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Volumn 6, Issue 7, 2011, Pages

Torsina and the Torsina-Interacting protein printor have no impact on endoplasmic reticulum stress or protein trafficking in yeast

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PRINTOR; TORSINA; UNCLASSIFIED DRUG; ALPHA SYNUCLEIN; CARRIER PROTEIN; CHAPERONE; SIGNAL PEPTIDE;

EID: 79960804408     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0022744     Document Type: Article
Times cited : (6)

References (53)
  • 1
    • 0027988344 scopus 로고
    • Dystonia in Ashkenazi Jews: clinical characterization of a founder mutation
    • Bressman SB, de Leon D, Kramer PL, Ozelius LJ, Brin MF, et al. (1994) Dystonia in Ashkenazi Jews: clinical characterization of a founder mutation. Ann Neurol 36: 771-777.
    • (1994) Ann Neurol , vol.36 , pp. 771-777
    • Bressman, S.B.1    de Leon, D.2    Kramer, P.L.3    Ozelius, L.J.4    Brin, M.F.5
  • 2
    • 0034623158 scopus 로고    scopus 로고
    • Torsin A and its torsion dystonia-associated mutant forms are lumenal glycoproteins that exhibit distinct subcellular localizations
    • Kustedjo K, Bracey MH, Cravatt BF, (2000) Torsin A and its torsion dystonia-associated mutant forms are lumenal glycoproteins that exhibit distinct subcellular localizations. J Biol Chem 275: 27933-27939.
    • (2000) J Biol Chem , vol.275 , pp. 27933-27939
    • Kustedjo, K.1    Bracey, M.H.2    Cravatt, B.F.3
  • 3
    • 0037445915 scopus 로고    scopus 로고
    • TorsinA in PC12 cells: localization in the endoplasmic reticulum and response to stress
    • Hewett J, Ziefer P, Bergeron D, Naismith T, Boston H, et al. (2003) TorsinA in PC12 cells: localization in the endoplasmic reticulum and response to stress. J Neurosci Res 72: 158-168.
    • (2003) J Neurosci Res , vol.72 , pp. 158-168
    • Hewett, J.1    Ziefer, P.2    Bergeron, D.3    Naismith, T.4    Boston, H.5
  • 4
    • 69249150847 scopus 로고    scopus 로고
    • Printor, a novel torsinA-interacting protein implicated in dystonia pathogenesis
    • Giles LM, Li L, Chin LS, (2009) Printor, a novel torsinA-interacting protein implicated in dystonia pathogenesis. J Biol Chem 284: 21765-21775.
    • (2009) J Biol Chem , vol.284 , pp. 21765-21775
    • Giles, L.M.1    Li, L.2    Chin, L.S.3
  • 5
    • 0042326841 scopus 로고    scopus 로고
    • Characterization of human torsinA and its dystonia-associated mutant form
    • Liu Z, Zolkiewska A, Zolkiewski M, (2003) Characterization of human torsinA and its dystonia-associated mutant form. Biochem J 374: 117-122.
    • (2003) Biochem J , vol.374 , pp. 117-122
    • Liu, Z.1    Zolkiewska, A.2    Zolkiewski, M.3
  • 6
    • 16944366666 scopus 로고    scopus 로고
    • The early-onset torsion dystonia gene (DYT1) encodes an ATP-binding protein
    • Ozelius LJ, Hewett JW, Page CE, Bressman SB, Kramer PL, et al. (1997) The early-onset torsion dystonia gene (DYT1) encodes an ATP-binding protein. Nat Genet 17: 40-48.
    • (1997) Nat Genet , vol.17 , pp. 40-48
    • Ozelius, L.J.1    Hewett, J.W.2    Page, C.E.3    Bressman, S.B.4    Kramer, P.L.5
  • 8
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell DA, Kowal AS, Singer MA, Lindquist S, (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372: 475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 9
    • 34247245632 scopus 로고    scopus 로고
    • Neuroprotection by Hsp104 and Hsp27 in lentiviral-based rat models of Huntington's disease
    • Perrin V, Regulier E, Abbas-Terki T, Hassig R, Brouillet E, et al. (2007) Neuroprotection by Hsp104 and Hsp27 in lentiviral-based rat models of Huntington's disease. Mol Ther 15: 903-911.
    • (2007) Mol Ther , vol.15 , pp. 903-911
    • Perrin, V.1    Regulier, E.2    Abbas-Terki, T.3    Hassig, R.4    Brouillet, E.5
  • 10
    • 8144230422 scopus 로고    scopus 로고
    • Effect of torsinA on membrane proteins reveals a loss of function and a dominant-negative phenotype of the dystonia-associated DeltaE-torsinA mutant
    • Torres GE, Sweeney AL, Beaulieu JM, Shashidharan P, Caron MG, (2004) Effect of torsinA on membrane proteins reveals a loss of function and a dominant-negative phenotype of the dystonia-associated DeltaE-torsinA mutant. Proc Natl Acad Sci U S A 101: 15650-15655.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 15650-15655
    • Torres, G.E.1    Sweeney, A.L.2    Beaulieu, J.M.3    Shashidharan, P.4    Caron, M.G.5
  • 11
    • 34249850241 scopus 로고    scopus 로고
    • Mutant torsinA interferes with protein processing through the secretory pathway in DYT1 dystonia cells
    • Hewett JW, Tannous B, Niland BP, Nery FC, Zeng J, et al. (2007) Mutant torsinA interferes with protein processing through the secretory pathway in DYT1 dystonia cells. Proc Natl Acad Sci U S A 104: 7271-7276.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7271-7276
    • Hewett, J.W.1    Tannous, B.2    Niland, B.P.3    Nery, F.C.4    Zeng, J.5
  • 12
    • 77955710947 scopus 로고    scopus 로고
    • The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro
    • Burdette AJ, Churchill PF, Caldwell GA, Caldwell KA, (2010) The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro. Cell Stress Chaperones.
    • (2010) Cell Stress Chaperones
    • Burdette, A.J.1    Churchill, P.F.2    Caldwell, G.A.3    Caldwell, K.A.4
  • 13
    • 77956113164 scopus 로고    scopus 로고
    • The early-onset torsion dystonia-associated protein, torsinA, is a homeostatic regulator of endoplasmic reticulum stress response
    • Chen P, Burdette AJ, Porter JC, Ricketts JC, Fox SA, et al. (2010) The early-onset torsion dystonia-associated protein, torsinA, is a homeostatic regulator of endoplasmic reticulum stress response. Hum Mol Genet 19: 3502-3515.
    • (2010) Hum Mol Genet , vol.19 , pp. 3502-3515
    • Chen, P.1    Burdette, A.J.2    Porter, J.C.3    Ricketts, J.C.4    Fox, S.A.5
  • 14
    • 79954415475 scopus 로고    scopus 로고
    • Exploring the influence of torsinA expression on protein quality control
    • Gordon KL, Glenn KA, Gonzalez-Alegre P, (2011) Exploring the influence of torsinA expression on protein quality control. Neurochem Res 36: 452-459.
    • (2011) Neurochem Res , vol.36 , pp. 452-459
    • Gordon, K.L.1    Glenn, K.A.2    Gonzalez-Alegre, P.3
  • 15
    • 0033987354 scopus 로고    scopus 로고
    • Immunohistochemical localization and distribution of torsinA in normal human and rat brain
    • Shashidharan P, Kramer BC, Walker RH, Olanow CW, Brin MF, (2000) Immunohistochemical localization and distribution of torsinA in normal human and rat brain. Brain Res 853: 197-206.
    • (2000) Brain Res , vol.853 , pp. 197-206
    • Shashidharan, P.1    Kramer, B.C.2    Walker, R.H.3    Olanow, C.W.4    Brin, M.F.5
  • 16
    • 0034703336 scopus 로고    scopus 로고
    • TorsinA accumulation in Lewy bodies in sporadic Parkinson's disease
    • Shashidharan P, Good PF, Hsu A, Perl DP, Brin MF, et al. (2000) TorsinA accumulation in Lewy bodies in sporadic Parkinson's disease. Brain Res 877: 379-381.
    • (2000) Brain Res , vol.877 , pp. 379-381
    • Shashidharan, P.1    Good, P.F.2    Hsu, A.3    Perl, D.P.4    Brin, M.F.5
  • 17
    • 0036846119 scopus 로고    scopus 로고
    • TorsinA and heat shock proteins act as molecular chaperones: suppression of alpha-synuclein aggregation
    • McLean PJ, Kawamata H, Shariff S, Hewett J, Sharma N, et al. (2002) TorsinA and heat shock proteins act as molecular chaperones: suppression of alpha-synuclein aggregation. J Neurochem 83: 846-854.
    • (2002) J Neurochem , vol.83 , pp. 846-854
    • McLean, P.J.1    Kawamata, H.2    Shariff, S.3    Hewett, J.4    Sharma, N.5
  • 18
    • 17644392138 scopus 로고    scopus 로고
    • Torsin-mediated protection from cellular stress in the dopaminergic neurons of Caenorhabditis elegans
    • Cao S, Gelwix CC, Caldwell KA, Caldwell GA, (2005) Torsin-mediated protection from cellular stress in the dopaminergic neurons of Caenorhabditis elegans. J Neurosci 25: 3801-3812.
    • (2005) J Neurosci , vol.25 , pp. 3801-3812
    • Cao, S.1    Gelwix, C.C.2    Caldwell, K.A.3    Caldwell, G.A.4
  • 19
    • 77952741735 scopus 로고    scopus 로고
    • Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker's yeast?
    • Khurana V, Lindquist S, (2010) Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker's yeast? Nat Rev Neurosci 11: 436-449.
    • (2010) Nat Rev Neurosci , vol.11 , pp. 436-449
    • Khurana, V.1    Lindquist, S.2
  • 20
    • 71949098172 scopus 로고    scopus 로고
    • Signalling pathways in the unfolded protein response: development from yeast to mammals
    • Mori K, (2009) Signalling pathways in the unfolded protein response: development from yeast to mammals. J Biochem 146: 743-750.
    • (2009) J Biochem , vol.146 , pp. 743-750
    • Mori, K.1
  • 22
    • 0034652127 scopus 로고    scopus 로고
    • Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
    • Krobitsch S, Lindquist S, (2000) Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc Natl Acad Sci U S A 97: 1589-1594.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 1589-1594
    • Krobitsch, S.1    Lindquist, S.2
  • 23
    • 0345189364 scopus 로고    scopus 로고
    • Yeast cells provide insight into alpha-synuclein biology and pathobiology
    • Outeiro TF, Lindquist S, (2003) Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science 302: 1772-1775.
    • (2003) Science , vol.302 , pp. 1772-1775
    • Outeiro, T.F.1    Lindquist, S.2
  • 24
    • 3242793658 scopus 로고    scopus 로고
    • Searching for the most effective screening system to identify cell-active inhibitors of beta-secretase
    • Middendorp O, Luthi U, Hausch F, Barberis A, (2004) Searching for the most effective screening system to identify cell-active inhibitors of beta-secretase. Biol Chem 385: 481-485.
    • (2004) Biol Chem , vol.385 , pp. 481-485
    • Middendorp, O.1    Luthi, U.2    Hausch, F.3    Barberis, A.4
  • 25
    • 35448944853 scopus 로고    scopus 로고
    • Alzheimer's Abeta fused to green fluorescent protein induces growth stress and a heat shock response
    • Caine J, Sankovich S, Antony H, Waddington L, Macreadie P, et al. (2007) Alzheimer's Abeta fused to green fluorescent protein induces growth stress and a heat shock response. FEMS Yeast Res 7: 1230-1236.
    • (2007) FEMS Yeast Res , vol.7 , pp. 1230-1236
    • Caine, J.1    Sankovich, S.2    Antony, H.3    Waddington, L.4    Macreadie, P.5
  • 26
    • 44849144494 scopus 로고    scopus 로고
    • A new method to measure cellular toxicity of non-fibrillar and fibrillar Alzheimer's Abeta using yeast
    • Bharadwaj P, Waddington L, Varghese J, Macreadie IG, (2008) A new method to measure cellular toxicity of non-fibrillar and fibrillar Alzheimer's Abeta using yeast. J Alzheimers Dis 13: 147-150.
    • (2008) J Alzheimers Dis , vol.13 , pp. 147-150
    • Bharadwaj, P.1    Waddington, L.2    Varghese, J.3    Macreadie, I.G.4
  • 27
    • 33746533924 scopus 로고    scopus 로고
    • Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models
    • Cooper AA, Gitler AD, Cashikar A, Haynes CM, Hill KJ, et al. (2006) Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science 313: 324-328.
    • (2006) Science , vol.313 , pp. 324-328
    • Cooper, A.A.1    Gitler, A.D.2    Cashikar, A.3    Haynes, C.M.4    Hill, K.J.5
  • 28
    • 61349147706 scopus 로고    scopus 로고
    • Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity
    • Gitler AD, Chesi A, Geddie ML, Strathearn KE, Hamamichi S, et al. (2009) Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity. Nat Genet 41: 308-315.
    • (2009) Nat Genet , vol.41 , pp. 308-315
    • Gitler, A.D.1    Chesi, A.2    Geddie, M.L.3    Strathearn, K.E.4    Hamamichi, S.5
  • 29
    • 61349114190 scopus 로고    scopus 로고
    • Bridging high-throughput genetic and transcriptional data reveals cellular responses to alpha-synuclein toxicity
    • Yeger-Lotem E, Riva L, Su LJ, Gitler AD, Cashikar AG, et al. (2009) Bridging high-throughput genetic and transcriptional data reveals cellular responses to alpha-synuclein toxicity. Nat Genet 41: 316-323.
    • (2009) Nat Genet , vol.41 , pp. 316-323
    • Yeger-Lotem, E.1    Riva, L.2    Su, L.J.3    Gitler, A.D.4    Cashikar, A.G.5
  • 30
    • 77949438990 scopus 로고    scopus 로고
    • Compounds from an unbiased chemical screen reverse both ER-to-Golgi trafficking defects and mitochondrial dysfunction in Parkinson's disease models
    • Su LJ, Auluck PK, Outeiro TF, Yeger-Lotem E, Kritzer JA, et al. (2010) Compounds from an unbiased chemical screen reverse both ER-to-Golgi trafficking defects and mitochondrial dysfunction in Parkinson's disease models. Dis Model Mech 3: 194-208.
    • (2010) Dis Model Mech , vol.3 , pp. 194-208
    • Su, L.J.1    Auluck, P.K.2    Outeiro, T.F.3    Yeger-Lotem, E.4    Kritzer, J.A.5
  • 31
    • 0026756722 scopus 로고
    • Purification and characterization of BiP/Kar2 protein from Saccharomyces cerevisiae
    • Tokunaga M, Kawamura A, Kohno K, (1992) Purification and characterization of BiP/Kar2 protein from Saccharomyces cerevisiae. J Biol Chem 267: 17553-17559.
    • (1992) J Biol Chem , vol.267 , pp. 17553-17559
    • Tokunaga, M.1    Kawamura, A.2    Kohno, K.3
  • 32
    • 0024427039 scopus 로고
    • Control of protein exit from the endoplasmic reticulum
    • Pelham HR, (1989) Control of protein exit from the endoplasmic reticulum. Annu Rev Cell Biol 5: 1-23.
    • (1989) Annu Rev Cell Biol , vol.5 , pp. 1-23
    • Pelham, H.R.1
  • 34
    • 0030838041 scopus 로고    scopus 로고
    • Use of conditional promoters for expression of heterologous proteins in Saccharomyces cerevisiae
    • Ronicke V, Graulich W, Mumberg D, Muller R, Funk M, (1997) Use of conditional promoters for expression of heterologous proteins in Saccharomyces cerevisiae. Methods Enzymol 283: 313-322.
    • (1997) Methods Enzymol , vol.283 , pp. 313-322
    • Ronicke, V.1    Graulich, W.2    Mumberg, D.3    Muller, R.4    Funk, M.5
  • 35
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox JS, Shamu CE, Walter P, (1993) Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73: 1197-1206.
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 36
    • 0031610364 scopus 로고    scopus 로고
    • Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
    • Pollard MG, Travers KJ, Weissman JS, (1998) Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol Cell 1: 171-182.
    • (1998) Mol Cell , vol.1 , pp. 171-182
    • Pollard, M.G.1    Travers, K.J.2    Weissman, J.S.3
  • 37
    • 54249121433 scopus 로고    scopus 로고
    • The torsin-family AAA+ protein OOC-5 contains a critical disulfide adjacent to Sensor-II that couples redox state to nucleotide binding
    • Zhu L, Wrabl JO, Hayashi AP, Rose LS, Thomas PJ, (2008) The torsin-family AAA+ protein OOC-5 contains a critical disulfide adjacent to Sensor-II that couples redox state to nucleotide binding. Mol Biol Cell 19: 3599-3612.
    • (2008) Mol Biol Cell , vol.19 , pp. 3599-3612
    • Zhu, L.1    Wrabl, J.O.2    Hayashi, A.P.3    Rose, L.S.4    Thomas, P.J.5
  • 38
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand AR, Kaiser CA, (1998) The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1: 161-170.
    • (1998) Mol Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 39
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers KJ, Patil CK, Wodicka L, Lockhart DJ, Weissman JS, et al. (2000) Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101: 249-258.
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5
  • 40
    • 43149106506 scopus 로고    scopus 로고
    • The dystonia-associated protein torsinA modulates synaptic vesicle recycling
    • Granata A, Watson R, Collinson LM, Schiavo G, Warner TT, (2008) The dystonia-associated protein torsinA modulates synaptic vesicle recycling. J Biol Chem 283: 7568-7579.
    • (2008) J Biol Chem , vol.283 , pp. 7568-7579
    • Granata, A.1    Watson, R.2    Collinson, L.M.3    Schiavo, G.4    Warner, T.T.5
  • 41
    • 0027404604 scopus 로고
    • The molecular machinery for secretion is conserved from yeast to neurons
    • Bennett MK, Scheller RH, (1993) The molecular machinery for secretion is conserved from yeast to neurons. Proc Natl Acad Sci U S A 90: 2559-2563.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2559-2563
    • Bennett, M.K.1    Scheller, R.H.2
  • 42
    • 0027198483 scopus 로고
    • Identification of a gene required for membrane protein retention in the early secretory pathway
    • Nishikawa S, Nakano A, (1993) Identification of a gene required for membrane protein retention in the early secretory pathway. Proc Natl Acad Sci U S A 90: 8179-8183.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 8179-8183
    • Nishikawa, S.1    Nakano, A.2
  • 43
    • 0037413714 scopus 로고    scopus 로고
    • Yeast is selectively hypersensitised to heat shock protein 90 (Hsp90)-targetting drugs with heterologous expression of the human Hsp90beta, a property that can be exploited in screens for new Hsp90 chaperone inhibitors
    • Piper PW, Panaretou B, Millson SH, Truman A, Mollapour M, et al. (2003) Yeast is selectively hypersensitised to heat shock protein 90 (Hsp90)-targetting drugs with heterologous expression of the human Hsp90beta, a property that can be exploited in screens for new Hsp90 chaperone inhibitors. Gene 302: 165-170.
    • (2003) Gene , vol.302 , pp. 165-170
    • Piper, P.W.1    Panaretou, B.2    Millson, S.H.3    Truman, A.4    Mollapour, M.5
  • 44
    • 49649120229 scopus 로고    scopus 로고
    • Dystonia-associated mutations cause premature degradation of torsinA protein and cell-type-specific mislocalization to the nuclear envelope
    • Giles LM, Chen J, Li L, Chin LS, (2008) Dystonia-associated mutations cause premature degradation of torsinA protein and cell-type-specific mislocalization to the nuclear envelope. Hum Mol Genet 17: 2712-2722.
    • (2008) Hum Mol Genet , vol.17 , pp. 2712-2722
    • Giles, L.M.1    Chen, J.2    Li, L.3    Chin, L.S.4
  • 45
    • 77953153048 scopus 로고    scopus 로고
    • Regulation of basal cellular physiology by the homeostatic unfolded protein response
    • Rutkowski DT, Hegde RS, (2010) Regulation of basal cellular physiology by the homeostatic unfolded protein response. J Cell Biol 189: 783-794.
    • (2010) J Cell Biol , vol.189 , pp. 783-794
    • Rutkowski, D.T.1    Hegde, R.S.2
  • 46
    • 29144460260 scopus 로고    scopus 로고
    • Loss of the dystonia-associated protein torsinA selectively disrupts the neuronal nuclear envelope
    • Goodchild RE, Kim CE, Dauer WT, (2005) Loss of the dystonia-associated protein torsinA selectively disrupts the neuronal nuclear envelope. Neuron 48: 923-932.
    • (2005) Neuron , vol.48 , pp. 923-932
    • Goodchild, R.E.1    Kim, C.E.2    Dauer, W.T.3
  • 47
    • 0033676098 scopus 로고    scopus 로고
    • DNA cloning using in vitro site-specific recombination
    • Hartley JL, Temple GF, Brasch MA, (2000) DNA cloning using in vitro site-specific recombination. Genome Res 10: 1788-1795.
    • (2000) Genome Res , vol.10 , pp. 1788-1795
    • Hartley, J.L.1    Temple, G.F.2    Brasch, M.A.3
  • 48
    • 0033732564 scopus 로고    scopus 로고
    • GATEWAY recombinational cloning: application to the cloning of large numbers of open reading frames or ORFeomes
    • Walhout AJ, Temple GF, Brasch MA, Hartley JL, Lorson MA, et al. (2000) GATEWAY recombinational cloning: application to the cloning of large numbers of open reading frames or ORFeomes. Methods Enzymol 328: 575-592.
    • (2000) Methods Enzymol , vol.328 , pp. 575-592
    • Walhout, A.J.1    Temple, G.F.2    Brasch, M.A.3    Hartley, J.L.4    Lorson, M.A.5
  • 49
    • 35349022993 scopus 로고    scopus 로고
    • A suite of Gateway (R) cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae
    • Alberti S, Gitler AD, Lindquist S, (2007) A suite of Gateway (R) cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae. Yeast 24: 913-919.
    • (2007) Yeast , vol.24 , pp. 913-919
    • Alberti, S.1    Gitler, A.D.2    Lindquist, S.3
  • 50
    • 0029682161 scopus 로고    scopus 로고
    • In vitro recombination and mutagenesis by overlap extension PCR
    • Pogulis RJ, Vallejo AN, Pease LR, (1996) In vitro recombination and mutagenesis by overlap extension PCR. Methods Mol Biol 57: 167-176.
    • (1996) Methods Mol Biol , vol.57 , pp. 167-176
    • Pogulis, R.J.1    Vallejo, A.N.2    Pease, L.R.3
  • 51
    • 0034723456 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro
    • Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O, (2000) Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res 7: 65-73.
    • (2000) DNA Res , vol.7 , pp. 65-73
    • Nagase, T.1    Kikuno, R.2    Ishikawa, K.I.3    Hirosawa, M.4    Ohara, O.5
  • 52
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz D, St Jean A, Woods RA, Schiestl RH, (1992) Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res 20: 1425.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 53
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • Gietz RD, Schiestl RH, Willems AR, Woods RA, (1995) Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11: 355-360.
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.