메뉴 건너뛰기




Volumn 4, Issue 2, 2014, Pages 349-365

Global analysis of serine/threonine and tyrosine protein phosphatase catalytic subunit genes in Neurospora crassa reveals interplay between phosphatases and the p38 mitogen-activated protein kinase

Author keywords

Filamentous fungi; Functional genomics; Protein phosphorylation; Serine threonine protein phosphatases; Tyrosine protein phosphatases

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE PHOSPHATASE; TRANSCRIPTION FACTOR;

EID: 84894592859     PISSN: None     EISSN: 21601836     Source Type: Journal    
DOI: 10.1534/g3.113.008813     Document Type: Article
Times cited : (33)

References (163)
  • 1
    • 2942581416 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in the human genome
    • Alonso, A., J. Sasin, N. Bottini, I. Friedberg, A. Osterman et al., 2004 Protein tyrosine phosphatases in the human genome. Cell 117: 699-711.
    • (2004) Cell , vol.117 , pp. 699-711
    • Alonso, A.1    Sasin, J.2    Bottini, N.3    Friedberg, I.4    Osterman, A.5
  • 2
    • 0034785827 scopus 로고    scopus 로고
    • Structural and evolutionary relationships among protein tyrosine phosphatase domains
    • Andersen, J. N., O. H. Mortensen, G. H. Peters, P. G. Drake, L. F. Iversen et al., 2001 Structural and evolutionary relationships among protein tyrosine phosphatase domains. Mol. Cell. Biol. 21: 7117-7136.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7117-7136
    • Andersen, J.N.1    Mortensen, O.H.2    Peters, G.H.3    Drake, P.G.4    Iversen, L.F.5
  • 3
    • 3342900058 scopus 로고    scopus 로고
    • Differential input by Ste5 scaffold and Msg5 phosphatase route a MAPK cascade to multiple outcomes
    • Andersson, J., D. M. Simpson, M. Qi, Y. Wang, and E. A. Elion, 2004 Differential input by Ste5 scaffold and Msg5 phosphatase route a MAPK cascade to multiple outcomes. EMBO J. 23: 2564-2576.
    • (2004) EMBO J. , vol.23 , pp. 2564-2576
    • Andersson, J.1    Simpson, D.M.2    Qi, M.3    Wang, Y.4    Elion, E.A.5
  • 4
    • 48349090987 scopus 로고    scopus 로고
    • Protozoan protein tyrosine phosphatases
    • Andreeva, A. V., and M. A. Kutuzov, 2008 Protozoan protein tyrosine phosphatases. Int. J. Parasitol. 38: 1279-1295.
    • (2008) Int. J. Parasitol. , vol.38 , pp. 1279-1295
    • Andreeva, A.V.1    Kutuzov, M.A.2
  • 5
    • 0031460227 scopus 로고    scopus 로고
    • An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae
    • Archambault, J., R. S. Chambers, M. S. Kobor, Y. Ho, M. Cartier et al., 1997 An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 94: 14300-14305.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14300-14305
    • Archambault, J.1    Chambers, R.S.2    Kobor, M.S.3    Ho, Y.4    Cartier, M.5
  • 6
    • 0032538444 scopus 로고    scopus 로고
    • FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO
    • Archambault, J., G. Pan, G. K. Dahmus, M. Cartier, N. Marshall et al., 1998 FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO. J. Biol. Chem. 273: 27593-27601.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27593-27601
    • Archambault, J.1    Pan, G.2    Dahmus, G.K.3    Cartier, M.4    Marshall, N.5
  • 8
    • 2442616070 scopus 로고    scopus 로고
    • The fluffy gene of Neurospora crassa is necessary and sufficient to induce conidiophore development
    • Bailey-Shrode, L., and D. J. Ebbole, 2004 The fluffy gene of Neurospora crassa is necessary and sufficient to induce conidiophore development. Genetics 166: 1741-1749.
    • (2004) Genetics , vol.166 , pp. 1741-1749
    • Bailey-Shrode, L.1    Ebbole, D.J.2
  • 9
    • 18544379785 scopus 로고    scopus 로고
    • Calcineurin, a calcium/calmodulin-dependent protein phosphatase, is involved in movement, fertility, egg laying, and growth in Caenorhabditis elegans
    • Bandyopadhyay, J., J. Lee, J. I. Lee, J. R. Yu, C. Jee et al., 2002 Calcineurin, a calcium/calmodulin-dependent protein phosphatase, is involved in movement, fertility, egg laying, and growth in Caenorhabditis elegans. Mol. Biol. Cell 13: 3281-3293.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3281-3293
    • Bandyopadhyay, J.1    Lee, J.2    Lee, J.I.3    Yu, J.R.4    Jee, C.5
  • 10
    • 33847233609 scopus 로고    scopus 로고
    • Roles of putative His-to-Asp signaling modules HPT-1 and RRG-2, on viability and sensitivity to osmotic and oxidative stresses in Neurospora crassa
    • Banno, S., R. Noguchi, K. Yamashita, F. Fukumori, M. Kimura et al., 2007 Roles of putative His-to-Asp signaling modules HPT-1 and RRG-2, on viability and sensitivity to osmotic and oxidative stresses in Neurospora crassa. Curr. Genet. 51: 197-208.
    • (2007) Curr. Genet. , vol.51 , pp. 197-208
    • Banno, S.1    Noguchi, R.2    Yamashita, K.3    Fukumori, F.4    Kimura, M.5
  • 11
    • 0036045812 scopus 로고    scopus 로고
    • Kinase-and phosphatase-anchoring proteins: harnessing the dynamic duo
    • Bauman, A. L., and J. D. Scott, 2002 Kinase-and phosphatase-anchoring proteins: harnessing the dynamic duo. Nat. Cell Biol. 4: E203-E206.
    • (2002) Nat. Cell Biol. , vol.4
    • Bauman, A.L.1    Scott, J.D.2
  • 12
    • 1842426345 scopus 로고    scopus 로고
    • Statistics review 9: one-way analysis of variance
    • Bewick, V., L. Cheek, and J. Ball, 2004 Statistics review 9: one-way analysis of variance. Crit. Care 8: 130-136.
    • (2004) Crit. Care , vol.8 , pp. 130-136
    • Bewick, V.1    Cheek, L.2    Ball, J.3
  • 13
    • 0023691731 scopus 로고
    • Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics
    • Bialojan, C., and A. Takai, 1988 Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics. Biochem. J. 256: 283-290.
    • (1988) Biochem. J. , vol.256 , pp. 283-290
    • Bialojan, C.1    Takai, A.2
  • 14
    • 84859437898 scopus 로고    scopus 로고
    • A homologue of the human STRIPAK complex controls sexual development in fungi
    • Bloemendal, S., Y. Bernhards, K. Bartho, A. Dettmann, O. Voigt et al., 2012 A homologue of the human STRIPAK complex controls sexual development in fungi. Mol. Microbiol. 84: 310-323.
    • (2012) Mol. Microbiol. , vol.84 , pp. 310-323
    • Bloemendal, S.1    Bernhards, Y.2    Bartho, K.3    Dettmann, A.4    Voigt, O.5
  • 15
    • 12144287318 scopus 로고    scopus 로고
    • Lessons from the genome sequence of Neurospora crassa: tracing the path from genomic blueprint to multicellular organism
    • Borkovich, K. A., L. A. Alex, O. Yarden, M. Freitag, G. E. Turner et al., 2004 Lessons from the genome sequence of Neurospora crassa: tracing the path from genomic blueprint to multicellular organism. Microbiol. Mol. Biol. Rev. 68: 1-108.
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 1-108
    • Borkovich, K.A.1    Alex, L.A.2    Yarden, O.3    Freitag, M.4    Turner, G.E.5
  • 16
    • 77953077420 scopus 로고    scopus 로고
    • A global protein kinase and phosphatase interaction network in yeast
    • Breitkreutz, A., H. Choi, J. R. Sharom, L. Boucher, V. Neduva et al., 2010 A global protein kinase and phosphatase interaction network in yeast. Science 328: 1043-1046.
    • (2010) Science , vol.328 , pp. 1043-1046
    • Breitkreutz, A.1    Choi, H.2    Sharom, J.R.3    Boucher, L.4    Neduva, V.5
  • 18
    • 77955458622 scopus 로고    scopus 로고
    • Loss of human Greatwall results in G2 arrest and multiple mitotic defects due to deregulation of the cyclin B-Cdc2/PP2A balance
    • Burgess, A., S. Vigneron, E. Brioudes, J. C. Labbe, T. Lorca et al., 2010 Loss of human Greatwall results in G2 arrest and multiple mitotic defects due to deregulation of the cyclin B-Cdc2/PP2A balance. Proc. Natl. Acad. Sci. USA 107: 12564-12569.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 12564-12569
    • Burgess, A.1    Vigneron, S.2    Brioudes, E.3    Labbe, J.C.4    Lorca, T.5
  • 19
    • 1642281603 scopus 로고    scopus 로고
    • A synthetic lethal screen identifies a role for the cortical actin patch/endocytosis complex in the response to nutrient deprivation in Saccharomyces cerevisiae
    • Care, A., K. A. Vousden, K. M. Binley, P. Radcliffe, J. Trevethick et al., 2004 A synthetic lethal screen identifies a role for the cortical actin patch/endocytosis complex in the response to nutrient deprivation in Saccharomyces cerevisiae. Genetics 166: 707-719.
    • (2004) Genetics , vol.166 , pp. 707-719
    • Care, A.1    Vousden, K.A.2    Binley, K.M.3    Radcliffe, P.4    Trevethick, J.5
  • 20
    • 79952435349 scopus 로고    scopus 로고
    • Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases
    • Cargnello, M., and P. P. Roux, 2011 Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases. Microbiol. Mol. Biol. Rev. 75: 50-83.
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 50-83
    • Cargnello, M.1    Roux, P.P.2
  • 21
    • 0032751695 scopus 로고    scopus 로고
    • Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases
    • Cheng, A., K. E. Ross, P. Kaldis, and M. J. Solomon, 1999 Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases. Genes Dev. 13: 2946-2957.
    • (1999) Genes Dev. , vol.13 , pp. 2946-2957
    • Cheng, A.1    Ross, K.E.2    Kaldis, P.3    Solomon, M.J.4
  • 22
    • 33846118688 scopus 로고    scopus 로고
    • Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
    • Cho, U. S., and W. Xu, 2007 Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme. Nature 445: 53-57.
    • (2007) Nature , vol.445 , pp. 53-57
    • Cho, U.S.1    Xu, W.2
  • 23
    • 0034644122 scopus 로고    scopus 로고
    • TOR signaling regulates microtubule structure and function
    • Choi, J. H., N. R. Adames, T. F. Chan, C. Zeng, J. A. Cooper et al., 2000 TOR signaling regulates microtubule structure and function. Curr. Biol. 10: 861-864.
    • (2000) Curr. Biol. , vol.10 , pp. 861-864
    • Choi, J.H.1    Adames, N.R.2    Chan, T.F.3    Zeng, C.4    Cooper, J.A.5
  • 24
    • 33745737918 scopus 로고    scopus 로고
    • Phosphorylation of Hsl1 by Hog1 leads to a G2 arrest essential for cell survival at high osmolarity
    • Clotet, J., X. Escote, M. A. Adrover, G. Yaakov, E. Gari et al., 2006 Phosphorylation of Hsl1 by Hog1 leads to a G2 arrest essential for cell survival at high osmolarity. EMBO J. 25: 2338-2346.
    • (2006) EMBO J. , vol.25 , pp. 2338-2346
    • Clotet, J.1    Escote, X.2    Adrover, M.A.3    Yaakov, G.4    Gari, E.5
  • 25
    • 0024985037 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen, P., 1990 The structure and regulation of protein phosphatases. Adv. Second Messenger Phosphoprotein Res. 24: 230-235.
    • (1990) Adv. Second Messenger Phosphoprotein Res. , vol.24 , pp. 230-235
    • Cohen, P.1
  • 26
    • 0034797512 scopus 로고    scopus 로고
    • The role of protein phosphorylation in human health and disease. The Sir Hans Krebs Medal Lecture
    • Cohen, P., 2001 The role of protein phosphorylation in human health and disease. The Sir Hans Krebs Medal Lecture. Eur. J. Biochem. 268: 5001-5010.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5001-5010
    • Cohen, P.1
  • 27
    • 33745924142 scopus 로고    scopus 로고
    • A high-throughput gene knockout procedure for Neurospora reveals functions for multiple transcription factors
    • Colot, H. V., G. Park, G. E. Turner, C. Ringelberg, C. M. Crew et al., 2006 A high-throughput gene knockout procedure for Neurospora reveals functions for multiple transcription factors. Proc. Natl. Acad. Sci. USA 103: 10352-10357.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10352-10357
    • Colot, H.V.1    Park, G.2    Turner, G.E.3    Ringelberg, C.4    Crew, C.M.5
  • 28
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper, J. A., 1987 Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105: 1473-1478.
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 29
    • 0033525748 scopus 로고    scopus 로고
    • Generic signals and specific outcomes: signaling through Ca2+, calcineurin, and NF-AT
    • Crabtree, G. R., 1999 Generic signals and specific outcomes: signaling through Ca2+, calcineurin, and NF-AT. Cell 96: 611-614.
    • (1999) Cell , vol.96 , pp. 611-614
    • Crabtree, G.R.1
  • 30
    • 0026637095 scopus 로고
    • Regulatory subunit (CNB1 gene product) of yeast Ca2+/calmodulin-dependent phosphoprotein phosphatases is required for adaptation to pheromone
    • Cyert, M. S., and J. Thorner, 1992 Regulatory subunit (CNB1 gene product) of yeast Ca2+/calmodulin-dependent phosphoprotein phosphatases is required for adaptation to pheromone. Mol. Cell. Biol. 12: 3460-3469.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3460-3469
    • Cyert, M.S.1    Thorner, J.2
  • 31
    • 0025913953 scopus 로고
    • Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase
    • Cyert, M. S., R. Kunisawa, D. Kaim, and J. Thorner, 1991 Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase. Proc. Natl. Acad. Sci. USA 88: 7376-7380.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7376-7380
    • Cyert, M.S.1    Kunisawa, R.2    Kaim, D.3    Thorner, J.4
  • 32
    • 77956995235 scopus 로고
    • Genetic and microbiological research techniques for Neurospora crassa
    • Davis, R. H., and F. J. DeSerres, 1970 Genetic and microbiological research techniques for Neurospora crassa. Methods Enzymol. 17: 79-143.
    • (1970) Methods Enzymol. , vol.17 , pp. 79-143
    • Davis, R.H.1    DeSerres, F.J.2
  • 33
    • 0036255812 scopus 로고    scopus 로고
    • Timeline: Neurospora: a model of model microbes
    • Davis, R. H., and D. D. Perkins, 2002 Timeline: Neurospora: a model of model microbes. Nat. Rev. Genet. 3: 397-403.
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 397-403
    • Davis, R.H.1    Perkins, D.D.2
  • 34
    • 0036584978 scopus 로고    scopus 로고
    • Transformation in heterokaryons of Neurospora crassa is nuclear rather than cellular phenomenon
    • Dev, K., and R. Maheshwari, 2002 Transformation in heterokaryons of Neurospora crassa is nuclear rather than cellular phenomenon. Curr. Microbiol. 44: 309-313.
    • (2002) Curr. Microbiol. , vol.44 , pp. 309-313
    • Dev, K.1    Maheshwari, R.2
  • 35
    • 67649442691 scopus 로고    scopus 로고
    • The dual specificity phosphatase Rok1 negatively regulates mating and pathogenicity in Ustilago maydis
    • Di Stasio, M., T. Brefort, A. Mendoza-Mendoza, K. Munch, and R. Kahmann, 2009 The dual specificity phosphatase Rok1 negatively regulates mating and pathogenicity in Ustilago maydis. Mol. Microbiol. 73: 73-88.
    • (2009) Mol. Microbiol. , vol.73 , pp. 73-88
    • Di Stasio, M.1    Brefort, T.2    Mendoza-Mendoza, A.3    Munch, K.4    Kahmann, R.5
  • 36
    • 84876847372 scopus 로고    scopus 로고
    • A serine/threonineprotein phosphatase PP2A catalytic subunit is essential for asexual development and plant infection in Magnaporthe oryzae
    • Du, Y., Y. Shi, J. Yang, X. Chen, M. Xue et al., 2013 A serine/threonineprotein phosphatase PP2A catalytic subunit is essential for asexual development and plant infection in Magnaporthe oryzae. Curr. Genet. 59: 33-41.
    • (2013) Curr. Genet. , vol.59 , pp. 33-41
    • Du, Y.1    Shi, Y.2    Yang, J.3    Chen, X.4    Xue, M.5
  • 37
    • 0025099697 scopus 로고
    • Distinct mechanisms of suppression of murine T cell activation by the related macrolides FK-506 and rapamycin
    • Dumont, F. J., M. J. Staruch, S. L. Koprak, M. R. Melino, and N. H. Sigal, 1990 Distinct mechanisms of suppression of murine T cell activation by the related macrolides FK-506 and rapamycin. J. Immunol. 144: 251-258.
    • (1990) J. Immunol. , vol.144 , pp. 251-258
    • Dumont, F.J.1    Staruch, M.J.2    Koprak, S.L.3    Melino, M.R.4    Sigal, N.H.5
  • 38
    • 0033525870 scopus 로고    scopus 로고
    • Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene
    • Elchebly, M., P. Payette, E. Michaliszyn, W. Cromlish, S. Collins et al., 1999 Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science 283: 1544-1548.
    • (1999) Science , vol.283 , pp. 1544-1548
    • Elchebly, M.1    Payette, P.2    Michaliszyn, E.3    Cromlish, W.4    Collins, S.5
  • 39
    • 34547114489 scopus 로고    scopus 로고
    • Type 2A phosphoprotein phosphatase is required for asexual development and pathogenesis of Sclerotinia sclerotiorum
    • Erental, A., A. Harel, and O. Yarden, 2007 Type 2A phosphoprotein phosphatase is required for asexual development and pathogenesis of Sclerotinia sclerotiorum. Mol. Plant Microbe Interact. 20: 944-954.
    • (2007) Mol. Plant Microbe Interact. , vol.20 , pp. 944-954
    • Erental, A.1    Harel, A.2    Yarden, O.3
  • 40
    • 0030992168 scopus 로고    scopus 로고
    • The PPS1 gene of Saccharomyces cerevisiae codes for a dual specificity protein phosphatase with a role in the DNA synthesis phase of the cell cycle
    • Ernsting, B. R., and J. E. Dixon, 1997 The PPS1 gene of Saccharomyces cerevisiae codes for a dual specificity protein phosphatase with a role in the DNA synthesis phase of the cell cycle. J. Biol. Chem. 272: 9332-9343.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9332-9343
    • Ernsting, B.R.1    Dixon, J.E.2
  • 41
    • 0029088948 scopus 로고
    • Protein phosphatase 2B of Saccharomyces cerevisiae is required for tolerance to manganese, in blocking the entry of ions into the cells
    • Farcasanu, I. C., D. Hirata, E. Tsuchiya, F. Nishiyama, and T. Miyakawa, 1995 Protein phosphatase 2B of Saccharomyces cerevisiae is required for tolerance to manganese, in blocking the entry of ions into the cells. Eur. J. Biochem. 232: 712-717.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 712-717
    • Farcasanu, I.C.1    Hirata, D.2    Tsuchiya, E.3    Nishiyama, F.4    Miyakawa, T.5
  • 42
    • 79954507616 scopus 로고    scopus 로고
    • Diverse protein kinase interactions identified by protein microarrays reveal novel connections between cellular processes
    • Fasolo, J., A. Sboner, M. G. Sun, H. Yu, R. Chen et al., 2011 Diverse protein kinase interactions identified by protein microarrays reveal novel connections between cellular processes. Genes Dev. 25: 767-778.
    • (2011) Genes Dev. , vol.25 , pp. 767-778
    • Fasolo, J.1    Sboner, A.2    Sun, M.G.3    Yu, H.4    Chen, R.5
  • 43
    • 0026343742 scopus 로고
    • The yeast GLC7 gene required for glycogen accumulation encodes a type 1 protein phosphatase
    • Feng, Z. H., S. E. Wilson, Z. Y. Peng, K. K. Schlender, E. M. Reimann et al., 1991 The yeast GLC7 gene required for glycogen accumulation encodes a type 1 protein phosphatase. J. Biol. Chem. 266: 23796-23801.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23796-23801
    • Feng, Z.H.1    Wilson, S.E.2    Peng, Z.Y.3    Schlender, K.K.4    Reimann, E.M.5
  • 44
    • 1642524418 scopus 로고    scopus 로고
    • Reciprocal regulation between Slt2 MAPK and isoforms of Msg5 dual-specificity protein phosphatase modulates the yeast cell integrity pathway
    • Flandez, M., I. C. Cosano, C. Nombela, H. Martin, and M. Molina, 2004 Reciprocal regulation between Slt2 MAPK and isoforms of Msg5 dual-specificity protein phosphatase modulates the yeast cell integrity pathway. J. Biol. Chem. 279: 11027-11034.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11027-11034
    • Flandez, M.1    Cosano, I.C.2    Nombela, C.3    Martin, H.4    Molina, M.5
  • 45
    • 79961038029 scopus 로고    scopus 로고
    • Identification and characterization of genes required for cell-to-cell fusion in Neurospora crassa
    • Fu, C., P. Iyer, A. Herkal, J. Abdullah, A. Stout et al., 2011 Identification and characterization of genes required for cell-to-cell fusion in Neurospora crassa. Eukaryot. Cell 10: 1100-1109.
    • (2011) Eukaryot. Cell , vol.10 , pp. 1100-1109
    • Fu, C.1    Iyer, P.2    Herkal, A.3    Abdullah, J.4    Stout, A.5
  • 46
    • 0037464589 scopus 로고    scopus 로고
    • The genome sequence of the filamentous fungus Neurospora crassa
    • Galagan, J. E., S. E. Calvo, K. A. Borkovich, E. U. Selker, N. D. Read et al., 2003 The genome sequence of the filamentous fungus Neurospora crassa. Nature 422: 859-868.
    • (2003) Nature , vol.422 , pp. 859-868
    • Galagan, J.E.1    Calvo, S.E.2    Borkovich, K.A.3    Selker, E.U.4    Read, N.D.5
  • 47
    • 0345269802 scopus 로고    scopus 로고
    • Ssu72 is a phosphatase essential for transcription termination of snoRNAs and specific mRNAs in yeast
    • Ganem, C., F. Devaux, C. Torchet, C. Jacq, S. Quevillon-Cheruel et al., 2003 Ssu72 is a phosphatase essential for transcription termination of snoRNAs and specific mRNAs in yeast. EMBO J. 22: 1588-1598.
    • (2003) EMBO J. , vol.22 , pp. 1588-1598
    • Ganem, C.1    Devaux, F.2    Torchet, C.3    Jacq, C.4    Quevillon-Cheruel, S.5
  • 48
    • 0028982199 scopus 로고
    • Calcineurin, the Ca2 +/calmodulin-dependent protein phosphatase, is essential in yeast mutants with cell integrity defects and in mutants that lack a functional vacuolar H(+)-ATPase
    • Garrett-Engele, P., B. Moilanen, and M. S. Cyert, 1995 Calcineurin, the Ca2 +/calmodulin-dependent protein phosphatase, is essential in yeast mutants with cell integrity defects and in mutants that lack a functional vacuolar H(+)-ATPase. Mol. Cell. Biol. 15: 4103-4114.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4103-4114
    • Garrett-Engele, P.1    Moilanen, B.2    Cyert, M.S.3
  • 49
    • 0025936510 scopus 로고
    • Cdc25 is a specific tyrosine phosphatase that directly activates P34cdc2
    • Gautier, J., M. J. Solomon, R. N. Booher, J. F. Bazan, and M. W. Kirschner, 1991 Cdc25 is a specific tyrosine phosphatase that directly activates P34cdc2. Cell 67: 197-211.
    • (1991) Cell , vol.67 , pp. 197-211
    • Gautier, J.1    Solomon, M.J.2    Booher, R.N.3    Bazan, J.F.4    Kirschner, M.W.5
  • 50
    • 78049339834 scopus 로고    scopus 로고
    • MAPK signalling in cellular metabolism: stress or wellness?
    • Gehart, H., S. Kumpf, A. Ittner, and R. Ricci, 2010 MAPK signalling in cellular metabolism: stress or wellness? EMBO Rep. 11: 834-840.
    • (2010) EMBO Rep. , vol.11 , pp. 834-840
    • Gehart, H.1    Kumpf, S.2    Ittner, A.3    Ricci, R.4
  • 51
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • Gohla, A., J. Birkenfeld, and G. M. Bokoch, 2005 Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat. Cell Biol. 7: 21-29.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 52
    • 33845959466 scopus 로고    scopus 로고
    • Transcriptional profiling of the protein phosphatase 2C family in yeast provides insights into the unique functional roles of Ptc1
    • Gonzalez, A., A. Ruiz, R. Serrano, J. Arino, and A. Casamayor, 2006 Transcriptional profiling of the protein phosphatase 2C family in yeast provides insights into the unique functional roles of Ptc1. J. Biol. Chem. 281: 35057-35069.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35057-35069
    • Gonzalez, A.1    Ruiz, A.2    Serrano, R.3    Arino, J.4    Casamayor, A.5
  • 53
    • 9044239223 scopus 로고
    • A series of histidineless mutants of Neurospora crassa
    • Haas, F., M. B. Mitchell, B. N. Ames, and H. K. Mitchell, 1952 A series of histidineless mutants of Neurospora crassa. Genetics 37: 217-226.
    • (1952) Genetics , vol.37 , pp. 217-226
    • Haas, F.1    Mitchell, M.B.2    Ames, B.N.3    Mitchell, H.K.4
  • 54
    • 0037077207 scopus 로고    scopus 로고
    • Regulation of the Saccharomyces cerevisiae Slt2 kinase pathway by the stress-inducible Sdp1 dual specificity phosphatase
    • Hahn, J. S., and D. J. Thiele, 2002 Regulation of the Saccharomyces cerevisiae Slt2 kinase pathway by the stress-inducible Sdp1 dual specificity phosphatase. J. Biol. Chem. 277: 21278-21284.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21278-21284
    • Hahn, J.S.1    Thiele, D.J.2
  • 55
    • 0027450048 scopus 로고
    • Reactive oxygen species associated with cell differentiation in Neurospora crassa
    • Hansberg, W., H. de Groot, and H. Sies, 1993 Reactive oxygen species associated with cell differentiation in Neurospora crassa. Free Radic. Biol. Med. 14: 287-293.
    • (1993) Free Radic. Biol. Med. , vol.14 , pp. 287-293
    • Hansberg, W.1    de Groot, H.2    Sies, H.3
  • 56
    • 0033954554 scopus 로고    scopus 로고
    • Effects of serine/threonine protein phosphatases on ion channels in excitable membranes
    • Herzig, S., and J. Neumann, 2000 Effects of serine/threonine protein phosphatases on ion channels in excitable membranes. Physiol. Rev. 80: 173-210.
    • (2000) Physiol. Rev. , vol.80 , pp. 173-210
    • Herzig, S.1    Neumann, J.2
  • 57
    • 42349100173 scopus 로고    scopus 로고
    • The chemical genomic portrait of yeast: uncovering a phenotype for all genes
    • Hillenmeyer, M. E., E. Fung, J. Wildenhain, S. E. Pierce, S. Hoon et al., 2008 The chemical genomic portrait of yeast: uncovering a phenotype for all genes. Science 320: 362-365.
    • (2008) Science , vol.320 , pp. 362-365
    • Hillenmeyer, M.E.1    Fung, E.2    Wildenhain, J.3    Pierce, S.E.4    Hoon, S.5
  • 58
    • 84864326726 scopus 로고    scopus 로고
    • DUSPs, to MAP kinases and beyond
    • Huang, C. Y., and T. H. Tan, 2012 DUSPs, to MAP kinases and beyond. Cell Biosci. 2: 24.
    • (2012) Cell Biosci. , vol.2 , pp. 24
    • Huang, C.Y.1    Tan, T.H.2
  • 59
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling
    • Hunter, T., 1995 Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80: 225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 60
    • 84867185148 scopus 로고    scopus 로고
    • Diversification of a protein kinase cascade: IME-2 is involved in nonself recognition and programmed cell death in Neurospora crassa
    • Hutchison, E. A., J. A. Bueche, and N. L. Glass, 2012 Diversification of a protein kinase cascade: IME-2 is involved in nonself recognition and programmed cell death in Neurospora crassa. Genetics 192: 467-482.
    • (2012) Genetics , vol.192 , pp. 467-482
    • Hutchison, E.A.1    Bueche, J.A.2    Glass, N.L.3
  • 61
    • 78751607188 scopus 로고    scopus 로고
    • Meiotic regulators Ndt80 and ime2 have different roles in Saccharomyces and Neurospora
    • Hutchison, E. A., and N. L. Glass, 2010 Meiotic regulators Ndt80 and ime2 have different roles in Saccharomyces and Neurospora. Genetics 185: 1271-1282.
    • (2010) Genetics , vol.185 , pp. 1271-1282
    • Hutchison, E.A.1    Glass, N.L.2
  • 62
    • 0020675427 scopus 로고
    • Photoinduction of protoperithecia in Neurospora crassa by blue light
    • Innocenti, F. D., U. Pohl, and V. E. Russo, 1983 Photoinduction of protoperithecia in Neurospora crassa by blue light. Photochem. Photobiol. 37: 49-51.
    • (1983) Photochem. Photobiol. , vol.37 , pp. 49-51
    • Innocenti, F.D.1    Pohl, U.2    Russo, V.E.3
  • 63
    • 65249093722 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase-mitogen-activated protein kinase pathway phosphorylates and targets Cdc25A for SCF beta-TrCP-dependent degradation for cell cycle arrest
    • Isoda, M., Y. Kanemori, N. Nakajo, S. Uchida, K. Yamashita et al., 2009 The extracellular signal-regulated kinase-mitogen-activated protein kinase pathway phosphorylates and targets Cdc25A for SCF beta-TrCP-dependent degradation for cell cycle arrest. Mol. Biol. Cell 20: 2186-2195.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2186-2195
    • Isoda, M.1    Kanemori, Y.2    Nakajo, N.3    Uchida, S.4    Yamashita, K.5
  • 64
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens, V., and J. Goris, 2001 Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem. J. 353: 417-439.
    • (2001) Biochem. J. , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 65
    • 34248210189 scopus 로고    scopus 로고
    • Targeting dual-specificity phosphatases: manipulating MAP kinase signalling and immune responses
    • Jeffrey, K. L., M. Camps, C. Rommel, and C. R. Mackay, 2007 Targeting dual-specificity phosphatases: manipulating MAP kinase signalling and immune responses. Nat. Rev. Drug Discov. 6: 391-403.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 391-403
    • Jeffrey, K.L.1    Camps, M.2    Rommel, C.3    Mackay, C.R.4
  • 66
    • 79952196925 scopus 로고    scopus 로고
    • Analysis of mitogen-activated protein kinase phosphorylation in response to stimulation of histidine kinase signaling pathways in Neurospora
    • Jones, C. A., and K. A. Borkovich, 2010 Analysis of mitogen-activated protein kinase phosphorylation in response to stimulation of histidine kinase signaling pathways in Neurospora. Methods Enzymol. 471: 319-334.
    • (2010) Methods Enzymol. , vol.471 , pp. 319-334
    • Jones, C.A.1    Borkovich, K.A.2
  • 67
    • 34250326301 scopus 로고    scopus 로고
    • The response regulator RRG-1 functions upstream of a mitogen-activated protein kinase pathway impacting asexual development, female fertility, osmotic stress, and fungicide resistance in Neurospora crassa
    • Jones, C. A., S. E. Greer-Phillips, and K. A. Borkovich, 2007 The response regulator RRG-1 functions upstream of a mitogen-activated protein kinase pathway impacting asexual development, female fertility, osmotic stress, and fungicide resistance in Neurospora crassa. Mol. Biol. Cell 18: 2123-2136.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2123-2136
    • Jones, C.A.1    Greer-Phillips, S.E.2    Borkovich, K.A.3
  • 68
    • 70350153322 scopus 로고    scopus 로고
    • Alternative splicing of PTC7 in Saccharomyces cerevisiae determines protein localization
    • Juneau, K., C. Nislow, and R. W. Davis, 2009 Alternative splicing of PTC7 in Saccharomyces cerevisiae determines protein localization. Genetics 183: 185-194.
    • (2009) Genetics , vol.183 , pp. 185-194
    • Juneau, K.1    Nislow, C.2    Davis, R.W.3
  • 69
    • 0029064172 scopus 로고
    • Interaction of FKBP12-FK506 with calcineurin A at the B subunit-binding domain
    • Kawamura, A., and M. S. Su, 1995 Interaction of FKBP12-FK506 with calcineurin A at the B subunit-binding domain. J. Biol. Chem. 270: 15463-15466.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15463-15466
    • Kawamura, A.1    Su, M.S.2
  • 70
    • 79952247189 scopus 로고    scopus 로고
    • Gel-based mass spectrometric and computational approaches to the mitochondrial proteome of Neurospora
    • Keeping, A., D. Deabreu, M. Dibernardo, and R. A. Collins, 2011 Gel-based mass spectrometric and computational approaches to the mitochondrial proteome of Neurospora. Fungal Genet. Biol. 48: 526-536.
    • (2011) Fungal Genet. Biol. , vol.48 , pp. 526-536
    • Keeping, A.1    Deabreu, D.2    Dibernardo, M.3    Collins, R.A.4
  • 71
    • 38949205017 scopus 로고    scopus 로고
    • Evolutionary radiation pattern of novel protein phosphatases revealed by analysis of protein data from the completely sequenced genomes of humans, green algae, and higher plants
    • Kerk, D., G. Templeton, and G. B. Moorhead, 2008 Evolutionary radiation pattern of novel protein phosphatases revealed by analysis of protein data from the completely sequenced genomes of humans, green algae, and higher plants. Plant Physiol. 146: 351-367.
    • (2008) Plant Physiol. , vol.146 , pp. 351-367
    • Kerk, D.1    Templeton, G.2    Moorhead, G.B.3
  • 72
    • 84872819657 scopus 로고    scopus 로고
    • Targeting the oxidative stress response system of fungi with redox-potent chemosensitizing agents
    • Kim, J. H., K. L. Chan, N. C. Faria, L. Martins Mde, and B. C. Campbell, 2012 Targeting the oxidative stress response system of fungi with redox-potent chemosensitizing agents. Front. Microbiol. 3: 88.
    • (2012) Front. Microbiol. , vol.3 , pp. 88
    • Kim, J.H.1    Chan, K.L.2    Faria, N.C.3    Martins Mde, L.4    Campbell, B.C.5
  • 74
    • 0032577483 scopus 로고    scopus 로고
    • Regulation of the calmodulinstimulated protein phosphatase, calcineurin
    • Klee, C. B., H. Ren, and X. Wang, 1998 Regulation of the calmodulinstimulated protein phosphatase, calcineurin. J. Biol. Chem. 273: 13367-13370.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13367-13370
    • Klee, C.B.1    Ren, H.2    Wang, X.3
  • 75
    • 0033165865 scopus 로고    scopus 로고
    • An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S
    • Kobor, M. S., J. Archambault, W. Lester, F. C. Holstege, O. Gileadi et al., 1999 An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae. Mol. Cell 4: 55-62.
    • (1999) cerevisiae. Mol. Cell , vol.4 , pp. 55-62
    • Kobor, M.S.1    Archambault, J.2    Lester, W.3    Holstege, F.C.4    Gileadi, O.5
  • 76
    • 77950388509 scopus 로고    scopus 로고
    • Comparative analysis of fungal protein kinases and associated domains
    • Kosti, I., Y. Mandel-Gutfreund, F. Glaser, and B. A. Horwitz, 2010 Comparative analysis of fungal protein kinases and associated domains. BMC Genomics 11: 133.
    • (2010) BMC Genomics , vol.11 , pp. 133
    • Kosti, I.1    Mandel-Gutfreund, Y.2    Glaser, F.3    Horwitz, B.A.4
  • 77
    • 0032051455 scopus 로고    scopus 로고
    • Calcineurin subunit B is required for normal vegetative growth in Neurospora crassa
    • Kothe, G. O., and S. J. Free, 1998a Calcineurin subunit B is required for normal vegetative growth in Neurospora crassa. Fungal Genet. Biol. 23: 248-258.
    • (1998) Fungal Genet. Biol. , vol.23 , pp. 248-258
    • Kothe, G.O.1    Free, S.J.2
  • 78
    • 0031805254 scopus 로고    scopus 로고
    • The isolation and characterization of nrc-1 and nrc-2, two genes encoding protein kinases that control growth and development in Neurospora crassa
    • Kothe, G. O., and S. J. Free, 1998b The isolation and characterization of nrc-1 and nrc-2, two genes encoding protein kinases that control growth and development in Neurospora crassa. Genetics 149: 117-130.
    • (1998) Genetics , vol.149 , pp. 117-130
    • Kothe, G.O.1    Free, S.J.2
  • 79
    • 13844306886 scopus 로고    scopus 로고
    • The heterotrimeric G-protein subunits GNG-1 and GNB-1 form a Gbetagamma dimer required for normal female fertility, asexual development, and galpha protein levels in Neurospora crassa
    • Krystofova, S., and K. A. Borkovich, 2005 The heterotrimeric G-protein subunits GNG-1 and GNB-1 form a Gbetagamma dimer required for normal female fertility, asexual development, and galpha protein levels in Neurospora crassa. Eukaryot. Cell 4: 365-378.
    • (2005) Eukaryot. Cell , vol.4 , pp. 365-378
    • Krystofova, S.1    Borkovich, K.A.2
  • 81
    • 84856766590 scopus 로고    scopus 로고
    • The Neurospora crassa OS MAPK pathway-activated transcription factor ASL-1 contributes to circadian rhythms in pathway responsive clock-controlled genes
    • Lamb, T. M., K. E. Finch, and D. Bell-Pedersen, 2012 The Neurospora crassa OS MAPK pathway-activated transcription factor ASL-1 contributes to circadian rhythms in pathway responsive clock-controlled genes. Fungal Genet. Biol. 49: 180-188.
    • (2012) Fungal Genet. Biol. , vol.49 , pp. 180-188
    • Lamb, T.M.1    Finch, K.E.2    Bell-Pedersen, D.3
  • 82
    • 80455158354 scopus 로고    scopus 로고
    • Direct transcriptional control of a p38 MAPK pathway by the circadian clock in Neurospora crassa
    • Lamb, T. M., C. S. Goldsmith, L. Bennett, K. E. Finch, and D. Bell-Pedersen, 2011 Direct transcriptional control of a p38 MAPK pathway by the circadian clock in Neurospora crassa. PLoS ONE 6: e27149.
    • (2011) PLoS ONE , vol.6
    • Lamb, T.M.1    Goldsmith, C.S.2    Bennett, L.3    Finch, K.E.4    Bell-Pedersen, D.5
  • 83
    • 62449226213 scopus 로고    scopus 로고
    • A high-density single nucleotide polymorphism map for Neurospora crassa
    • Lambreghts, R., M. Shi, W. J. Belden, D. Decaprio, D. Park et al., 2009 A high-density single nucleotide polymorphism map for Neurospora crassa. Genetics 181: 767-781.
    • (2009) Genetics , vol.181 , pp. 767-781
    • Lambreghts, R.1    Shi, M.2    Belden, W.J.3    Decaprio, D.4    Park, D.5
  • 84
    • 0344643062 scopus 로고    scopus 로고
    • PP2C phosphatases Ptc2 and Ptc3 are required for DNA checkpoint inactivation after a double-strand break
    • Leroy, C., S. E. Lee, M. B. Vaze, F. Ochsenbein, R. Guerois et al., 2003 PP2C phosphatases Ptc2 and Ptc3 are required for DNA checkpoint inactivation after a double-strand break. Mol. Cell 11: 827-835.
    • (2003) Mol. Cell , vol.11 , pp. 827-835
    • Leroy, C.1    Lee, S.E.2    Vaze, M.B.3    Ochsenbein, F.4    Guerois, R.5
  • 85
    • 23344437797 scopus 로고    scopus 로고
    • A mitogenactivated protein kinase pathway essential for mating and contributing to vegetative growth in Neurospora crassa
    • Li, D., P. Bobrowicz, H. H. Wilkinson, and D. J. Ebbole, 2005 A mitogenactivated protein kinase pathway essential for mating and contributing to vegetative growth in Neurospora crassa. Genetics 170: 1091-1104.
    • (2005) Genetics , vol.170 , pp. 1091-1104
    • Li, D.1    Bobrowicz, P.2    Wilkinson, H.H.3    Ebbole, D.J.4
  • 86
    • 49149087049 scopus 로고    scopus 로고
    • CDK1 promotes cell proliferation and survival via phosphorylation and inhibition of FOXO1 transcription factor
    • Liu, P., T. P. Kao, and H. Huang, 2008 CDK1 promotes cell proliferation and survival via phosphorylation and inhibition of FOXO1 transcription factor. Oncogene 27: 4733-4744.
    • (2008) Oncogene , vol.27 , pp. 4733-4744
    • Liu, P.1    Kao, T.P.2    Huang, H.3
  • 87
    • 78650173771 scopus 로고    scopus 로고
    • Menadione triggers cell death through ROS-dependent mechanisms involving PARP activation without requiring apoptosis
    • Loor, G., J. Kondapalli, J. M. Schriewer, N. S. Chandel, T. L. Vanden Hoek et al., 2010 Menadione triggers cell death through ROS-dependent mechanisms involving PARP activation without requiring apoptosis. Free Radic. Biol. Med. 49: 1925-1936.
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 1925-1936
    • Loor, G.1    Kondapalli, J.2    Schriewer, J.M.3    Chandel, N.S.4    Vanden Hoek, T.L.5
  • 88
    • 77954355722 scopus 로고    scopus 로고
    • Constant regulation of both the MPF amplification loop and the Greatwall-PP2A pathway is required for metaphase II arrest and correct entry into the first embryonic cell cycle
    • Lorca, T., C. Bernis, S. Vigneron, A. Burgess, E. Brioudes et al., 2010 Constant regulation of both the MPF amplification loop and the Greatwall-PP2A pathway is required for metaphase II arrest and correct entry into the first embryonic cell cycle. J. Cell Sci. 123: 2281-2291.
    • (2010) J. Cell Sci. , vol.123 , pp. 2281-2291
    • Lorca, T.1    Bernis, C.2    Vigneron, S.3    Burgess, A.4    Brioudes, E.5
  • 89
    • 38149011286 scopus 로고    scopus 로고
    • Functional diversity of mammalian type 2C protein phosphatase isoforms: new tales from an old family
    • Lu, G., and Y. Wang, 2008 Functional diversity of mammalian type 2C protein phosphatase isoforms: new tales from an old family. Clin. Exp. Pharmacol. Physiol. 35: 107-112.
    • (2008) Clin. Exp. Pharmacol. Physiol. , vol.35 , pp. 107-112
    • Lu, G.1    Wang, Y.2
  • 90
    • 4344560876 scopus 로고    scopus 로고
    • The p53-induced oncogenic phosphatase PPM1D interacts with uracil DNA glycosylase and suppresses base excision repair
    • Lu, X., D. Bocangel, B. Nannenga, H. Yamaguchi, E. Appella et al., 2004 The p53-induced oncogenic phosphatase PPM1D interacts with uracil DNA glycosylase and suppresses base excision repair. Mol. Cell 15: 621-634.
    • (2004) Mol. Cell , vol.15 , pp. 621-634
    • Lu, X.1    Bocangel, D.2    Nannenga, B.3    Yamaguchi, H.4    Appella, E.5
  • 91
    • 66249133969 scopus 로고    scopus 로고
    • Regulators of PP2C phosphatase activity function as abscisic acid sensors
    • Ma, Y., I. Szostkiewicz, A. Korte, D. Moes, Y. Yang et al., 2009 Regulators of PP2C phosphatase activity function as abscisic acid sensors. Science 324: 1064-1068.
    • (2009) Science , vol.324 , pp. 1064-1068
    • Ma, Y.1    Szostkiewicz, I.2    Korte, A.3    Moes, D.4    Yang, Y.5
  • 92
    • 61349186933 scopus 로고    scopus 로고
    • Different modulation of the outputs of yeast MAPK-mediated pathways by distinct stimuli and isoforms of the dual-specificity phosphatase Msg5
    • Marin, M. J., M. Flandez, C. Bermejo, J. Arroyo, H. Martin et al., 2009 Different modulation of the outputs of yeast MAPK-mediated pathways by distinct stimuli and isoforms of the dual-specificity phosphatase Msg5. Mol. Genet. Genomics 281: 345-359.
    • (2009) Mol. Genet. Genomics , vol.281 , pp. 345-359
    • Marin, M.J.1    Flandez, M.2    Bermejo, C.3    Arroyo, J.4    Martin, H.5
  • 93
    • 0034117149 scopus 로고    scopus 로고
    • Involvement of the PP2C-like phosphatase Ptc2p in the DNA checkpoint pathways of Saccharomyces cerevisiae
    • Marsolier, M. C., P. Roussel, C. Leroy, and C. Mann, 2000 Involvement of the PP2C-like phosphatase Ptc2p in the DNA checkpoint pathways of Saccharomyces cerevisiae. Genetics 154: 1523-1532.
    • (2000) Genetics , vol.154 , pp. 1523-1532
    • Marsolier, M.C.1    Roussel, P.2    Leroy, C.3    Mann, C.4
  • 94
    • 80055111905 scopus 로고    scopus 로고
    • Rediscovery by whole genome sequencing: classical mutations and genome polymorphisms in Neurospora crassa
    • McCluskey, K, A E Wiest, I V Grigoriev, A Lipzen, J Martin et al. 2011. Rediscovery by whole genome sequencing: classical mutations and genome polymorphisms in Neurospora crassa. G3 (Bethesda) 1: 303-316.
    • (2011) G3 (Bethesda) , vol.1 , pp. 303-316
    • McCluskey, K.1    Wiest, A.E.2    Grigoriev, I.V.3    Lipzen, A.4    Martin, J.5
  • 95
    • 66849115406 scopus 로고    scopus 로고
    • Targeting protein serine/ threonine phosphatases for drug development
    • McConnell, J. L., and B. E. Wadzinski, 2009 Targeting protein serine/ threonine phosphatases for drug development. Mol. Pharmacol. 75: 1249-1261.
    • (2009) Mol. Pharmacol. , vol.75 , pp. 1249-1261
    • McConnell, J.L.1    Wadzinski, B.E.2
  • 97
    • 58249089943 scopus 로고    scopus 로고
    • Evolution of protein phosphatases in plants and animals
    • Moorhead, G. B., V. De Wever, G. Templeton, and D. Kerk, 2009 Evolution of protein phosphatases in plants and animals. Biochem. J. 417: 401-409.
    • (2009) Biochem. J. , vol.417 , pp. 401-409
    • Moorhead, G.B.1    De Wever, V.2    Templeton, G.3    Kerk, D.4
  • 98
    • 19444385669 scopus 로고    scopus 로고
    • An Os-1 family histidine kinase from a filamentous fungus confers fungicide-sensitivity to yeast
    • Motoyama, T., T. Ohira, K. Kadokura, A. Ichiishi, M. Fujimura et al., 2005 An Os-1 family histidine kinase from a filamentous fungus confers fungicide-sensitivity to yeast. Curr. Genet. 47: 298-306.
    • (2005) Curr. Genet. , vol.47 , pp. 298-306
    • Motoyama, T.1    Ohira, T.2    Kadokura, K.3    Ichiishi, A.4    Fujimura, M.5
  • 99
    • 33845609865 scopus 로고    scopus 로고
    • Mutual antagonism of target of rapamycin and calcineurin signaling
    • Mulet, J. M., D. E. Martin, R. Loewith, and M. N. Hall, 2006 Mutual antagonism of target of rapamycin and calcineurin signaling. J. Biol. Chem. 281: 33000-33007.
    • (2006) J. Biol. Chem. , vol.281 , pp. 33000-33007
    • Mulet, J.M.1    Martin, D.E.2    Loewith, R.3    Hall, M.N.4
  • 101
    • 0035805596 scopus 로고    scopus 로고
    • Akt, MAPK (Erk1/2), and p38 act in concert to promote apoptosis in response to ErbB receptor family inhibition
    • Nelson, J. M., and D. W. Fry, 2001 Akt, MAPK (Erk1/2), and p38 act in concert to promote apoptosis in response to ErbB receptor family inhibition. J. Biol. Chem. 276: 14842-14847.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14842-14847
    • Nelson, J.M.1    Fry, D.W.2
  • 102
    • 0035043007 scopus 로고    scopus 로고
    • Characterization of mutations in the two-component histidine kinase gene that confer fludioxonil resistance and osmotic sensitivity in the os-1 mutants of Neurospora crassa
    • Ochiai, N., M. Fujimura, T. Motoyama, A. Ichiishi, R. Usami et al., 2001 Characterization of mutations in the two-component histidine kinase gene that confer fludioxonil resistance and osmotic sensitivity in the os-1 mutants of Neurospora crassa. Pest Manag. Sci. 57: 437-442.
    • (2001) Pest Manag. Sci. , vol.57 , pp. 437-442
    • Ochiai, N.1    Fujimura, M.2    Motoyama, T.3    Ichiishi, A.4    Usami, R.5
  • 103
    • 0037515747 scopus 로고    scopus 로고
    • Cell cycle regulation and p53 activation by protein phosphatase 2C alpha
    • Ofek, P., D. Ben-Meir, Z. Kariv-Inbal, M. Oren, and S. Lavi, 2003 Cell cycle regulation and p53 activation by protein phosphatase 2C alpha. J. Biol. Chem. 278: 14299-14305.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14299-14305
    • Ofek, P.1    Ben-Meir, D.2    Kariv-Inbal, Z.3    Oren, M.4    Lavi, S.5
  • 104
    • 0029095003 scopus 로고
    • Cloning and characterization of a Saccharomyces cerevisiae gene encoding the low molecular weight protein-tyrosine phosphatase
    • Ostanin, K., C. Pokalsky, S. Wang, and R. L. Van Etten, 1995 Cloning and characterization of a Saccharomyces cerevisiae gene encoding the low molecular weight protein-tyrosine phosphatase. J. Biol. Chem. 270: 18491-18499.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18491-18499
    • Ostanin, K.1    Pokalsky, C.2    Wang, S.3    Van Etten, R.L.4
  • 105
    • 0021844163 scopus 로고
    • Gene disruption by transformation in Neurospora crassa
    • Paietta, J. V., and G. A. Marzluf, 1985 Gene disruption by transformation in Neurospora crassa. Mol. Cell. Biol. 5: 1554-1559.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1554-1559
    • Paietta, J.V.1    Marzluf, G.A.2
  • 106
    • 33847394655 scopus 로고    scopus 로고
    • MAPK-mediated bimodal gene expression and adaptive gradient sensing in yeast
    • Paliwal, S., P. A. Iglesias, K. Campbell, Z. Hilioti, A. Groisman et al., 2007 MAPK-mediated bimodal gene expression and adaptive gradient sensing in yeast. Nature 446: 46-51.
    • (2007) Nature , vol.446 , pp. 46-51
    • Paliwal, S.1    Iglesias, P.A.2    Campbell, K.3    Hilioti, Z.4    Groisman, A.5
  • 107
    • 16544382262 scopus 로고    scopus 로고
    • Role of a mitogenactivated protein kinase pathway during conidial germination and hyphal fusion in Neurospora crassa
    • Pandey, A., M. G. Roca, N. D. Read, and N. L. Glass, 2004 Role of a mitogenactivated protein kinase pathway during conidial germination and hyphal fusion in Neurospora crassa. Eukaryot. Cell 3: 348-358.
    • (2004) Eukaryot. Cell , vol.3 , pp. 348-358
    • Pandey, A.1    Roca, M.G.2    Read, N.D.3    Glass, N.L.4
  • 108
    • 34247881790 scopus 로고    scopus 로고
    • Nonreceptor protein-tyrosine phosphatases in immune cell signaling
    • Pao, L. I., K. Badour, K. A. Siminovitch, and B. G. Neel, 2007 Nonreceptor protein-tyrosine phosphatases in immune cell signaling. Annu. Rev. Immunol. 25: 473-523.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 473-523
    • Pao, L.I.1    Badour, K.2    Siminovitch, K.A.3    Neel, B.G.4
  • 109
    • 84860776777 scopus 로고    scopus 로고
    • The functions of grainy head-like proteins in animals and fungi and the evolution of apical extracellular barriers
    • Pare, A., M. Kim, M. T. Juarez, S. Brody, and W. McGinnis, 2012 The functions of grainy head-like proteins in animals and fungi and the evolution of apical extracellular barriers. PLoS ONE 7: e36254.
    • (2012) PLoS ONE , vol.7
    • Pare, A.1    Kim, M.2    Juarez, M.T.3    Brody, S.4    McGinnis, W.5
  • 110
    • 80053120609 scopus 로고    scopus 로고
    • High-throughput production of gene replacement mutants in Neurospora crassa
    • Park, G., H. V. Colot, P. D. Collopy, S. Krystofova, C. Crew et al., 2011a High-throughput production of gene replacement mutants in Neurospora crassa. Methods Mol. Biol. 722: 179-189.
    • (2011) Methods Mol. Biol. , vol.722 , pp. 179-189
    • Park, G.1    Colot, H.V.2    Collopy, P.D.3    Krystofova, S.4    Crew, C.5
  • 111
    • 80055109852 scopus 로고    scopus 로고
    • Global analysis of serine-threonine protein kinase genes in Neurospora crassa
    • Park, G., J. A. Servin, G. E. Turner, L. Altamirano, H. V. Colot et al., 2011b Global analysis of serine-threonine protein kinase genes in Neurospora crassa. Eukaryot. Cell 10: 1553-1564.
    • (2011) Eukaryot. Cell , vol.10 , pp. 1553-1564
    • Park, G.1    Servin, J.A.2    Turner, G.E.3    Altamirano, L.4    Colot, H.V.5
  • 112
    • 0029030776 scopus 로고
    • Biochemical characterization of recombinant yeast PPZ1, a protein phosphatase involved in salt tolerance
    • Posas, F., M. Bollen, W. Stalmans, and J. Arino, 1995 Biochemical characterization of recombinant yeast PPZ1, a protein phosphatase involved in salt tolerance. FEBS Lett. 368: 39-44.
    • (1995) FEBS Lett. , vol.368 , pp. 39-44
    • Posas, F.1    Bollen, M.2    Stalmans, W.3    Arino, J.4
  • 113
    • 0027463465 scopus 로고
    • The gene PPG encodes a novel yeast protein phosphatase involved in glycogen accumulation
    • Posas, F., J. Clotet, M. T. Muns, J. Corominas, A. Casamayor et al., 1993 The gene PPG encodes a novel yeast protein phosphatase involved in glycogen accumulation. J. Biol. Chem. 268: 1349-1354.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1349-1354
    • Posas, F.1    Clotet, J.2    Muns, M.T.3    Corominas, J.4    Casamayor, A.5
  • 114
    • 0030667518 scopus 로고    scopus 로고
    • Impairment of calcineurin function in Neurospora crassa reveals its essential role in hyphal growth, morphology and maintenance of the apical Ca2+ gradient
    • Prokisch, H., O. Yarden, M. Dieminger, M. Tropschug, and I. B. Barthelmess, 1997 Impairment of calcineurin function in Neurospora crassa reveals its essential role in hyphal growth, morphology and maintenance of the apical Ca2+ gradient. Mol. Gen. Genet. 256: 104-114.
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 104-114
    • Prokisch, H.1    Yarden, O.2    Dieminger, M.3    Tropschug, M.4    Barthelmess, I.B.5
  • 115
    • 0026455099 scopus 로고
    • Cytology of recessive sexual-phase mutants from wild strains of Neurospora crassa
    • Raju, N. B., and J. F. Leslie, 1992 Cytology of recessive sexual-phase mutants from wild strains of Neurospora crassa. Genome 35: 815-826.
    • (1992) Genome , vol.35 , pp. 815-826
    • Raju, N.B.1    Leslie, J.F.2
  • 116
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: form and function
    • Rusnak, F., and P. Mertz, 2000 Calcineurin: form and function. Physiol. Rev. 80: 1483-1521.
    • (2000) Physiol. Rev. , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 117
    • 0024559540 scopus 로고
    • Conservation of mitotic controls in fission and budding yeasts
    • Russell, P., S. Moreno, and S. I. Reed, 1989 Conservation of mitotic controls in fission and budding yeasts. Cell 57: 295-303.
    • (1989) Cell , vol.57 , pp. 295-303
    • Russell, P.1    Moreno, S.2    Reed, S.I.3
  • 118
    • 0036092193 scopus 로고    scopus 로고
    • A series of double disruptants for protein phosphatase genes in Saccharomyces cerevisiae and their phenotypic analysis
    • Sakumoto, N., I. Matsuoka, Y. Mukai, N. Ogawa, Y. Kaneko et al., 2002 A series of double disruptants for protein phosphatase genes in Saccharomyces cerevisiae and their phenotypic analysis. Yeast 19: 587-599.
    • (2002) Yeast , vol.19 , pp. 587-599
    • Sakumoto, N.1    Matsuoka, I.2    Mukai, Y.3    Ogawa, N.4    Kaneko, Y.5
  • 119
    • 83455225642 scopus 로고    scopus 로고
    • A global circadian repressor controls antiphasic expression of metabolic genes in Neurospora
    • Sancar, G., C. Sancar, B. Brugger, N. Ha, T. Sachsenheimer et al., 2011 A global circadian repressor controls antiphasic expression of metabolic genes in Neurospora. Mol. Cell 44: 687-697.
    • (2011) Mol. Cell , vol.44 , pp. 687-697
    • Sancar, G.1    Sancar, C.2    Brugger, B.3    Ha, N.4    Sachsenheimer, T.5
  • 120
    • 0035952318 scopus 로고    scopus 로고
    • Protein phosphatase 1 catalyses the direct hydrolytic cleavage of phosphate monoester in a ternary complex mechanism
    • Sanvoisin, J., and D. Gani, 2001 Protein phosphatase 1 catalyses the direct hydrolytic cleavage of phosphate monoester in a ternary complex mechanism. Bioorg. Med. Chem. Lett. 11: 471-474.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 471-474
    • Sanvoisin, J.1    Gani, D.2
  • 121
    • 22744455874 scopus 로고    scopus 로고
    • Transcriptional feedback of Neurospora circadian clock gene by phosphorylation-dependent inactivation of its transcription factor
    • Schafmeier, T., A. Haase, K. Kaldi, J. Scholz,M. Fuchs et al., 2005 Transcriptional feedback of Neurospora circadian clock gene by phosphorylation-dependent inactivation of its transcription factor. Cell 122: 235-246.
    • (2005) Cell , vol.122 , pp. 235-246
    • Schafmeier, T.1    Haase, A.2    Kaldi, K.3    Scholz, M.4    Fuchs, J.5
  • 122
    • 62549136628 scopus 로고    scopus 로고
    • Rhythmic conidiation in constant light in vivid mutants of Neurospora crassa
    • Schneider, K., S. Perrino, K. Oelhafen, S. Li, A. Zatsepin et al., 2009 Rhythmic conidiation in constant light in vivid mutants of Neurospora crassa. Genetics 181: 917-931.
    • (2009) Genetics , vol.181 , pp. 917-931
    • Schneider, K.1    Perrino, S.2    Oelhafen, K.3    Li, S.4    Zatsepin, A.5
  • 123
    • 84872817040 scopus 로고    scopus 로고
    • Human HAD phosphatases: structure, mechanism, and roles in health and disease
    • Seifried, A., J. Schultz, and A. Gohla, 2013 Human HAD phosphatases: structure, mechanism, and roles in health and disease. FEBS J. 280: 549-571.
    • (2013) FEBS J. , vol.280 , pp. 549-571
    • Seifried, A.1    Schultz, J.2    Gohla, A.3
  • 124
    • 0016358751 scopus 로고
    • Phase-specific genes for macroconidiation in Neurospora crassa
    • Selitrennikoff, C. P., R. E. Nelson, and R. W. Siegel, 1974 Phase-specific genes for macroconidiation in Neurospora crassa. Genetics 78: 679-690.
    • (1974) Genetics , vol.78 , pp. 679-690
    • Selitrennikoff, C.P.1    Nelson, R.E.2    Siegel, R.W.3
  • 125
    • 84878431342 scopus 로고    scopus 로고
    • Phosphatase: PP2A structural importance, regulation and its aberrant expression in cancer
    • Seshacharyulu, P., P. Pandey, K. Datta, and S. K. Batra, 2013 Phosphatase: PP2A structural importance, regulation and its aberrant expression in cancer. Cancer Lett. 335: 9-18.
    • (2013) Cancer Lett. , vol.335 , pp. 9-18
    • Seshacharyulu, P.1    Pandey, P.2    Datta, K.3    Batra, S.K.4
  • 126
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: mechanism through structure
    • Shi, Y., 2009 Serine/threonine phosphatases: mechanism through structure. Cell 139: 468-484.
    • (2009) Cell , vol.139 , pp. 468-484
    • Shi, Y.1
  • 127
    • 0029906773 scopus 로고    scopus 로고
    • Cdc28 tyrosine phosphorylation and the morphogenesis checkpoint in budding yeast
    • Sia, R. A., H. A. Herald, and D. J. Lew, 1996 Cdc28 tyrosine phosphorylation and the morphogenesis checkpoint in budding yeast. Mol. Biol. Cell 7: 1657-1666.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1657-1666
    • Sia, R.A.1    Herald, H.A.2    Lew, D.J.3
  • 128
    • 0034705625 scopus 로고    scopus 로고
    • Psr1p/Psr2p, two plasma membrane phosphatases with an essential DXDX(T/V) motif required for sodium stress response in yeast
    • Siniossoglou, S., E. C. Hurt, and H. R. Pelham, 2000 Psr1p/Psr2p, two plasma membrane phosphatases with an essential DXDX(T/V) motif required for sodium stress response in yeast. J. Biol. Chem. 275: 19352-19360.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19352-19360
    • Siniossoglou, S.1    Hurt, E.C.2    Pelham, H.R.3
  • 129
    • 77956144334 scopus 로고    scopus 로고
    • Transcription factors in light and circadian clock signaling networks revealed by genomewide mapping of direct targets for Neurospora white collar complex
    • Smith, K. M., G. Sancar, R. Dekhang, C. M. Sullivan, S. Li et al., 2010 Transcription factors in light and circadian clock signaling networks revealed by genomewide mapping of direct targets for Neurospora white collar complex. Eukaryot. Cell 9: 1549-1556.
    • (2010) Eukaryot. Cell , vol.9 , pp. 1549-1556
    • Smith, K.M.1    Sancar, G.2    Dekhang, R.3    Sullivan, C.M.4    Li, S.5
  • 130
    • 0038874611 scopus 로고
    • Role of nitrogen in the photoinduction of protoperithecia and carotenoids in Neurospora crassa
    • Sommer, T., F. Degliinnocenti, and V. E. A. Russo, 1987 Role of nitrogen in the photoinduction of protoperithecia and carotenoids in Neurospora crassa. Planta 170: 205-208.
    • (1987) Planta , vol.170 , pp. 205-208
    • Sommer, T.1    Degliinnocenti, F.2    Russo, V.E.A.3
  • 131
    • 64749095066 scopus 로고    scopus 로고
    • Analysis of all protein phosphatase genes in Aspergillus nidulans identifies a new mitotic regulator, fcp1
    • Son, S., and S. A. Osmani, 2009 Analysis of all protein phosphatase genes in Aspergillus nidulans identifies a new mitotic regulator, fcp1. Eukaryot. Cell 8: 573-585.
    • (2009) Eukaryot. Cell , vol.8 , pp. 573-585
    • Son, S.1    Osmani, S.A.2
  • 132
    • 0027620486 scopus 로고
    • Genetic control of fungal differentiation: the three sporulation pathways of Neurospora crassa
    • Springer, M. L., 1993 Genetic control of fungal differentiation: the three sporulation pathways of Neurospora crassa. Bioessays 15: 365-374.
    • (1993) Bioessays , vol.15 , pp. 365-374
    • Springer, M.L.1
  • 133
    • 0024651274 scopus 로고
    • A morphological and genetic analysis of conidiophore development in Neurospora crassa
    • Springer, M. L., and C. Yanofsky, 1989 A morphological and genetic analysis of conidiophore development in Neurospora crassa. Genes Dev. 3: 559-571.
    • (1989) Genes Dev. , vol.3 , pp. 559-571
    • Springer, M.L.1    Yanofsky, C.2
  • 134
    • 9444236854 scopus 로고    scopus 로고
    • Oxidative stress activates FUS1 and RLM1 transcription in the yeast Saccharomyces cerevisiae in an oxidant-dependent manner
    • Staleva, L., A. Hall, and S. J. Orlow, 2004 Oxidative stress activates FUS1 and RLM1 transcription in the yeast Saccharomyces cerevisiae in an oxidant-dependent manner. Mol. Biol. Cell 15: 5574-5582.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5574-5582
    • Staleva, L.1    Hall, A.2    Orlow, S.J.3
  • 135
    • 10944240060 scopus 로고    scopus 로고
    • Closing mitosis: the functions of the Cdc14 phosphatase and its regulation
    • Stegmeier, F., and A. Amon, 2004 Closing mitosis: the functions of the Cdc14 phosphatase and its regulation. Annu. Rev. Genet. 38: 203-232.
    • (2004) Annu. Rev. Genet. , vol.38 , pp. 203-232
    • Stegmeier, F.1    Amon, A.2
  • 136
    • 78651165488 scopus 로고
    • Mutational alteration of permeability in Neurospora: effects on growth and the uptake of certain amino acids and related compounds
    • St. Lawrence, P., B. D. Maling, L. Altwerger, and M. Rachmeler, 1964 Mutational alteration of permeability in Neurospora: effects on growth and the uptake of certain amino acids and related compounds. Genetics 50: 1383-1402.
    • (1964) Genetics , vol.50 , pp. 1383-1402
    • St. Lawrence, P.1    Maling, B.D.2    Altwerger, L.3    Rachmeler, M.4
  • 137
    • 17844403782 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases and signalling
    • Stoker, A. W., 2005 Protein tyrosine phosphatases and signalling. J. Endocrinol. 185: 19-33.
    • (2005) J. Endocrinol. , vol.185 , pp. 19-33
    • Stoker, A.W.1
  • 138
    • 80053321725 scopus 로고    scopus 로고
    • Identification of the CRE-1 cellulolytic regulon in Neurospora crassa
    • Sun, J., and N. L. Glass, 2011 Identification of the CRE-1 cellulolytic regulon in Neurospora crassa. PLoS ONE 6: e25654.
    • (2011) PLoS ONE , vol.6
    • Sun, J.1    Glass, N.L.2
  • 139
    • 0030816398 scopus 로고    scopus 로고
    • The activity of Cdc14p, an oligomeric dual specificity protein phosphatase from Saccharomyces cerevisiae, is required for cell cycle progression
    • Taylor, G. S., Y. Liu, C. Baskerville, and H. Charbonneau, 1997 The activity of Cdc14p, an oligomeric dual specificity protein phosphatase from Saccharomyces cerevisiae, is required for cell cycle progression. J. Biol. Chem. 272: 24054-24063.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24054-24063
    • Taylor, G.S.1    Liu, Y.2    Baskerville, C.3    Charbonneau, H.4
  • 140
    • 76049107428 scopus 로고    scopus 로고
    • Systems analysis of plant cell wall degradation by the model filamentous fungus Neurospora crassa
    • Tian, C., W. T. Beeson, A. T. Iavarone, J. Sun, M. A. Marletta et al., 2009 Systems analysis of plant cell wall degradation by the model filamentous fungus Neurospora crassa. Proc. Natl. Acad. Sci. USA 106: 22157-22162.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 22157-22162
    • Tian, C.1    Beeson, W.T.2    Iavarone, A.T.3    Sun, J.4    Marletta, M.A.5
  • 141
    • 0028074668 scopus 로고
    • Enzyme inactivation related to a hyperoxidant state during conidiation of Neurospora crassa
    • Toledo, I., J. Aguirre, and W. Hansberg, 1994 Enzyme inactivation related to a hyperoxidant state during conidiation of Neurospora crassa. Microbiology 140(Pt 9): 2391-2397.
    • (1994) Microbiology , vol.140 , Issue.PART 9 , pp. 2391-2397
    • Toledo, I.1    Aguirre, J.2    Hansberg, W.3
  • 142
    • 33750299450 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: from genes, to function, to disease
    • Tonks, N. K., 2006 Protein tyrosine phosphatases: from genes, to function, to disease. Nat. Rev. Mol. Cell Biol. 7: 833-846.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 833-846
    • Tonks, N.K.1
  • 143
    • 80053100694 scopus 로고    scopus 로고
    • Phenotypic analysis of Neurospora crassa gene deletion strains
    • Turner, G. E., 2011 Phenotypic analysis of Neurospora crassa gene deletion strains. Methods Mol. Biol. 722: 191-198.
    • (2011) Methods Mol. Biol. , vol.722 , pp. 191-198
    • Turner, G.E.1
  • 144
    • 0001963674 scopus 로고
    • A convenient growth medium for Neurospora
    • Vogel, H. J., 1956 A convenient growth medium for Neurospora. Microbial. Genet. Bull. 13: 42-46.
    • (1956) Microbial. Genet. Bull. , vol.13 , pp. 42-46
    • Vogel, H.J.1
  • 145
    • 0034750802 scopus 로고    scopus 로고
    • Ptc1, a type 2C Ser/Thr phosphatase, inactivates the HOG pathway by dephosphorylating the mitogen-activated protein kinase Hog1
    • Warmka, J., J. Hanneman, J. Lee, D. Amin, and I. Ota, 2001 Ptc1, a type 2C Ser/Thr phosphatase, inactivates the HOG pathway by dephosphorylating the mitogen-activated protein kinase Hog1. Mol. Cell. Biol. 21: 51-60.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 51-60
    • Warmka, J.1    Hanneman, J.2    Lee, J.3    Amin, D.4    Ota, I.5
  • 146
    • 0001355008 scopus 로고
    • Neurospora-V-a Synthetic Medium Favoring Sexual Reproduction
    • Westergaard, M., and H. K. Mitchell, 1947 Neurospora-V-a Synthetic Medium Favoring Sexual Reproduction. Am. J. Bot. 34: 573-577.
    • (1947) Am. J. Bot. , vol.34 , pp. 573-577
    • Westergaard, M.1    Mitchell, H.K.2
  • 147
    • 0032928614 scopus 로고    scopus 로고
    • Mitogenactivated protein kinase: conservation of a three-kinase module from yeast to human
    • Widmann, C., S. Gibson, M. B. Jarpe, and G. L. Johnson, 1999 Mitogenactivated protein kinase: conservation of a three-kinase module from yeast to human. Physiol. Rev. 79: 143-180.
    • (1999) Physiol. Rev. , vol.79 , pp. 143-180
    • Widmann, C.1    Gibson, S.2    Jarpe, M.B.3    Johnson, G.L.4
  • 149
    • 1542328903 scopus 로고    scopus 로고
    • Models for biological phosphoryl transfer
    • Williams, N. H., 2004 Models for biological phosphoryl transfer. Biochim. Biophys. Acta 1697: 279-287.
    • (2004) Biochim. Biophys. Acta , vol.1697 , pp. 279-287
    • Williams, N.H.1
  • 150
    • 84873733244 scopus 로고    scopus 로고
    • Direct cellobiose production from cellulose using sextuple beta-glucosidase gene deletion Neurospora crassa mutants
    • Wu, W., A. Hildebrand, T. Kasuga, X. Xiong, and Z. Fan, 2013 Direct cellobiose production from cellulose using sextuple beta-glucosidase gene deletion Neurospora crassa mutants. Enzyme Microb. Technol. 52: 184-189.
    • (2013) Enzyme Microb. Technol. , vol.52 , pp. 184-189
    • Wu, W.1    Hildebrand, A.2    Kasuga, T.3    Xiong, X.4    Fan, Z.5
  • 151
    • 0031027466 scopus 로고    scopus 로고
    • Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein kinase by the PTP2 and PTP3 protein tyrosine phosphatases
    • Wurgler-Murphy, S. M., T. Maeda, E. A. Witten, and H. Saito, 1997 Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein kinase by the PTP2 and PTP3 protein tyrosine phosphatases. Mol. Cell. Biol. 17: 1289-1297.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1289-1297
    • Wurgler-Murphy, S.M.1    Maeda, T.2    Witten, E.A.3    Saito, H.4
  • 152
    • 33750006297 scopus 로고    scopus 로고
    • Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins
    • Xing, Y., Y. Xu, Y. Chen, P. D. Jeffrey, Y. Chao et al., 2006 Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins. Cell 127: 341-353.
    • (2006) Cell , vol.127 , pp. 341-353
    • Xing, Y.1    Xu, Y.2    Chen, Y.3    Jeffrey, P.D.4    Chao, Y.5
  • 153
    • 33845404441 scopus 로고    scopus 로고
    • Structure of the protein phosphatase 2A holoenzyme
    • Xu, Y., Y. Xing, Y. Chen, Y. Chao, Z. Lin et al., 2006 Structure of the protein phosphatase 2A holoenzyme. Cell 127: 1239-1251.
    • (2006) Cell , vol.127 , pp. 1239-1251
    • Xu, Y.1    Xing, Y.2    Chen, Y.3    Chao, Y.4    Lin, Z.5
  • 154
    • 1042266554 scopus 로고    scopus 로고
    • Distinct roles for PP1 and PP2A in the Neurospora circadian clock
    • Yang, Y., Q. He, P. Cheng, P. Wrage, O. Yarden et al., 2004 Distinct roles for PP1 and PP2A in the Neurospora circadian clock. Genes Dev. 18: 255-260.
    • (2004) Genes Dev. , vol.18 , pp. 255-260
    • Yang, Y.1    He, Q.2    Cheng, P.3    Wrage, P.4    Yarden, O.5
  • 155
    • 0031659579 scopus 로고    scopus 로고
    • Protein phosphatase 2A is involved in hyphal growth of Neurospora crassa
    • Yatzkan, E., B. Szoor, Z. Feher, V. Dombradi, and O. Yarden, 1998 Protein phosphatase 2A is involved in hyphal growth of Neurospora crassa. Mol. Gen. Genet. 259: 523-531.
    • (1998) Mol. Gen. Genet. , vol.259 , pp. 523-531
    • Yatzkan, E.1    Szoor, B.2    Feher, Z.3    Dombradi, V.4    Yarden, O.5
  • 156
    • 0036500159 scopus 로고    scopus 로고
    • The Ppz protein phosphatases are key regulators of K+ and pH homeostasis: implications for salt tolerance, cell wall integrity and cell cycle progression
    • Yenush, L., J. M. Mulet, J. Arino, and R. Serrano, 2002 The Ppz protein phosphatases are key regulators of K+ and pH homeostasis: implications for salt tolerance, cell wall integrity and cell cycle progression. EMBO J. 21: 920-929.
    • (2002) EMBO J. , vol.21 , pp. 920-929
    • Yenush, L.1    Mulet, J.M.2    Arino, J.3    Serrano, R.4
  • 157
    • 79954882400 scopus 로고    scopus 로고
    • Comprehensive phenotypic analysis of single-gene deletion and overexpression strains of Saccharomyces cerevisiae
    • Yoshikawa, K., T. Tanaka, Y. Ida, C. Furusawa, T. Hirasawa et al., 2011 Comprehensive phenotypic analysis of single-gene deletion and overexpression strains of Saccharomyces cerevisiae. Yeast 28: 349-361.
    • (2011) Yeast , vol.28 , pp. 349-361
    • Yoshikawa, K.1    Tanaka, T.2    Ida, Y.3    Furusawa, C.4    Hirasawa, T.5
  • 158
    • 0037657573 scopus 로고    scopus 로고
    • Role of Ptc2 type 2C Ser/Thr phosphatase in yeast high-osmolarity glycerol pathway inactivation
    • Young, C., J. Mapes, J. Hanneman, S. Al-Zarban, and I. Ota, 2002 Role of Ptc2 type 2C Ser/Thr phosphatase in yeast high-osmolarity glycerol pathway inactivation. Eukaryot. Cell 1: 1032-1040.
    • (2002) Eukaryot. Cell , vol.1 , pp. 1032-1040
    • Young, C.1    Mapes, J.2    Hanneman, J.3    Al-Zarban, S.4    Ota, I.5
  • 159
    • 0033996104 scopus 로고    scopus 로고
    • Essential functions of protein tyrosine phosphatases PTP2 and PTP3 and RIM11 tyrosine phosphorylation in Saccharomyces cerevisiae meiosis and sporulation
    • Zhan, X. L., Y. Hong, T. Zhu, A. P. Mitchell, R. J. Deschenes et al., 2000 Essential functions of protein tyrosine phosphatases PTP2 and PTP3 and RIM11 tyrosine phosphorylation in Saccharomyces cerevisiae meiosis and sporulation. Mol. Biol. Cell 11: 663-676.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 663-676
    • Zhan, X.L.1    Hong, Y.2    Zhu, T.3    Mitchell, A.P.4    Deschenes, R.J.5
  • 160
    • 84863229897 scopus 로고    scopus 로고
    • Ssu72 Phosphatase-dependent Erasure of Phospho-Ser7 Marks on the RNA Polymerase II C-terminal Domain Is Essential for Viability and Transcription Termination
    • Zhang, D. W., A. L. Mosley, S. R. Ramisetty, J. B. Rodriguez-Molina, M. P. Washburn et al., 2012 Ssu72 Phosphatase-dependent Erasure of Phospho-Ser7 Marks on the RNA Polymerase II C-terminal Domain Is Essential for Viability and Transcription Termination. J. Biol. Chem. 287: 8541-8551.
    • (2012) J. Biol. Chem. , vol.287 , pp. 8541-8551
    • Zhang, D.W.1    Mosley, A.L.2    Ramisetty, S.R.3    Rodriguez-Molina, J.B.4    Washburn, M.P.5
  • 161
    • 77951587359 scopus 로고    scopus 로고
    • Structural and functional analysis of the phosphoryl transfer reaction mediated by the human small C-terminal domain phosphatase, Scp1
    • Zhang, M., J. Liu, Y. Kim, J. E. Dixon, S. L. Pfaff et al., 2010 Structural and functional analysis of the phosphoryl transfer reaction mediated by the human small C-terminal domain phosphatase, Scp1. Protein Sci. 19: 974-986.
    • (2010) Protein Sci. , vol.19 , pp. 974-986
    • Zhang, M.1    Liu, J.2    Kim, Y.3    Dixon, J.E.4    Pfaff, S.L.5
  • 162
    • 0036156879 scopus 로고    scopus 로고
    • Osmoregulation and fungicide resistance: the Neurospora crassa os-2 gene encodes a HOG1 mitogen-activated protein kinase homologue
    • Zhang, Y., R. Lamm, C. Pillonel, S. Lam, and J. R. Xu, 2002 Osmoregulation and fungicide resistance: the Neurospora crassa os-2 gene encodes a HOG1 mitogen-activated protein kinase homologue. Appl. Environ. Microbiol. 68: 532-538.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 532-538
    • Zhang, Y.1    Lamm, R.2    Pillonel, C.3    Lam, S.4    Xu, J.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.