozaki, K.2
  • 10
    • 0037827692 scopus 로고    scopus 로고
    • Regulation of the transcriptional response to oxidative stress in fungi: Similarities and differences
    • Moye-Rowley, W.S. Regulation of the transcriptional response to oxidative stress in fungi: Similarities and differences. Eukaryot. Cell 2003, 2, 381-389.
    • (2003) Eukaryot. Cell , vol.2 , pp. 381-389
    • Moye-Rowley, W.S.1
  • 11
    • 77950650357 scopus 로고    scopus 로고
    • Oxidative stress in yeast
    • Lushchak, V.I. Oxidative stress in yeast. Biochemistry 2010, 75, 281-296.
    • (2010) Biochemistry , vol.75 , pp. 281-296
    • Lushchak, V.I.1
  • 12
    • 34648813720 scopus 로고    scopus 로고
    • Ros as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • D'Autreaux, B.; Toledano, M.B. Ros as signalling molecules: Mechanisms that generate specificity in ROS homeostasis. Nat. Rev. Mol. Cell Biol. 2007, 8, 813-824.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 813-824
    • D'autreaux, B.1    Toledano, M.B.2
  • 13
    • 84901741434 scopus 로고    scopus 로고
    • Hydrogen peroxide sensing, signaling and regulation of transcription factors
    • Marinho, H.S.; Real, C.; Cyrne, L.; Soares, H.; Antunes, F. Hydrogen peroxide sensing, signaling and regulation of transcription factors. Redox Biol. 2014, 2, 535-562.
    • (2014) Redox Biol , vol.2 , pp. 535-562
    • Marinho, H.S.1    Real, C.2    Cyrne, L.3    Soares, H.4    Antunes, F.5
  • 15
    • 65349113056 scopus 로고    scopus 로고
    • Signaling components of redox active endosomes: The redoxosomes
    • Oakley, F.D.; Abbott, D.; Li, Q.; Engelhardt, J.F. Signaling components of redox active endosomes: The redoxosomes. Antioxid. Redox Signal. 2009, 11, 1313-1333.
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 1313-1333
    • Oakley, F.D.1    Abbott, D.2    Li, Q.3    Engelhardt, J.F.4
  • 16
    • 84872550003 scopus 로고    scopus 로고
    • Sod1 integrates signals from oxygen and glucose to repress respiration
    • Reddi, A.R.; Culotta, V.C. Sod1 integrates signals from oxygen and glucose to repress respiration. Cell 2013, 152, 224-235.
    • (2013) Cell , vol.152 , pp. 224-235
    • Reddi, A.R.1    Culotta, V.C.2
  • 17
    • 79551493261 scopus 로고    scopus 로고
    • Analysis of the peroxiredoxin family: Using active-site structure and sequence information for global classification and residue analysis
    • Nelson, K.J.; Knutson, S.T.; Soito, L.; Klomsiri, C.; Poole, L.B.; Fetrow, J.S. Analysis of the peroxiredoxin family: Using active-site structure and sequence information for global classification and residue analysis. Proteins 2011, 79, 947-964.
    • (2011) Proteins , vol.79 , pp. 947-964
    • Nelson, K.J.1    Knutson, S.T.2    Soito, L.3    Klomsiri, C.4    Poole, L.B.5    Fetrow, J.S.6
  • 18
    • 84858283859 scopus 로고    scopus 로고
    • Measurement of peroxiredoxin activity
    • Nelson, K.J.; Parsonage, D. Measurement of peroxiredoxin activity. Curr. Protoc. Toxicol. 2011, doi:10.1002/0471140856.tx0710s49.
    • (2011) Curr. Protoc. Toxicol
    • Nelson, K.J.1    Parsonage, D.2
  • 19
    • 64149085448 scopus 로고    scopus 로고
    • Typical 2-Cys peroxiredoxins-Structures, mechanisms and functions
    • Hall, A.; Karplus, P.A.; Poole, L.B. Typical 2-Cys peroxiredoxins-Structures, mechanisms and functions. FEBS J. 2009, 276, 2469-2477.
    • (2009) FEBS J , vol.276 , pp. 2469-2477
    • Hall, A.1    Karplus, P.A.2    Poole, L.B.3
  • 20
    • 67651202633 scopus 로고    scopus 로고
    • Peroxiredoxin Tsa1 is the key peroxidase suppressing genome instability and protecting against cell death in Saccharomyces cerevisiae
    • 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 Genet. 2009, 5, e1000524.
    • (2009) Plos Genet , vol.5
    • Iraqui, I.1    Kienda, G.2    Soeur, J.3    Faye, G.4    Baldacci, G.5    Kolodner, R.D.6    Huang, M.E.7
  • 22
    • 84899962183 scopus 로고    scopus 로고
    • Comprehensive analysis of genes involved in the oxidative stress tolerance using yeast heterozygous deletion collection
    • Okada, N.; Ogawa, J.; Shima, J. Comprehensive analysis of genes involved in the oxidative stress tolerance using yeast heterozygous deletion collection. FEMS Yeast Res. 2014, 14, 425-434.
    • (2014) FEMS Yeast Res , vol.14 , pp. 425-434
    • Okada, N.1    Ogawa, J.2    Shima, J.3
  • 23
    • 0000056465 scopus 로고    scopus 로고
    • Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae
    • Park, S.G.; Cha, M.K.; Jeong, W.; Kim, I.H. Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae. J. Biol. Chem. 2000, 275, 5723-5732.
    • (2000) J. Biol. Chem , vol.275 , pp. 5723-5732
    • Park, S.G.1    Cha, M.K.2    Jeong, W.3    Kim, I.H.4
  • 24
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Wood, Z.A.; Poole, L.B.; Karplus, P.A. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 2003, 300, 650-653.
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 25
    • 2342487990 scopus 로고    scopus 로고
    • Cells have distinct mechanisms to maintain protection against different reactive oxygen species: Oxidative-stress-response genes
    • 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. Proc. Natl. Acad. Sci. USA 2004, 101, 6564-6569.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6564-6569
    • Thorpe, G.W.1    Fong, C.S.2    Alic, N.3    Higgins, V.J.4    Dawes, I.W.5
  • 26
    • 84856940017 scopus 로고    scopus 로고
    • Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
    • Rhee, S.G.; Woo, H.A.; Kil, I.S.; Bae, S.H. Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides. J. Biol. Chem. 2012, 287, 4403-4410.
    • (2012) J. Biol. Chem , vol.287 , pp. 4403-4410
    • Rhee, S.G.1    Woo, H.A.2    Kil, I.S.3    Bae, S.H.4
  • 27
    • 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 Dev. 2012, 26, 2001-2008.
    • (2012) Genes Dev , vol.26 , pp. 2001-2008
    • Nystrom, T.1    Yang, J.2    Molin, M.3
  • 28
    • 38749116271 scopus 로고    scopus 로고
    • The peroxiredoxin repair proteins. Subcell
    • Jonsson, T.J.; Lowther, W.T. The peroxiredoxin repair proteins. Subcell. Biochem. 2007, 44, 115-141.
    • (2007) Biochem , vol.44 , pp. 115-141
    • Jonsson, T.J.1    Lowther, W.T.2
  • 29
    • 84859480323 scopus 로고    scopus 로고
    • Protein disulfide isomerase in redox cell signaling and homeostasis
    • Laurindo, F.R.; Pescatore, L.A.; Fernandes Dde, C. Protein disulfide isomerase in redox cell signaling and homeostasis. Free Radic. Biol. Med. 2012, 52, 1954-1969.
    • (2012) Free Radic. Biol. Med , vol.52 , pp. 1954-1969
    • Laurindo, F.R.1    Pescatore, L.A.2    Fernandes Dde, C.3
  • 30
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D.; Walter, P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 2007, 8, 519-529.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 32
    • 35348827324 scopus 로고    scopus 로고
    • That which does not kill me makes me stronger: Adapting to chronic ER stress
    • Rutkowski, D.T.; Kaufman, R.J. That which does not kill me makes me stronger: Adapting to chronic ER stress. Trends Biochem. Sci. 2007, 32, 469-476.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 469-476
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 33
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas, I.; Ron, D. Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat. Cell Biol. 2011, 13, 184-190.
    • (2011) Nat. Cell Biol , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 34
    • 70349341899 scopus 로고    scopus 로고
    • Downstream targets and intracellular compartmentalization in Nox signaling
    • Chen, K.; Craige, S.E.; Keaney, J.F. Downstream targets and intracellular compartmentalization in Nox signaling. Antioxid. Redox Signal. 2009, 11, 2467-2480.
    • (2009) Antioxid. Redox Signal , vol.11 , pp. 2467-2480
    • Chen, K.1    Craige, S.E.2    Keaney, J.F.3
  • 35
    • 46249108461 scopus 로고    scopus 로고
    • Regulation of ROS signal transduction by NADPH oxidase 4 localization
    • Chen, K.; Kirber, M.T.; Xiao, H.; Yang, Y.; Keaney, J.F., Jr. Regulation of ROS signal transduction by NADPH oxidase 4 localization. J. Cell Biol. 2008, 181, 1129-1139.
    • (2008) J. Cell Biol , vol.181 , pp. 1129-1139
    • Chen, K.1    Kirber, M.T.2    Xiao, H.3    Yang, Y.4    Keaney, J.F.5
  • 39
    • 80053513183 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatases by reversible oxidation
    • Ostman, A.; Frijhoff, J.; Sandin, A.; Bohmer, F.D. Regulation of protein tyrosine phosphatases by reversible oxidation. J. Biochem. 2011, 150, 345-356.
    • (2011) J. Biochem , vol.150 , pp. 345-356
    • Ostman, A.1    Frijhoff, J.2    Sandin, A.3    Bohmer, F.D.4
  • 41
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: Revisiting PTPs and the control of cell signaling
    • Tonks, N.K. Redox redux: Revisiting PTPs and the control of cell signaling. Cell 2005, 121, 667-670.
    • (2005) Cell , vol.121 , pp. 667-670
    • Tonks, N.K.1
  • 43
    • 84862777700 scopus 로고    scopus 로고
    • Inactivation of a peroxiredoxin by hydrogen peroxide is critical for thioredoxin-mediated repair of oxidized proteins and cell survival
    • Day, A.M.; Brown, J.D.; Taylor, S.R.; Rand, J.D.; Morgan, B.A.; Veal, E.A. Inactivation of a peroxiredoxin by hydrogen peroxide is critical for thioredoxin-mediated repair of oxidized proteins and cell survival. Mol. Cell 2012, 45, 398-408.
    • (2012) Mol. Cell , vol.45 , pp. 398-408
    • Day, A.M.1    Brown, J.D.2    Taylor, S.R.3    Rand, J.D.4    Morgan, B.A.5    Veal, E.A.6
  • 44
    • 1342326585 scopus 로고    scopus 로고
    • Role of thioredoxin peroxidase in aging of stationary cultures of Saccharomyces cerevisiae
    • Lee, J.H.; Park, J.W. Role of thioredoxin peroxidase in aging of stationary cultures of Saccharomyces cerevisiae. Free Radic. Res. 2004, 38, 225-231.
    • (2004) Free Radic. Res , vol.38 , pp. 225-231
    • Lee, J.H.1    Park, J.W.2
  • 45
    • 79952197002 scopus 로고    scopus 로고
    • A new dominant peroxiredoxin allele identified by whole-genome re-sequencing of random mutagenized yeast causes oxidant-resistance and premature aging
    • Timmermann, B.; Jarolim, S.; Russmayer, H.; Kerick, M.; Michel, S.; Kruger, A.; Bluemlein, K.; Laun, P.; Grillari, J.; Lehrach, H.; et al. A new dominant peroxiredoxin allele identified by whole-genome re-sequencing of random mutagenized yeast causes oxidant-resistance and premature aging. Aging 2010, 2, 475-486.
    • (2010) Aging , vol.2 , pp. 475-486
    • Timmermann, B.1    Jarolim, S.2    Russmayer, H.3    Kerick, M.4    Michel, S.5    Kruger, A.6    Bluemlein, K.7    Laun, P.8    Grillari, J.9    Lehrach, H.10
  • 46
    • 76749102420 scopus 로고    scopus 로고
    • Inactivation of peroxiredoxin I by phosphorylation allows localized H2O2 accumulation for cell signaling
    • Woo, H.A.; Yim, S.H.; Shin, D.H.; Kang, D.; Yu, D.Y.; Rhee, S.G. Inactivation of peroxiredoxin I by phosphorylation allows localized H2O2 accumulation for cell signaling. Cell 2010, 140, 517-528.
    • (2010) Cell , vol.140 , pp. 517-528
    • Woo, H.A.1    Yim, S.H.2    Shin, D.H.3    Kang, D.4    Yu, D.Y.5    Rhee, S.G.6
  • 47
    • 84896823538 scopus 로고    scopus 로고
    • 2-Cys peroxiredoxins: Emerging hubs determining redox dependency of mammalian signaling networks
    • Park, J.; Lee, S.; Lee, S.; Kang, S.W. 2-Cys peroxiredoxins: Emerging hubs determining redox dependency of mammalian signaling networks. Int. J. Cell Biol. 2014, doi:10.1155/2014/715867.
    • (2014) Int. J. Cell Biol
    • Park, J.1    Lee, S.2    Lee, S.3    Kang, S.W.4
  • 49
    • 77957652745 scopus 로고    scopus 로고
    • Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling
    • Miller, E.W.; Dickinson, B.C.; Chang, C.J. Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling. Proc. Natl. Acad. Sci. USA 2010, 107, 15681-15686.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 15681-15686
    • Miller, E.W.1    Dickinson, B.C.2    Chang, C.J.3
  • 50
    • 33646698671 scopus 로고    scopus 로고
    • Hydrogen peroxide: A signaling messenger
    • Stone, J.R.; Yang, S. Hydrogen peroxide: A signaling messenger. Antioxid. Redox Signal. 2006, 8, 243-270.
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 243-270
    • Stone, J.R.1    Yang, S.2
  • 51
    • 84863463209 scopus 로고    scopus 로고
    • Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression
    • Jeong, W.; Bae, S.H.; Toledano, M.B.; Rhee, S.G. Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression. Free Radic. Biol. Med. 2012, 53, 447-456.
    • (2012) Free Radic. Biol. Med , vol.53 , pp. 447-456
    • Jeong, W.1    Bae, S.H.2    Toledano, M.B.3    Rhee, S.G.4
  • 52
    • 53149092498 scopus 로고    scopus 로고
    • Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin
    • Jonsson, T.J.; Tsang, A.W.; Lowther, W.T.; Furdui, C.M. Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin. J. Biol. Chem. 2008, 283, 22890-22894.
    • (2008) J. Biol. Chem , vol.283 , pp. 22890-22894
    • Jonsson, T.J.1    Tsang, A.W.2    Lowther, W.T.3    Furdui, C.M.4
  • 54
    • 53049110477 scopus 로고    scopus 로고
    • Evidence for the formation of a covalent thiosulfinate intermediate with peroxiredoxin in the catalytic mechanism of sulfiredoxin
    • Roussel, X.; Bechade, G.; Kriznik, A.; Van Dorsselaer, A.; Sanglier-Cianferani, S.; Branlant, G.; Rahuel-Clermont, S. Evidence for the formation of a covalent thiosulfinate intermediate with peroxiredoxin in the catalytic mechanism of sulfiredoxin. J. Biol. Chem. 2008, 283, 22371-22382.
    • (2008) J. Biol. Chem , vol.283 , pp. 22371-22382
    • Roussel, X.1    Bechade, G.2    Kriznik, A.3    Van Dorsselaer, A.4    Sanglier-Cianferani, S.5    Branlant, G.6    Rahuel-Clermont, S.7
  • 55
    • 70450240741 scopus 로고    scopus 로고
    • Catalytic mechanism of sulfiredoxin from Saccharomyces cerevisiae passes through an oxidized disulfide sulfiredoxin intermediate that is reduced by thioredoxin
    • Roussel, X.; Kriznik, A.; Richard, C.; Rahuel-Clermont, S.; Branlant, G. Catalytic mechanism of sulfiredoxin from Saccharomyces cerevisiae passes through an oxidized disulfide sulfiredoxin intermediate that is reduced by thioredoxin. J. Biol. Chem. 2009, 284, 33048-33055.
    • (2009) J. Biol. Chem , vol.284 , pp. 33048-33055
    • Roussel, X.1    Kriznik, A.2    Richard, C.3    Rahuel-Clermont, S.4    Branlant, G.5
  • 56
    • 84857914934 scopus 로고    scopus 로고
    • Fungal Aryl-alcohol oxidase: A peroxide-producing flavoenzyme involved in lignin degradation
    • Hernandez-Ortega, A.; Ferreira, P.; Martinez, A.T. Fungal Aryl-alcohol oxidase: A peroxide-producing flavoenzyme involved in lignin degradation. Appl. Microbiol. Biotechnol. 2012, 93, 1395-1410.
    • (2012) Appl. Microbiol. Biotechnol , vol.93 , pp. 1395-1410
    • Hernandez-Ortega, A.1    Ferreira, P.2    Martinez, A.T.3
  • 57
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M.P. How mitochondria produce reactive oxygen species. Biochem. J. 2009, 417, 1-13.
    • (2009) Biochem. J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 58
    • 80054856662 scopus 로고    scopus 로고
    • Mitochondria, reactive oxygen species, and chronological aging: A message from yeast
    • Pan, Y. Mitochondria, reactive oxygen species, and chronological aging: A message from yeast. Exp. Gerontol. 2011, 46, 847-852.
    • (2011) Exp. Gerontol , vol.46 , pp. 847-852
    • Pan, Y.1
  • 59
    • 0345689448 scopus 로고    scopus 로고
    • Reactive oxygen species generated by microbial NADPH oxidase NoxA regulate sexual development in Aspergillus nidulans
    • Lara-Ortiz, T.; Riveros-Rosas, H.; Aguirre, J. Reactive oxygen species generated by microbial NADPH oxidase NoxA regulate sexual development in Aspergillus nidulans. Mol. Microbiol. 2003, 50, 1241-1255.
    • (2003) Mol. Microbiol , vol.50 , pp. 1241-1255
    • Lara-Ortiz, T.1    Riveros-Rosas, H.2    Aguirre, J.3
  • 60
    • 33846794822 scopus 로고    scopus 로고
    • The Nox family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard, K.; Krause, K.H. The Nox family of ROS-generating NADPH oxidases: Physiology and pathophysiology. Physiol. Rev. 2007, 87, 245-313.
    • (2007) Physiol. Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 61
    • 34547852400 scopus 로고    scopus 로고
    • Nox family NADPH oxidases: Not just in mammals
    • Bedard, K.; Lardy, B.; Krause, K.H. Nox family NADPH oxidases: Not just in mammals. Biochimie 2007, 89, 1107-1112.
    • (2007) Biochimie , vol.89 , pp. 1107-1112
    • Bedard, K.1    Lardy, B.2    Krause, K.H.3
  • 62
    • 34948812423 scopus 로고    scopus 로고
    • NADPH oxidases in fungi: Diverse roles of reactive oxygen species in fungal cellular differentiation
    • Takemoto, D.; Tanaka, A.; Scott, B. NADPH oxidases in fungi: Diverse roles of reactive oxygen species in fungal cellular differentiation. Fungal. Genet. Biol. 2007, 44, 1065-1076.
    • (2007) Fungal. Genet. Biol , vol.44 , pp. 1065-1076
    • Takemoto, D.1    Tanaka, A.2    Scott, B.3
  • 63
    • 77956173860 scopus 로고    scopus 로고
    • The Nox/Ferric reductase/ferric reductase-like families of eumycetes
    • Grissa, I.; Bidard, F.; Grognet, P.; Grossetete, S.; Silar, P. The Nox/Ferric reductase/ferric reductase-like families of eumycetes. Fungal Biol. 2010, 114, 766-777.
    • (2010) Fungal Biol , vol.114 , pp. 766-777
    • Grissa, I.1    Bidard, F.2    Grognet, P.3    Grossetete, S.4    Silar, P.5
  • 64
    • 34547697113 scopus 로고    scopus 로고
    • Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox/Duox) family of enzymes
    • Kawahara, B.T.; Quinn, M.T.; Lambeth, J.D. Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox/Duox) family of enzymes. BMCEvol. Biol. 2007, doi:10.1186/1471-2148-7-109.
    • (2007) Bmcevol. Biol
    • Kawahara, B.T.1    Quinn, M.T.2    Lambeth, J.D.3
  • 65
    • 36849064316 scopus 로고    scopus 로고
    • Molecular evolution of phox-related regulatory subunits for NADPH oxidase enzymes
    • Kawahara, T.; Lambeth, J.D. Molecular evolution of phox-related regulatory subunits for NADPH oxidase enzymes. BMC Evol. Biol. 2007, doi:10.1186/1471-2148-7-178.
    • (2007) BMC Evol. Biol
    • Kawahara, T.1    Lambeth, J.D.2
  • 66
    • 84879504272 scopus 로고    scopus 로고
    • Differential roles of NADPH oxidases and associated regulators in polarized growth, conidiation and hyphal fusion in the symbiotic fungus epichloe festucae
    • Kayano, Y.; Tanaka, A.; Akano, F.; Scott, B.; Takemoto, D. Differential roles of NADPH oxidases and associated regulators in polarized growth, conidiation and hyphal fusion in the symbiotic fungus epichloe festucae. Fungal. Genet. Biol. 2013, 56, 87-97.
    • (2013) Fungal. Genet. Biol , vol.56 , pp. 87-97
    • Kayano, Y.1    Tanaka, A.2    Akano, F.3    Scott, B.4    Takemoto, D.5
  • 67
    • 14644437730 scopus 로고    scopus 로고
    • Reactive oxygen species and development in microbial eukaryotes
    • Aguirre, J.; Rios-Momberg, M.; Hewitt, D.; Hansberg, W. Reactive oxygen species and development in microbial eukaryotes. Trends Microbiol. 2005, 13, 111-118.
    • (2005) Trends Microbiol , vol.13 , pp. 111-118
    • Aguirre, J.1    Rios-Momberg, M.2    Hewitt, D.3    Hansberg, W.4
  • 68
    • 4744362719 scopus 로고    scopus 로고
    • Two NADPH oxidase isoforms are required for sexual reproduction and ascospore germination in the filamentous fungus Podospora anserina
    • Malagnac, F.; Lalucque, H.; Lepere, G.; Silar, P. Two NADPH oxidase isoforms are required for sexual reproduction and ascospore germination in the filamentous fungus Podospora anserina. Fungal Genet. Biol. 2004, 41, 982-997.
    • (2004) Fungal Genet. Biol , vol.41 , pp. 982-997
    • Malagnac, F.1    Lalucque, H.2    Lepere, G.3    Silar, P.4
  • 69
    • 43449132091 scopus 로고    scopus 로고
    • NoxA activation by the small gtpase raca is required to maintain a mutualistic symbiotic association between Epichloe festucae and Perennial ryegrass
    • Tanaka, A.; Takemoto, D.; Hyon, G.S.; Park, P.; Scott, B. NoxA activation by the small gtpase raca is required to maintain a mutualistic symbiotic association between Epichloe festucae and Perennial ryegrass. Mol. Microbiol. 2008, 68, 1165-1178.
    • (2008) Mol. Microbiol , vol.68 , pp. 1165-1178
    • Tanaka, A.1    Takemoto, D.2    Hyon, G.S.3    Park, P.4    Scott, B.5
  • 70
    • 70349900168 scopus 로고    scopus 로고
    • Functions and regulation of the Nox family in the filamentous fungus Podospora anserina: A new role in cellulose degradation
    • Brun, S.; Malagnac, F.; Bidard, F.; Lalucque, H.; Silar, P. Functions and regulation of the Nox family in the filamentous fungus Podospora anserina: A new role in cellulose degradation. Mol. Microbiol. 2009, 74, 480-496.
    • (2009) Mol. Microbiol , vol.74 , pp. 480-496
    • Brun, S.1    Malagnac, F.2    Bidard, F.3    Lalucque, H.4    Silar, P.5
  • 71
    • 48949086212 scopus 로고    scopus 로고
    • NADPH oxidases Nox-1 and Nox-2 require the regulatory subunit Nor-1 to control cell differentiation and growth in Neurospora crassa
    • Cano-Dominguez, N.; Alvarez-Delfin, K.; Hansberg, W.; Aguirre, J. NADPH oxidases Nox-1 and Nox-2 require the regulatory subunit Nor-1 to control cell differentiation and growth in Neurospora crassa. Eukaryot. Cell 2008, 7, 1352-1361.
    • (2008) Eukaryot. Cell , vol.7 , pp. 1352-1361
    • Cano-Dominguez, N.1    Alvarez-Delfin, K.2    Hansberg, W.3    Aguirre, J.4
  • 72
  • 74
    • 0037230597 scopus 로고    scopus 로고
    • NADPH oxidase: An enzyme for multicellularity?
    • Lalucque, H.; Silar, P. NADPH oxidase: An enzyme for multicellularity? Trends Microbiol. 2003, 11, 9-12.
    • (2003) Trends Microbiol , vol.11 , pp. 9-12
    • Lalucque, H.1    Silar, P.2
  • 75
    • 0030797706 scopus 로고    scopus 로고
    • Phytopathogenic filamentous (Ashbya, Eremothecium) and dimorphic fungi (Holleya, Nematospora) with needle-shaped ascospores as new members within the Saccharomycetaceae
    • Prillinger, H.; Schweigkofler, W.; Breitenbach, M.; Briza, P.; Staudacher, E.; Lopandic, K.; Molnar, O.; Weigang, F.; Ibl, M.; Ellinger, A. Phytopathogenic filamentous (Ashbya, Eremothecium) and dimorphic fungi (Holleya, Nematospora) with needle-shaped ascospores as new members within the Saccharomycetaceae. Yeast 1997, 13, 945-960.
    • (1997) Yeast , vol.13 , pp. 945-960
    • Prillinger, H.1    Schweigkofler, W.2    Breitenbach, M.3    Briza, P.4    Staudacher, E.5    Lopandic, K.6    Molnar, O.7    Weigang, F.8    Ibl, M.9    Ellinger, A.10
  • 78
    • 33745662410 scopus 로고    scopus 로고
    • Reactive oxygen species signaling in response to pathogens
    • Torres, M.A.; Jones, J.D.; Dangl, J.L. Reactive oxygen species signaling in response to pathogens. Plant Physiol. 2006, 141, 373-378.
    • (2006) Plant Physiol , vol.141 , pp. 373-378
    • Torres, M.A.1    Jones, J.D.2    Dangl, J.L.3
  • 79
    • 34547456941 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by fungal NADPH oxidases is required for rice blast disease
    • Egan, M.J.; Wang, Z.Y.; Jones, M.A.; Smirnoff, N.; Talbot, N.J. Generation of reactive oxygen species by fungal NADPH oxidases is required for rice blast disease. Proc. Natl. Acad. Sci. USA 2007, 104, 11772-11777.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11772-11777
    • Egan, M.J.1    Wang, Z.Y.2    Jones, M.A.3    Smirnoff, N.4    Talbot, N.J.5
  • 80
    • 84887110943 scopus 로고    scopus 로고
    • Proa, a transcriptional regulator of fungal fruiting body development, regulates leaf hyphal network development in the epichloe festucae-lolium perenne symbiosis
    • Tanaka, A.; Cartwright, G.M.; Saikia, S.; Kayano, Y.; Takemoto, D.; Kato, M.; Tsuge, T.; Scott, B. Proa, a transcriptional regulator of fungal fruiting body development, regulates leaf hyphal network development in the epichloe festucae-lolium perenne symbiosis. Mol. Microbiol. 2013, 90, 551-568.
    • (2013) Mol. Microbiol , vol.90 , pp. 551-568
    • Tanaka, A.1    Cartwright, G.M.2    Saikia, S.3    Kayano, Y.4    Takemoto, D.5    Kato, M.6    Tsuge, T.7    Scott, B.8
  • 81
    • 33846347336 scopus 로고    scopus 로고
    • Characterization of a hydroxyl-radical-producing glycoprotein and its presumptive genes from the white-rot basidiomycete Phanerochaete chrysosporium
    • Tanaka, H.; Yoshida, G.; Baba, Y.; Matsumura, K.; Wasada, H.; Murata, J.; Agawa, M.; Itakura, S.; Enoki, A. Characterization of a hydroxyl-radical-producing glycoprotein and its presumptive genes from the white-rot basidiomycete Phanerochaete chrysosporium. J. Biotechnol. 2007, 128, 500-511.
    • (2007) J. Biotechnol , vol.128 , pp. 500-511
    • Tanaka, H.1    Yoshida, G.2    Baba, Y.3    Matsumura, K.4    Wasada, H.5    Murata, J.6    Agawa, M.7    Itakura, S.8    Enoki, A.9
  • 82
    • 84928893704 scopus 로고    scopus 로고
    • Renewable energy. Cellulosic ethanol at last?
    • Service, R.F. Renewable energy. Cellulosic ethanol at last? Science 2014, doi:10.1126/science.345.6201.1111.
    • (2014) Science
    • Service, R.F.1
  • 83
    • 42149110897 scopus 로고    scopus 로고
    • Degradation of cellulose by basidiomycetous fungi
    • Baldrian, P.; Valaskova, V. Degradation of cellulose by basidiomycetous fungi. FEMS Microbiol. Rev. 2008, 32, 501-521.
    • (2008) FEMS Microbiol. Rev , vol.32 , pp. 501-521
    • Baldrian, P.1    Valaskova, V.2
  • 84
    • 81355123362 scopus 로고    scopus 로고
    • Pathways for degradation of lignin in bacteria and fungi
    • Bugg, T.D.; Ahmad, M.; Hardiman, E.M.; Rahmanpour, R. Pathways for degradation of lignin in bacteria and fungi. Nat. Prod. Rep. 2011, 28, 1883-1896.
    • (2011) Nat. Prod. Rep , vol.28 , pp. 1883-1896
    • Bugg, T.D.1    Ahmad, M.2    Hardiman, E.M.3    Rahmanpour, R.4
  • 85
    • 41649104638 scopus 로고    scopus 로고
    • Foly: An integrated database for the classification and functional annotation of fungal oxidoreductases potentially involved in the degradation of lignin and related aromatic compounds
    • Levasseur, A.; Piumi, F.; Coutinho, P.M.; Rancurel, C.; Asther, M.; Delattre, M.; Henrissat, B.; Pontarotti, P.; Asther, M.; Record, E. Foly: An integrated database for the classification and functional annotation of fungal oxidoreductases potentially involved in the degradation of lignin and related aromatic compounds. Fungal Genet. Biol. 2008, 45, 638-645.
    • (2008) Fungal Genet. Biol , vol.45 , pp. 638-645
    • Levasseur, A.1    Piumi, F.2    Coutinho, P.M.3    Rancurel, C.4    Asther, M.5    Delattre, M.6    Henrissat, B.7    Pontarotti, P.8    Asther, M.9    Record, E.10
  • 86
    • 33745013111 scopus 로고    scopus 로고
    • Oxidative stress and neurodegeneration: Where are we now?
    • Halliwell, B. Oxidative stress and neurodegeneration: Where are we now? J. Neurochem. 2006, 97, 1634-1658.
    • (2006) J. Neurochem , vol.97 , pp. 1634-1658
    • Halliwell, B.1
  • 87
    • 0035379763 scopus 로고    scopus 로고
    • Pathways for extracellular fenton chemistry in the brown rot basidiomycete Gloeophyllum trabeum
    • Jensen, K.A., Jr.; Houtman, C.J.; Ryan, Z.C.; Hammel, K.E. Pathways for extracellular fenton chemistry in the brown rot basidiomycete Gloeophyllum trabeum. Appl. Environ. Microbiol. 2001, 67, 2705-2711.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 2705-2711
    • Jensen, K.A.1    Houtman, C.J.2    Ryan, Z.C.3    Hammel, K.E.4
  • 90
    • 0025870677 scopus 로고
    • Production and degradation of oxalic acid by brown rot fungi
    • Espejo, E.; Agosin, E. Production and degradation of oxalic acid by brown rot fungi. Appl. Environ. Microbiol. 1991, 57, 1980-1986.
    • (1991) Appl. Environ. Microbiol , vol.57 , pp. 1980-1986
    • Espejo, E.1    Agosin, E.2


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