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Volumn 274, Issue 16, 2007, Pages 4287-4305

Analysis of the vacuolar luminal proteome of Saccharomyces cerevisiae

Author keywords

2D gel electrophoresis; Luminal proteins; Mass spectrometry; Proteome; Vacuole purification

Indexed keywords

GLUTATHIONE; GLYCOSIDASE; ION; LIPID BINDING PROTEIN; PHOSPHATASE; POLYPEPTIDE; PROTEINASE K; PROTEOME; REGULATOR PROTEIN;

EID: 34547780657     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05959.x     Document Type: Article
Times cited : (29)

References (66)
  • 2
    • 0035756320 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae - A model organism for the studies on vacuolar transport
    • Kucharczyk R Rytka J (2001) Saccharomyces cerevisiae - a model organism for the studies on vacuolar transport. Acta Biochim Pol 48, 1025 1042.
    • (2001) Acta Biochim Pol , vol.48 , pp. 1025-1042
    • Kucharczyk, R.1    Rytka, J.2
  • 3
    • 0036702197 scopus 로고    scopus 로고
    • Molecular machinery required for autophagy and the cytoplasm to vacuole targeting (Cvt) pathway in S. cerevisiae
    • Khalfan WA Klionsky DJ (2002) Molecular machinery required for autophagy and the cytoplasm to vacuole targeting (Cvt) pathway in S. cerevisiae. Curr Opin Cell Biol 14, 468 475.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 468-475
    • Khalfan, W.A.1    Klionsky, D.J.2
  • 6
    • 1242294379 scopus 로고    scopus 로고
    • Large-scale characterization of integral proteins from Arabidopsis vacuolar membrane by two-dimensional liquid chromatography
    • Szponarski W, Sommerer N, Boyer JC, Rossignol M Gibrat R (2004) Large-scale characterization of integral proteins from Arabidopsis vacuolar membrane by two-dimensional liquid chromatography. Proteomics 4, 397 406.
    • (2004) Proteomics , vol.4 , pp. 397-406
    • Szponarski, W.1    Sommerer, N.2    Boyer, J.C.3    Rossignol, M.4    Gibrat, R.5
  • 7
    • 15744385479 scopus 로고    scopus 로고
    • The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins
    • Carter C, Pan S, Zouhar J, Avila EL, Girke T Raikhel NV (2004) The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins. Plant Cell 16, 3285 3303.
    • (2004) Plant Cell , vol.16 , pp. 3285-3303
    • Carter, C.1    Pan, S.2    Zouhar, J.3    Avila, E.L.4    Girke, T.5    Raikhel, N.V.6
  • 8
    • 0018668142 scopus 로고
    • Vacuoles: The sole compartments of digestive enzymes in yeast (Saccharomyces cerevisiae)?
    • Wiemken A, Schellenberg M Urech K (1979) Vacuoles: the sole compartments of digestive enzymes in yeast (Saccharomyces cerevisiae)? Arch Microbiol 123, 23 35.
    • (1979) Arch Microbiol , vol.123 , pp. 23-35
    • Wiemken, A.1    Schellenberg, M.2    Urech, K.3
  • 10
    • 0028278224 scopus 로고
    • Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of substrate-binding subunit for proton transport
    • Kim EJ, Zhen R Rea PA (1994) Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of substrate-binding subunit for proton transport. Proc Natl Acad Sci USA 91, 6128 6132.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6128-6132
    • Kim, E.J.1    Zhen, R.2    Rea, P.A.3
  • 11
    • 0029983266 scopus 로고    scopus 로고
    • The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump
    • Li Z-S, Szczypka M, Lu Y-P, Thiele DJ Rea PA (1996) The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump. J Biol Chem 271, 6509 6517.
    • (1996) J Biol Chem , vol.271 , pp. 6509-6517
    • Li, Z.-S.1    Szczypka, M.2    Lu, Y.-P.3    Thiele, D.J.4    Rea, P.A.5
  • 12
    • 0022493616 scopus 로고
    • Gene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y
    • Stevens TH, Rothman JH, Payne GS Schekman R (1986) Gene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y. J Cell Biol 102, 1551 1557.
    • (1986) J Cell Biol , vol.102 , pp. 1551-1557
    • Stevens, T.H.1    Rothman, J.H.2    Payne, G.S.3    Schekman, R.4
  • 13
    • 0025871691 scopus 로고
    • Three proteolytic systems in the yeast Saccharomyces cerevisiae
    • Jones EW (1991) Three proteolytic systems in the yeast Saccharomyces cerevisiae. J Biol Chem 266, 7963 7966.
    • (1991) J Biol Chem , vol.266 , pp. 7963-7966
    • Jones, E.W.1
  • 14
    • 0022001851 scopus 로고
    • Characterization of a specific α-mannosidase involved in oligosaccharide processing in Saccharomyces cerevisiae
    • Jelinek-Kelly S, Akiyama T, Saunier B, Tkacz JS Herscovics A (1985) Characterization of a specific α-mannosidase involved in oligosaccharide processing in Saccharomyces cerevisiae. J Biol Chem 260, 2253 2257.
    • (1985) J Biol Chem , vol.260 , pp. 2253-2257
    • Jelinek-Kelly, S.1    Akiyama, T.2    Saunier, B.3    Tkacz, J.S.4    Herscovics, A.5
  • 15
    • 0023939244 scopus 로고
    • Solubilization and purification of alpha-mannosidase, a marker enzyme of vacuolar membranes in Saccharomyces cerevisiae
    • Yoshihisa T, Ohsumi Y Anraku Y (1988) Solubilization and purification of alpha-mannosidase, a marker enzyme of vacuolar membranes in Saccharomyces cerevisiae. J Biol Chem 263, 5158 5163.
    • (1988) J Biol Chem , vol.263 , pp. 5158-5163
    • Yoshihisa, T.1    Ohsumi, Y.2    Anraku, Y.3
  • 16
    • 0032823270 scopus 로고    scopus 로고
    • Import into and degradation of cytosolic proteins by isolated yeast vacuoles
    • Horst M, Knecht EC Schu PV (1999) Import into and degradation of cytosolic proteins by isolated yeast vacuoles. Mol Biol Cell 10, 2879 2889.
    • (1999) Mol Biol Cell , vol.10 , pp. 2879-2889
    • Horst, M.1    Knecht, E.C.2    Schu, P.V.3
  • 17
    • 0028332917 scopus 로고
    • The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene
    • Marcusson EG, Horazdovsky BF, Cereghino JL, Gharakhanian E Emr SD (1994) The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene. Cell 77, 579 586.
    • (1994) Cell , vol.77 , pp. 579-586
    • Marcusson, E.G.1    Horazdovsky, B.F.2    Cereghino, J.L.3    Gharakhanian, E.4    Emr, S.D.5
  • 18
    • 0029916949 scopus 로고    scopus 로고
    • Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I
    • Oda MN, Scott SV, Hefner GA, Caffarelli AD Klionsky DJ (1996) Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I. J Cell Biol 132, 999 1010.
    • (1996) J Cell Biol , vol.132 , pp. 999-1010
    • Oda, M.N.1    Scott, S.V.2    Hefner, G.A.3    Caffarelli, A.D.4    Klionsky, D.J.5
  • 19
    • 0028308218 scopus 로고
    • Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae - Purification, properties, localization, and processing by protease-b
    • Yasuhara T, Nakai T Ohashi A (1994) Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae - purification, properties, localization, and processing by protease-b. J Biol Chem 269, 13644 13650.
    • (1994) J Biol Chem , vol.269 , pp. 13644-13650
    • Yasuhara, T.1    Nakai, T.2    Ohashi, A.3
  • 20
    • 0022753540 scopus 로고
    • PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors
    • Ammerer G, Hunter CP, Rothman JH, Saari GC, Valls A Stevens TH (1986) PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors. Mol Cell Biol 6, 2490 2499.
    • (1986) Mol Cell Biol , vol.6 , pp. 2490-2499
    • Ammerer, G.1    Hunter, C.P.2    Rothman, J.H.3    Saari, G.C.4    Valls, A.5    Stevens, T.H.6
  • 21
    • 0026786755 scopus 로고
    • Cloning and characterization of a cysteine proteinase from Saccharomyces cerevisiae
    • Kambouris NG, Burke DJ Creutz CE (1992) Cloning and characterization of a cysteine proteinase from Saccharomyces cerevisiae. J Biol Chem 267, 21570 21576.
    • (1992) J Biol Chem , vol.267 , pp. 21570-21576
    • Kambouris, N.G.1    Burke, D.J.2    Creutz, C.E.3
  • 22
    • 0027499191 scopus 로고
    • BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian bleomycin hydrolase
    • Enenkel C Wolf DH (1993) BLH1 codes for a yeast thiol aminopeptidase, the equivalent of mammalian bleomycin hydrolase. J Biol Chem 268, 7036 7043.
    • (1993) J Biol Chem , vol.268 , pp. 7036-7043
    • Enenkel, C.1    Wolf, D.H.2
  • 23
    • 33644878272 scopus 로고    scopus 로고
    • Identification of yeast aspartyl aminopeptidase gene by purifying and characterizing its product from yeast cells
    • Yokoyama R, Kawasaki H Hirano H (2006) Identification of yeast aspartyl aminopeptidase gene by purifying and characterizing its product from yeast cells. FEBS Lett 273, 192 198.
    • (2006) FEBS Lett , vol.273 , pp. 192-198
    • Yokoyama, R.1    Kawasaki, H.2    Hirano, H.3
  • 24
    • 0033568252 scopus 로고    scopus 로고
    • Disruption of six novel ORFs on the left arm of chromosome XII reveals one gene essential for vegetative growth of Saccharomyces cerevisiae
    • Zhang N, Ismail T, Wu J, Woodwark KC, Gardner DC, Walmsley RM Oliver SG (1999) Disruption of six novel ORFs on the left arm of chromosome XII reveals one gene essential for vegetative growth of Saccharomyces cerevisiae. Yeast 15, 1287 1296.
    • (1999) Yeast , vol.15 , pp. 1287-1296
    • Zhang, N.1    Ismail, T.2    Wu, J.3    Woodwark, K.C.4    Gardner, D.C.5    Walmsley, R.M.6    Oliver, S.G.7
  • 26
    • 0030727185 scopus 로고    scopus 로고
    • Expression profiles of transcripts from 126 open reading frames in the entire chromosome VI of Saccharomyces cerevisiae by systematic northern analyses
    • Naitou M, Hagiwara H, Hanaoka F, Eki T Murakami Y (1997) Expression profiles of transcripts from 126 open reading frames in the entire chromosome VI of Saccharomyces cerevisiae by systematic northern analyses. Yeast 13, 1275 1290.
    • (1997) Yeast , vol.13 , pp. 1275-1290
    • Naitou, M.1    Hagiwara, H.2    Hanaoka, F.3    Eki, T.4    Murakami, Y.5
  • 27
    • 0033956060 scopus 로고    scopus 로고
    • The COG database: A tool for genome-scale analysis of protein functions and evolution
    • Tatukova RL, Galperin MY, Natale DA Koonin EV (2000) The COG database: a tool for genome-scale analysis of protein functions and evolution. Nucleic Acids Res 28, 33 36.
    • (2000) Nucleic Acids Res , vol.28 , pp. 33-36
    • Tatukova, R.L.1    Galperin, M.Y.2    Natale, D.A.3    Koonin, E.V.4
  • 29
    • 33846520786 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system regulates membrane fusion of yeast vacuoles
    • Kleijnen MF, Kirkpatrick DS Gygi SP (2007) The ubiquitin-proteasome system regulates membrane fusion of yeast vacuoles. EMBO J 26, 275 287.
    • (2007) EMBO J , vol.26 , pp. 275-287
    • Kleijnen, M.F.1    Kirkpatrick, D.S.2    Gygi, S.P.3
  • 30
    • 27744528392 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Npc2p is a functionally conserved homologue of the human Niemann-Pick disease type C2 protein, hNPC2
    • Berger AC, Vanderford TH, Gernert KM, Nichols JW, Faundez V Corbett AH (2005) Saccharomyces cerevisiae Npc2p is a functionally conserved homologue of the human Niemann-Pick disease type C2 protein, hNPC2. Eukaryotic Cell 4, 1851 1862.
    • (2005) Eukaryotic Cell , vol.4 , pp. 1851-1862
    • Berger, A.C.1    Vanderford, T.H.2    Gernert, K.M.3    Nichols, J.W.4    Faundez, V.5    Corbett, A.H.6
  • 31
    • 33846116102 scopus 로고    scopus 로고
    • The vacuolar transporter chaperone (VTC) is required for microautophagy
    • Uttenweiler A, Schwarz H, Neumann H Mayer A (2006) The vacuolar transporter chaperone (VTC) is required for microautophagy. Mol Biol Cell 18, 166 175.
    • (2006) Mol Biol Cell , vol.18 , pp. 166-175
    • Uttenweiler, A.1    Schwarz, H.2    Neumann, H.3    Mayer, A.4
  • 32
    • 0030008819 scopus 로고    scopus 로고
    • Deletion of the ATH1 gene in Saccharomyces cerevisiae prevents growth on trehalose
    • Nwaka S, Mechler B Holzer H (1996) Deletion of the ATH1 gene in Saccharomyces cerevisiae prevents growth on trehalose. FEBS Lett 386, 235 238.
    • (1996) FEBS Lett , vol.386 , pp. 235-238
    • Nwaka, S.1    Mechler, B.2    Holzer, H.3
  • 33
    • 0024447838 scopus 로고
    • Membrane protein sorting: Biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase
    • Klionsky DJ Emr SD (1989) Membrane protein sorting: biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase. EMBO J 8, 2241 2250.
    • (1989) EMBO J , vol.8 , pp. 2241-2250
    • Klionsky, D.J.1    Emr, S.D.2
  • 34
    • 0025804582 scopus 로고
    • Regulated import and degradation of a cytosolic protein in the yeast vacuole
    • Chiang H-L Schekman R (1991) Regulated import and degradation of a cytosolic protein in the yeast vacuole. Nature 350, 313 318.
    • (1991) Nature , vol.350 , pp. 313-318
    • Chiang, H.-L.1    Schekman, R.2
  • 36
    • 0032079372 scopus 로고    scopus 로고
    • Nonclassical protein sorting to the yeast vacuole
    • Klionsky DJ (1998) Nonclassical protein sorting to the yeast vacuole. J Biol Chem 273, 10807 10810.
    • (1998) J Biol Chem , vol.273 , pp. 10807-10810
    • Klionsky, D.J.1
  • 38
    • 1942469479 scopus 로고    scopus 로고
    • Ald6p is a preferred target for autophagy in yeast, Saccharomyces cerevisiae
    • Onodera J Ohsumi Y (2004) Ald6p is a preferred target for autophagy in yeast, Saccharomyces cerevisiae. J Biol Chem 279, 16071 16076.
    • (2004) J Biol Chem , vol.279 , pp. 16071-16076
    • Onodera, J.1    Ohsumi, Y.2
  • 39
    • 0037135973 scopus 로고    scopus 로고
    • The Vtc proteins in vacuole fusion: Coupling NSF activity to Vo trans-complex formation
    • Eitzen G, Wang L, Thirngren N Wickner W (2002) The Vtc proteins in vacuole fusion: coupling NSF activity to Vo trans-complex formation. J Cell Biol 158, 669 679.
    • (2002) J Cell Biol , vol.158 , pp. 669-679
    • Eitzen, G.1    Wang, L.2    Thirngren, N.3    Wickner, W.4
  • 40
    • 1942453869 scopus 로고    scopus 로고
    • The GTPase-activating enzyme Gyp1p is required for recycling of internalized membrane material by inactivation of the Rab/Ypt GTPase Ypt1p
    • Lafourcade C, Galan J-M, Gloor Y, Haguenauer-Tsapis R Peter M (2004) The GTPase-activating enzyme Gyp1p is required for recycling of internalized membrane material by inactivation of the Rab/Ypt GTPase Ypt1p. Mol Cel Biol 24, 3815 3826.
    • (2004) Mol Cel Biol , vol.24 , pp. 3815-3826
    • Lafourcade, C.1    Galan, J.-M.2    Gloor, Y.3    Haguenauer-Tsapis, R.4    Peter, M.5
  • 42
    • 20544432791 scopus 로고    scopus 로고
    • Cell wall integrity signaling in Saccharomyces cerevisiae
    • Levin DE (2005) Cell wall integrity signaling in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 69, 262 291.
    • (2005) Microbiol Mol Biol Rev , vol.69 , pp. 262-291
    • Levin, D.E.1
  • 44
    • 0034602377 scopus 로고    scopus 로고
    • Targeting of aminopeptidase I to the yeast vacuole is mediated by Ssa1p, a cytosolic member of the 70-kDa stress protein family
    • Silles E, Mazon MJ, Gevaert K, Goethals M, Vandekerckhove J, Leber R Sandoval IV (2000) Targeting of aminopeptidase I to the yeast vacuole is mediated by Ssa1p, a cytosolic member of the 70-kDa stress protein family. J Biol Chem 275, 34054 34059.
    • (2000) J Biol Chem , vol.275 , pp. 34054-34059
    • Silles, E.1    Mazon, M.J.2    Gevaert, K.3    Goethals, M.4    Vandekerckhove, J.5    Leber, R.6    Sandoval, I.V.7
  • 46
    • 0027940215 scopus 로고
    • Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments
    • Hahne K, Haucke V Schatz G (1994) Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments. Cell 79, 829 839.
    • (1994) Cell , vol.79 , pp. 829-839
    • Hahne, K.1    Haucke, V.2    Schatz, G.3
  • 47
    • 0024501822 scopus 로고
    • Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae
    • Chang YH Smith JA (1989) Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae. J Biol Chem 264, 6979 6983.
    • (1989) J Biol Chem , vol.264 , pp. 6979-6983
    • Chang, Y.H.1    Smith, J.A.2
  • 48
    • 0028308218 scopus 로고
    • Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae. Purification, properties, localization, and processing by protease B
    • Yasuhara T, Nakai T Ohashi A (1994) Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae. Purification, properties, localization, and processing by protease B. J Biol Chem 269, 13644 13650.
    • (1994) J Biol Chem , vol.269 , pp. 13644-13650
    • Yasuhara, T.1    Nakai, T.2    Ohashi, A.3
  • 49
    • 0028304451 scopus 로고
    • Molecular cloning of the aminopeptidase Y gene of Saccharomyces cerevisiae. Sequence analysis and gene disruption of a new aminopeptidase
    • Nishizawa M, Yasuhara T, Nakai T, Fujiki Y Ohashi A (1994) Molecular cloning of the aminopeptidase Y gene of Saccharomyces cerevisiae. Sequence analysis and gene disruption of a new aminopeptidase. J Biol Chem 269, 13651 13655.
    • (1994) J Biol Chem , vol.269 , pp. 13651-13655
    • Nishizawa, M.1    Yasuhara, T.2    Nakai, T.3    Fujiki, Y.4    Ohashi, A.5
  • 50
    • 0026317974 scopus 로고
    • Activation of the proteinase B precursor of the yeast Saccharomyces cerevisiae by autocatalysis and by an internal sequence
    • Nebes VL Jones EW (1991) Activation of the proteinase B precursor of the yeast Saccharomyces cerevisiae by autocatalysis and by an internal sequence. J Biol Chem 266, 22851 22857.
    • (1991) J Biol Chem , vol.266 , pp. 22851-22857
    • Nebes, V.L.1    Jones, E.W.2
  • 51
  • 52
    • 0017842062 scopus 로고
    • Biosynthesis of the vacuolar yeast glycoprotein carboxypeptidase Y. Conversion of precursor into the enzyme
    • Hasilik A Tanner W (1978) Biosynthesis of the vacuolar yeast glycoprotein carboxypeptidase Y. Conversion of precursor into the enzyme. Eur J Biochem 85, 599 608.
    • (1978) Eur J Biochem , vol.85 , pp. 599-608
    • Hasilik, A.1    Tanner, W.2
  • 53
    • 0023652379 scopus 로고
    • Protein sorting in yeast: The localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide
    • Valls LA, Hunter CP, Rothman JH Stevens TH (1987) Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide. Cell 48, 887 897.
    • (1987) Cell , vol.48 , pp. 887-897
    • Valls, L.A.1    Hunter, C.P.2    Rothman, J.H.3    Stevens, T.H.4
  • 55
    • 0024006019 scopus 로고
    • Intracellular sorting and processing of a yeast vacuolar hydrolase: Proteinase a propeptide contains vacuolar targeting information
    • Klionsky DJ, Banta LM Emr SD (1988) Intracellular sorting and processing of a yeast vacuolar hydrolase: proteinase A propeptide contains vacuolar targeting information. Mol Cell Biol 8, 2105 2116.
    • (1988) Mol Cell Biol , vol.8 , pp. 2105-2116
    • Klionsky, D.J.1    Banta, L.M.2    Emr, S.D.3
  • 56
    • 0027220822 scopus 로고
    • The propeptide is required for in vivo formation of stable active yeast proteinase a and can function even when not covalently linked to the mature region
    • van den Hazel HB, Kielland-Brandt MC Winther JR (1993) The propeptide is required for in vivo formation of stable active yeast proteinase A and can function even when not covalently linked to the mature region. J Biol Chem 268, 18002 18007.
    • (1993) J Biol Chem , vol.268 , pp. 18002-18007
    • Van Den Hazel, H.B.1    Kielland-Brandt, M.C.2    Winther, J.R.3
  • 57
    • 0028916486 scopus 로고
    • Random substitution of large parts of the propeptide of yeast proteinase a
    • van den Hazel HB, Kielland-Brandt MC Winther JR (1995) Random substitution of large parts of the propeptide of yeast proteinase A. J Biol Chem 270, 8602 8609.
    • (1995) J Biol Chem , vol.270 , pp. 8602-8609
    • Van Den Hazel, H.B.1    Kielland-Brandt, M.C.2    Winther, J.R.3
  • 58
    • 0003603451 scopus 로고    scopus 로고
    • CSIRO Publishing, Collingwood, Australia.
    • De DN (2000) Plant Cell Vacuoles. CSIRO Publishing, Collingwood, Australia.
    • (2000) Plant Cell Vacuoles.
    • De, D.N.1
  • 59
    • 0032894143 scopus 로고    scopus 로고
    • What do proteins need to reach different vacuoles?
    • Vitale A Raikhel NV (1999) What do proteins need to reach different vacuoles? Trends Plant Sci 4, 149 155.
    • (1999) Trends Plant Sci , vol.4 , pp. 149-155
    • Vitale, A.1    Raikhel, N.V.2
  • 60
    • 0023739386 scopus 로고
    • Protein sorting in Saccharomyces cerevisiae: Isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
    • Robinson JS, Klionsky DJ, Banta LM Emr SD (1988) Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol Cell Biol 8, 4936 4948.
    • (1988) Mol Cell Biol , vol.8 , pp. 4936-4948
    • Robinson, J.S.1    Klionsky, D.J.2    Banta, L.M.3    Emr, S.D.4
  • 61
    • 0028064872 scopus 로고
    • A yeast metal resistance protein similar to human cystic fibrosis transmembrane conductance regulator (CFTR) and multidrug resistance-associated protein
    • Szczypka MS, Wemmie JA, Moye-Rowley WS Thiele DJ (1994) A yeast metal resistance protein similar to human cystic fibrosis transmembrane conductance regulator (CFTR) and multidrug resistance-associated protein. J Biol Chem 269, 22853 22857.
    • (1994) J Biol Chem , vol.269 , pp. 22853-22857
    • Szczypka, M.S.1    Wemmie, J.A.2    Moye-Rowley, W.S.3    Thiele, D.J.4
  • 62
    • 0000964662 scopus 로고
    • Bimane fluorescent labels: Labeling of normal human red cells under physiological conditions
    • Kosower NS, Kosower EM, Newton GL Ranney HM (1979) Bimane fluorescent labels: labeling of normal human red cells under physiological conditions. Proc Natl Acad Sci USA 76, 3382 3386.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 3382-3386
    • Kosower, N.S.1    Kosower, E.M.2    Newton, G.L.3    Ranney, H.M.4
  • 63
    • 32244436993 scopus 로고    scopus 로고
    • Dynamics of Arabidopsis thaliana soluble proteome in response to different nutrient culture conditions
    • Sarry J-E, Kuhn L, LeLay P, Garin J Bourguignon J (2006) Dynamics of Arabidopsis thaliana soluble proteome in response to different nutrient culture conditions. Electrophoresis 27, 495 507.
    • (2006) Electrophoresis , vol.27 , pp. 495-507
    • Sarry, J.-E.1    Kuhn, L.2    Lelay, P.3    Garin, J.4    Bourguignon, J.5
  • 64
    • 31344479864 scopus 로고    scopus 로고
    • Rapid protein identification using direct infusion nanoelectrospray ionization mass spectrometry
    • Chen S (2006) Rapid protein identification using direct infusion nanoelectrospray ionization mass spectrometry. Proteomics 6, 16 25.
    • (2006) Proteomics , vol.6 , pp. 16-25
    • Chen, S.1
  • 65
    • 33645094371 scopus 로고    scopus 로고
    • Cassava root proteome: Protein identification and differential expression
    • Sheffield J, Taylor N, Fauquet C Chen S (2006) Cassava root proteome: protein identification and differential expression. Proteomics 6, 1588 1598.
    • (2006) Proteomics , vol.6 , pp. 1588-1598
    • Sheffield, J.1    Taylor, N.2    Fauquet, C.3    Chen, S.4
  • 66
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.