메뉴 건너뛰기




Volumn 132, Issue 6, 1996, Pages 999-1010

Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMINOPEPTIDASE; CYTOSOL AMINOPEPTIDASE; PEPTIDE; PROTEINASE; SIGNAL PEPTIDE;

EID: 0029916949     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.132.6.999     Document Type: Article
Times cited : (80)

References (58)
  • 1
    • 0018073585 scopus 로고
    • Identification of tubulin from the yeast Saccharomyces cerevisiae
    • Baum, P., J. Thorner, and L. Honig. 1978. Identification of tubulin from the yeast Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA. 75:4962-4966.
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 4962-4966
    • Baum, P.1    Thorner, J.2    Honig, L.3
  • 2
    • 0029088909 scopus 로고
    • The cytoplasmic tail domain of the vacuolar protein sorting receptor vps10p and a subset of vps gene products regulate receptor stability, function, and localization
    • Cereghino, J.L., E.G. Marcusson, and S.D. Emr. 1995 The cytoplasmic tail domain of the vacuolar protein sorting receptor vps10p and a subset of vps gene products regulate receptor stability, function, and localization. Mol. Biol. Cell 6:1089-1102.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1089-1102
    • Cereghino, J.L.1    Marcusson, E.G.2    Emr, S.D.3
  • 3
    • 0024501822 scopus 로고
    • Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae
    • Chang, Y.H., and J.A. Smith. 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
  • 4
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou, P.Y., and G.D. Fasman. 1974. Prediction of protein conformation. Biochemistry. 13.222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 5
    • 0024788273 scopus 로고
    • Yeast vacuolar aminopeptidase yscI. Isolation and regulation of the APE1 (LAP4) structural gene
    • Cueva, R., N. Garcia-Alvarez, and P. Suarez-Rendueles. 1989. Yeast vacuolar aminopeptidase yscI. Isolation and regulation of the APE1 (LAP4) structural gene. FEBS Lett. 259:125-129.
    • (1989) FEBS Lett. , vol.259 , pp. 125-129
    • Cueva, R.1    Garcia-Alvarez, N.2    Suarez-Rendueles, P.3
  • 6
    • 0023567026 scopus 로고
    • A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum
    • Deshaies, R.J., and R. Schekman 1987 A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum. J. Cell Biol. 105:633-645.
    • (1987) J. Cell Biol. , vol.105 , pp. 633-645
    • Deshaies, R.J.1    Schekman, R.2
  • 7
    • 0026711129 scopus 로고
    • Multiple mutant of Escherichia coli synthesizing virtually thymineless DNA during limited growth
    • el-Hajj, H.H., L. Wang, and B. Weiss. 1992. Multiple mutant of Escherichia coli synthesizing virtually thymineless DNA during limited growth. J. Bacteriol. 174:4450-4456.
    • (1992) J. Bacteriol. , vol.174 , pp. 4450-4456
    • El-Hajj, H.H.1    Wang, L.2    Weiss, B.3
  • 8
    • 0018183217 scopus 로고
    • Subcellular localization and levels of aminopeplidases and dipeptidase in Saccharomyces cerevisiae
    • Frey, J., and K.H. Rohm. 1978. Subcellular localization and levels of aminopeplidases and dipeptidase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 527:31-41.
    • (1978) Biochim. Biophys. Acta , vol.527 , pp. 31-41
    • Frey, J.1    Rohm, K.H.2
  • 9
    • 0025994140 scopus 로고
    • Guide to yeast genetics and molecular biology
    • J.N. Abelson and M.I. Simon, editors. Academic Press, Inc., NY
    • Guthrie, C., and G.R. Fink. 1991. Guide to yeast genetics and molecular biology. In Methods in Enzymology. Vol. 194. J.N. Abelson and M.I. Simon, editors. Academic Press, Inc., NY. 863 pp.
    • (1991) Methods in Enzymology , vol.194
    • Guthrie, C.1    Fink, G.R.2
  • 10
    • 0028800171 scopus 로고
    • Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway
    • Harding, T.M., K.A. Morano, S.V. Scott, and D.J. Klionsky. 1995. Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway. J Cell Biol. 131:591-602.
    • (1995) J Cell Biol. , vol.131 , pp. 591-602
    • Harding, T.M.1    Morano, K.A.2    Scott, S.V.3    Klionsky, D.J.4
  • 11
    • 0026724078 scopus 로고
    • Biogenesis of the yeast vacuole (lysosome). Proteinase yscB contributes molecularly and kinetically to vacuolar hydrolase-precursor maturation
    • Hirsch, H.H., H.H. Schiffer, and D.H. Wolf. 1992. Biogenesis of the yeast vacuole (lysosome). Proteinase yscB contributes molecularly and kinetically to vacuolar hydrolase-precursor maturation. Eur. J. Biochem. 207:867-876.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 867-876
    • Hirsch, H.H.1    Schiffer, H.H.2    Wolf, D.H.3
  • 12
    • 0023652394 scopus 로고
    • Distinct sequence determinants direct intracellular sorting and modification of a yeast vacuolar protease
    • Johnson, L.M., V.A. Bankaitis, and S.D. Emr. 1987. Distinct sequence determinants direct intracellular sorting and modification of a yeast vacuolar protease. Cell. 48:875-885
    • (1987) Cell , vol.48 , pp. 875-885
    • Johnson, L.M.1    Bankaitis, V.A.2    Emr, S.D.3
  • 13
    • 0025170681 scopus 로고
    • The fungal vacuole: Composition, function, and biogenesis
    • Klionsky, D.J , P.K Herman, and S.D. Emr. 1990. The fungal vacuole: composition, function, and biogenesis Microbiol. Rev. 54:266-292.
    • (1990) Microbiol. Rev. , vol.54 , pp. 266-292
    • Klionsky, D.J.1    Herman, P.K.2    Emr, S.D.3
  • 14
    • 0026640551 scopus 로고
    • Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway
    • Klionsky, D.J., R. Cueva, and D.S. Yaver. 1992. Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway J. Cell Biol. 119:287-299.
    • (1992) J. Cell Biol. , vol.119 , pp. 287-299
    • Klionsky, D.J.1    Cueva, R.2    Yaver, D.S.3
  • 15
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl Acad. Sci. USA. 82:488-492
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 16
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., J.D Roberts, and R.A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154: 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0025643362 scopus 로고
    • A general method for rapid site-directed mutagenesis using the polymerase chain reaction
    • Landt, O., H.P Grunert, and U. Hahn. 1990. A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene. 96:125-128.
    • (1990) Gene. , vol.96 , pp. 125-128
    • Landt, O.1    Grunert, H.P.2    Hahn, U.3
  • 19
    • 0024358184 scopus 로고
    • Identification and characterization of a nuclear localization sequence-binding protein in yeast
    • Lee, W.C., and T. Melese. 1989. Identification and characterization of a nuclear localization sequence-binding protein in yeast. Proc. Natl. Acad. Sci. USA. 86:8808-8812.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8808-8812
    • Lee, W.C.1    Melese, T.2
  • 20
    • 0025906753 scopus 로고
    • The NSRI gene encodes a protein that specifically binds nuclear localization sequences and has two RNA recognition motifs
    • Lee, W.C., Z.X. Xue, and T. Melese. 1991. The NSRI gene encodes a protein that specifically binds nuclear localization sequences and has two RNA recognition motifs. J. Cell Biol. 113:1-12.
    • (1991) J. Cell Biol. , vol.113 , pp. 1-12
    • Lee, W.C.1    Xue, Z.X.2    Melese, T.3
  • 22
    • 0025289981 scopus 로고
    • The ERD2 gene determines the specificity of the luminal ER protein retention system
    • Lewis, M.J., D J. Sweet, and H.R. Pelham 1990. The ERD2 gene determines the specificity of the luminal ER protein retention system. Cell. 61 1359-1363.
    • (1990) Cell , vol.61 , pp. 1359-1363
    • Lewis, M.J.1    Sweet, D.J.2    Pelham, H.R.3
  • 23
    • 0018471274 scopus 로고
    • Comparative studies on the dodecameric and hexameric forms of yeast aminopeptidase I
    • Loffler, H.G., and K.H. Rohm. 1979. Comparative studies on the dodecameric and hexameric forms of yeast aminopeptidase I. Z. Naturforsch. 34C:381-386.
    • (1979) Z. Naturforsch. , vol.34 C , pp. 381-386
    • Loffler, H.G.1    Rohm, K.H.2
  • 24
    • 0026657841 scopus 로고
    • MP11, an essential gene encoding a mitochondrial membrane protein, is possibly involved in protein import into yeast mitochondria
    • Maarse, A.C., J. Blom, L.A Grivell, and M. Meijer. 1992. MP11, an essential gene encoding a mitochondrial membrane protein, is possibly involved in protein import into yeast mitochondria. EMBO (Eur. Mol. Biol. Organ.) J. 11:3619-3628.
    • (1992) EMBO (Eur. Mol. Biol. Organ.) J. , vol.11 , pp. 3619-3628
    • Maarse, A.C.1    Blom, J.2    Grivell, L.A.3    Meijer, M.4
  • 25
    • 0027324927 scopus 로고
    • An efficient 1-tube PCR method for internal site-directed mutagenesis of large amplified molecules
    • Marini, F , 3d, A. Naeem, and J.N. Lapeyre. 1993. An efficient 1-tube PCR method for internal site-directed mutagenesis of large amplified molecules. Nucleic Acids Res 21:2277-2278.
    • (1993) Nucleic Acids Res , vol.21 , pp. 2277-2278
    • Marini III, F.1    Naeem, A.2    Lapeyre, J.N.3
  • 26
    • 0028332917 scopus 로고
    • The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene
    • Marcusson, E.G., B.F. Horazdovsky, JL Cereghino, E. Gharakhanian, and S.D. Emr. 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
  • 27
    • 0027168271 scopus 로고
    • The pas8 mutant of Pichia pastoris exhibits the peroxisomal protein import deficiencies of Zellweger syndrome cells - The PAS8 protein binds to the COOH-terminal tripeptide peroxisomal targeting signal, and is a member of the TPR protein family
    • McCollum, D., E. Monosov, and S. Subramani. 1993. The pas8 mutant of Pichia pastoris exhibits the peroxisomal protein import deficiencies of Zellweger syndrome cells - the PAS8 protein binds to the COOH-terminal tripeptide peroxisomal targeting signal, and is a member of the TPR protein family. J. Cell Biol 121:761-774.
    • (1993) J. Cell Biol , vol.121 , pp. 761-774
    • McCollum, D.1    Monosov, E.2    Subramani, S.3
  • 28
    • 0028033934 scopus 로고
    • An oligomeric protein is imported into peroxisomes in vivo
    • McNew, J.A , and J M. Goodman. 1994. An oligomeric protein is imported into peroxisomes in vivo J Cell Biol. 127:1245-1257.
    • (1994) J Cell Biol. , vol.127 , pp. 1245-1257
    • McNew, J.A.1    Goodman, J.M.2
  • 29
    • 0027293043 scopus 로고
    • The signal anchor sequence of mitochondrial Mas70p contains an oligomerization domain
    • Millar, D G., and G.C. Shore. 1993. The signal anchor sequence of mitochondrial Mas70p contains an oligomerization domain. J. Biol. Chem. 268:18403-18406.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18403-18406
    • Millar, D.G.1    Shore, G.C.2
  • 30
    • 0028234557 scopus 로고
    • Mitochondrial Mas70p signal anchor sequence. Mutations in the transmembrane domain that disrupt dimerization but not targeting or membrane insertion
    • Millar, D.G., and G.C. Shore. 1994. Mitochondrial Mas70p signal anchor sequence. Mutations in the transmembrane domain that disrupt dimerization but not targeting or membrane insertion. J. Biol. Chem. 269:12229-12232.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12229-12232
    • Millar, D.G.1    Shore, G.C.2
  • 31
    • 0026501752 scopus 로고
    • A rapid method for localized mutagenesis of yeast genes
    • Muhlrad, D., R. Hunter, and R. Parker. 1992. A rapid method for localized mutagenesis of yeast genes Yeast 8:79-82.
    • (1992) Yeast , vol.8 , pp. 79-82
    • Muhlrad, D.1    Hunter, R.2    Parker, R.3
  • 32
    • 0028283489 scopus 로고
    • Sorting of membrane proteins in the yeast secretory pathway
    • Nothwehr, S.F., and T.H. Stevens. 1994. Sorting of membrane proteins in the yeast secretory pathway. J Biol. Chem 269:10185-10188
    • (1994) J Biol. Chem , vol.269 , pp. 10185-10188
    • Nothwehr, S.F.1    Stevens, T.H.2
  • 35
    • 0025604836 scopus 로고
    • Site-specific mutagenesis using asymmetric polymerase chain reaction and a single mutant primer
    • Perrin, S., and G. Gilliland. 1990. Site-specific mutagenesis using asymmetric polymerase chain reaction and a single mutant primer. Nucleic Acids Res. 18: 7433-7438.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 7433-7438
    • Perrin, S.1    Gilliland, G.2
  • 37
    • 0027455339 scopus 로고
    • end3 and end4: Two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae
    • Raths, S., J. Rohrer, F. Crausaz, and H. Riezman. 1993. end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae. J. Cell Biol. 120:55-65.
    • (1993) J. Cell Biol. , vol.120 , pp. 55-65
    • Raths, S.1    Rohrer, J.2    Crausaz, F.3    Riezman, H.4
  • 38
    • 0027199241 scopus 로고
    • Yeast Endocytosis
    • Riezman, H. 1993. Yeast Endocytosis. Trends Cell Biol. 3:273-277.
    • (1993) Trends Cell Biol. , vol.3 , pp. 273-277
    • Riezman, H.1
  • 39
    • 0023739386 scopus 로고
    • Protein sorting in Saccharomyces cerevisiae: Isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
    • Robinson, J.S., D.J. Klionsky, L.M. Banta, and S.D. Emr. 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
  • 41
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarkar, G., and S.S. Sommer. 1990. The "megaprimer" method of site-directed mutagenesis. Biotechniques. 8:404-107.
    • (1990) Biotechniques , vol.8 , pp. 404-1107
    • Sarkar, G.1    Sommer, S.S.2
  • 42
    • 0029558544 scopus 로고
    • In vitro reconstitution of the cytoplasm to vacuole protein targeting pathway in yeast
    • Scott, S V , and D.J. Klionsky. 1995 In vitro reconstitution of the cytoplasm to vacuole protein targeting pathway in yeast. J. Cell Biol. 131:1727-1736.
    • (1995) J. Cell Biol. , vol.131 , pp. 1727-1736
    • Scott, S.V.1    Klionsky, D.J.2
  • 43
    • 0026584008 scopus 로고
    • Autophagy and other vacuolar protein degradation mechanisms
    • Seglen, P.O., and P. Bohley. 1992. Autophagy and other vacuolar protein degradation mechanisms. Experientia. 48:158-172.
    • (1992) Experientia , vol.48 , pp. 158-172
    • Seglen, P.O.1    Bohley, P.2
  • 45
    • 0028949981 scopus 로고
    • Folding mediated by an intramolecular chaperone: Autoprocessing pathway of the precursor resolved via a substrate assisted catalysis mechanism
    • Shinde, U., and M. Inouye. 1995 Folding mediated by an intramolecular chaperone: autoprocessing pathway of the precursor resolved via a substrate assisted catalysis mechanism. J. Mol. Biol. 247:390-395.
    • (1995) J. Mol. Biol. , vol.247 , pp. 390-395
    • Shinde, U.1    Inouye, M.2
  • 46
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 47
    • 0024425004 scopus 로고
    • The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo
    • Silen, J.L., and D.A. Agard. 1989. The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo. Nature (Lond.). 341:462-464.
    • (1989) Nature (Lond.) , vol.341 , pp. 462-464
    • Silen, J.L.1    Agard, D.A.2
  • 48
    • 0024432012 scopus 로고
    • Yeast proteins that recognize nuclear localization sequences
    • Silver, P., I. Sadler, and M.A. Osborne. 1989. Yeast proteins that recognize nuclear localization sequences. J. Cell Biol. 109:983-989.
    • (1989) J. Cell Biol. , vol.109 , pp. 983-989
    • Silver, P.1    Sadler, I.2    Osborne, M.A.3
  • 49
    • 0027639720 scopus 로고
    • Genetic and biochemical studies of protein sorting to the yeast vacuole
    • Stack, J.H., and S.D. Emr. 1993. Genetic and biochemical studies of protein sorting to the yeast vacuole. Curr. Opin. Cell Biol. 5:641-646.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 641-646
    • Stack, J.H.1    Emr, S.D.2
  • 50
    • 0029087571 scopus 로고
    • The Pichia pasturis peroxisomal protein PAS8p is the receptor for the C-terminal tripeptide peroxisomal targeting signal
    • Terlecky, S.R., W.M. Nuttley, D. McCollum, E. Sock, and S. Subramani. 1995. The Pichia pasturis peroxisomal protein PAS8p is the receptor for the C-terminal tripeptide peroxisomal targeting signal. EMBO (Eur. Mol. Biol. Organ.) J. 14:3627-3634.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 3627-3634
    • Terlecky, S.R.1    Nuttley, W.M.2    McCollum, D.3    Sock, E.4    Subramani, S.5
  • 52
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • Tsukada, M., and Y. Ohsumi. 1993. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett. 333:169-174.
    • (1993) FEBS Lett. , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 53
    • 0023652379 scopus 로고
    • Protein sorting in yeast: The localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide
    • Valls, L.A., C.P. Hunter, J.H. Rothman, and T.H. Stevens. 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
  • 54
    • 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, H.B., M.C. Kielland-Brandt, and J.R. Winther. 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
  • 55
    • 0026004831 scopus 로고
    • Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity
    • Winther, J.R., and P. Sorensen. 1991. Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity. Proc. Natl. Acad. Sci. USA. 88:9330-9334.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9330-9334
    • Winther, J.R.1    Sorensen, P.2
  • 56
    • 0028068376 scopus 로고
    • Refolding of a carboxypeptidase Y folding intermediate in vitro by low-affinity binding of the proregion
    • Winther, J R., P. Sorensen, and M.C. Kielland-Brandt. 1994. Refolding of a carboxypeptidase Y folding intermediate in vitro by low-affinity binding of the proregion. J. Biol. Chem. 269:22007-22013.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22007-22013
    • Winther, J.R.1    Sorensen, P.2    Kielland-Brandt, M.C.3
  • 57
    • 0025696339 scopus 로고
    • A novel pathway of import of α-mannosidase, a marker enzyme of vacuolar membrane, in Saccharomyces cerevisiae
    • Yoshihisa, T., and Y. Anraku. 1990. A novel pathway of import of α-mannosidase, a marker enzyme of vacuolar membrane, in Saccharomyces cerevisiae. J. Biol. Chem. 265:22418-22425.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22418-22425
    • Yoshihisa, T.1    Anraku, Y.2
  • 58
    • 0024409494 scopus 로고
    • Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process
    • Zhu, X.L., Y. Ohta, F. Jordan, and M. Inouye. 1989. Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process. Nature (Lond.). 339:483-484.
    • (1989) Nature (Lond.) , vol.339 , pp. 483-484
    • Zhu, X.L.1    Ohta, Y.2    Jordan, F.3    Inouye, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.