메뉴 건너뛰기




Volumn 14, Issue 1, 1998, Pages 87-96

The chloroplast small heat shock protein - Purification and characterization of pea recombinant protein

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; BETA PROTEIN; CHLOROPLAST; CIRCULAR DICHROISM SPECTROSCOPY; CRYSTALLOGRAPHY; HEAT SHOCK PROTEIN; HEAT TOLERANCE; ION EXCHANGE CHROMATOGRAPHY; ISOELECTRIC POINT; LENS; OLIGOMER; PLANT DEVELOPMENT; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; RECOMBINANT PROTEIN; STRESS; WESTERN BLOTTING;

EID: 0344222184     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1998.0921     Document Type: Article
Times cited : (11)

References (60)
  • 2
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters E. R., Lee G. J., Vierling E. Evolution, structure and function of the small heat shock proteins in plants. J. Exp. Bot. 47:1996;325-338.
    • (1996) J. Exp. Bot. , vol.47 , pp. 325-338
    • Waters, E.R.1    Lee, G.J.2    Vierling, E.3
  • 3
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Palo Alto: Annual Reviews. p. 437-496
    • Parsell D. A., Lindquist S. The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins. Annual Review of Genetics. 1993;Annual Reviews, Palo Alto. p. 437-496.
    • (1993) Annual Review of Genetics
    • Parsell, D.A.1    Lindquist, S.2
  • 4
    • 0001082038 scopus 로고
    • Accumulation of heat shock proteins in field-grown cottonGossypium hirsutum.
    • Burke J. J., Hatfield J. L., Klein R. R., Mullet J. E. Accumulation of heat shock proteins in field-grown cottonGossypium hirsutum. Plant Physiol. 78:1985;394-398.
    • (1985) Plant Physiol. , vol.78 , pp. 394-398
    • Burke, J.J.1    Hatfield, J.L.2    Klein, R.R.3    Mullet, J.E.4
  • 5
    • 0000602720 scopus 로고
    • Presence of heat shock messenger RNA species in field grown soybeansGlycine max.
    • Kimpel J. A., Key J. L. Presence of heat shock messenger RNA species in field grown soybeansGlycine max. Plant Physiol. 79:1985;672-678.
    • (1985) Plant Physiol. , vol.79 , pp. 672-678
    • Kimpel, J.A.1    Key, J.L.2
  • 7
    • 0027417852 scopus 로고
    • Induction of chinesemhamster Hsp27 gene expression in mouse cells confers resistance to heat shock Hsp27 stabilization of the microfilament organization
    • Lavoie J. N., Gingras Breton G., Tanguay R. M., Landry J. Induction of chinesemhamster Hsp27 gene expression in mouse cells confers resistance to heat shock Hsp27 stabilization of the microfilament organization. J. Biol. Chem. 268:1993;3420-3429.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3420-3429
    • Lavoie, J.N.1    Gingras Breton, G.2    Tanguay, R.M.3    Landry, J.4
  • 9
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob U., Gaestel M., Engel K., Buchner J. Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268:1993;1517-1520.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 10
    • 0028949832 scopus 로고
    • Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea
    • Lee G. J., Pokala N., Vierling E. Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea. J. Biol. Chem. 270:1995;10432-10438.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10432-10438
    • Lee, G.J.1    Pokala, N.2    Vierling, E.3
  • 11
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M., Graeber S., Gaestel M., Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16:1997;221-229.
    • (1997) EMBO J. , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graeber, S.2    Gaestel, M.3    Buchner, J.4
  • 12
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee G. J., Roseman A. M., Saibil H. R., Vierling E. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16:1997;659-671.
    • (1997) EMBO J. , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 13
    • 0023975891 scopus 로고
    • A heat shock protein localized to chloroplasts is a member of a eukaryotic superfamily of heat shock proteins
    • Vierling E., Nagao R. T., Derocher A. E., Harris L. M. A heat shock protein localized to chloroplasts is a member of a eukaryotic superfamily of heat shock proteins. EMBO J. 7:1988;575-582.
    • (1988) EMBO J. , vol.7 , pp. 575-582
    • Vierling, E.1    Nagao, R.T.2    Derocher, A.E.3    Harris, L.M.4
  • 14
    • 0025764158 scopus 로고
    • Analysis of conserved domains identifies a unique structural feature of a chloroplast heat shock protein
    • Chen Q., Vierling E. Analysis of conserved domains identifies a unique structural feature of a chloroplast heat shock protein. Mol. Gen. Genet. 226:1991;425-431.
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 425-431
    • Chen, Q.1    Vierling, E.2
  • 15
    • 0001480444 scopus 로고
    • Synthesis transport and localization of a nuclear coded 22-kilodalton heat-shock proteini in the chloroplast membranes of peas andChlamydomonas reinhardi.
    • Kloppstech K., Meyer G., Schuster G., Ohad I. Synthesis transport and localization of a nuclear coded 22-kilodalton heat-shock proteini in the chloroplast membranes of peas andChlamydomonas reinhardi. EMBO J. 4:1985;1901-1910.
    • (1985) EMBO J. , vol.4 , pp. 1901-1910
    • Kloppstech, K.1    Meyer, G.2    Schuster, G.3    Ohad, I.4
  • 16
    • 0024276145 scopus 로고
    • Temperature-dependent binding to the thylakoid membranes of nuclear-coded chloroplast heat-shock proteins
    • Glaczinski H., Kloppstech K. Temperature-dependent binding to the thylakoid membranes of nuclear-coded chloroplast heat-shock proteins. Eur. J. Biochem. 173:1988;579-584.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 579-584
    • Glaczinski, H.1    Kloppstech, K.2
  • 17
    • 0025796650 scopus 로고
    • Evidence for the localization of the nuclear-coded 22-kDa heat-shock protein in a subfraction of thylakoid membranes
    • Adamska I., Kloppstech K. Evidence for the localization of the nuclear-coded 22-kDa heat-shock protein in a subfraction of thylakoid membranes. Eur. J. Biochem. 198:1991;375-382.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 375-382
    • Adamska, I.1    Kloppstech, K.2
  • 18
    • 0025302387 scopus 로고
    • Accumulation stability and localization of a major chloroplast heat-shock protein
    • Chen Q., Lauzon L. M., Derocher A. E., Vierling E. Accumulation stability and localization of a major chloroplast heat-shock protein. J. Cell Biol. 110:1990;1873-1884.
    • (1990) J. Cell Biol. , vol.110 , pp. 1873-1884
    • Chen, Q.1    Lauzon, L.M.2    Derocher, A.E.3    Vierling, E.4
  • 19
    • 0028233236 scopus 로고
    • A 21-kDa chloroplast heat shock protein assembles into high molecular weight complexes in vivo and in organelle
    • Chen Q., Osteryoung K., Vierling E. A 21-kDa chloroplast heat shock protein assembles into high molecular weight complexes in vivo and in organelle. J. Biol. Chem. 269:1994;13216-13223.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13216-13223
    • Chen, Q.1    Osteryoung, K.2    Vierling, E.3
  • 20
    • 0028113521 scopus 로고
    • Dynamics of small heat shock protein distribution within the chloroplasts of higher plants
    • Osteryoung K. W., Vierling E. Dynamics of small heat shock protein distribution within the chloroplasts of higher plants. J. Biol. Chem. 269:1994;28676-28682.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28676-28682
    • Osteryoung, K.W.1    Vierling, E.2
  • 22
    • 0028280702 scopus 로고
    • Close packing of an oligomeric eye lens beta-crystallin induces loss of symmetry and ordering of sequence extensions
    • Nalini V., Bax B., Driessen H., Moss D. S., Lindley P. F., Slingsby C. Close packing of an oligomeric eye lens beta-crystallin induces loss of symmetry and ordering of sequence extensions. J. Mol. Biol. 236:1994;1250-1258.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1250-1258
    • Nalini, V.1    Bax, B.2    Driessen, H.3    Moss, D.S.4    Lindley, P.F.5    Slingsby, C.6
  • 23
    • 0021106995 scopus 로고
    • Structural homology of lens crystallins. 3. Secondary structure estimation from circular dichroism and prediction from amino-acid sequences
    • Siezen R. J., Argos P. Structural homology of lens crystallins. 3. Secondary structure estimation from circular dichroism and prediction from amino-acid sequences. Biochim. Biophys. Acta. 748:1983;56-67.
    • (1983) Biochim. Biophys. Acta , vol.748 , pp. 56-67
    • Siezen, R.J.1    Argos, P.2
  • 24
    • 0019995966 scopus 로고
    • Spectroscopic investigations of bovine lens crystallins. 1. Circular dichroism and intrinsic fluorescence
    • Liang J. N., Chakrabarti B. Spectroscopic investigations of bovine lens crystallins. 1. Circular dichroism and intrinsic fluorescence. Biochemistry. 21:1982;1847-1852.
    • (1982) Biochemistry , vol.21 , pp. 1847-1852
    • Liang, J.N.1    Chakrabarti, B.2
  • 25
    • 0027230161 scopus 로고
    • Estimation of the secondary structure and conformation of bovine lens crystallins by infrared spectroscopy quantitative analysis and resolution by Fourier self-deconvolution and curve fit
    • Lamba O. P., Borchman D., Sinha S. K., Shah J., Renugopalakrishnan V., Yappert M. C. Estimation of the secondary structure and conformation of bovine lens crystallins by infrared spectroscopy quantitative analysis and resolution by Fourier self-deconvolution and curve fit. Biochim. Biophys. Acta. 1163:1993;113-123.
    • (1993) Biochim. Biophys. Acta , vol.1163 , pp. 113-123
    • Lamba, O.P.1    Borchman, D.2    Sinha, S.K.3    Shah, J.4    Renugopalakrishnan, V.5    Yappert, M.C.6
  • 26
    • 0032013798 scopus 로고    scopus 로고
    • The chloroplast small heat shock protein is a non-phosphorylated homo-oligomer
    • Suzuki T. C., Krawitz D. C., Vierling E. The chloroplast small heat shock protein is a non-phosphorylated homo-oligomer. Plant Physiol. 116:1998;1151-1161.
    • (1998) Plant Physiol. , vol.116 , pp. 1151-1161
    • Suzuki, T.C.1    Krawitz, D.C.2    Vierling, E.3
  • 27
    • 0027995077 scopus 로고
    • PJC20 and pJC40: Two high-copy-number vectors for T7 RNA polymerase-dependent expression of recombinant genes inEscherichia coli.
    • Clos J., Brandau S. PJC20 and pJC40: Two high-copy-number vectors for T7 RNA polymerase-dependent expression of recombinant genes inEscherichia coli. Protein Express. Purif. 5:1994;133-137.
    • (1994) Protein Express. Purif. , vol.5 , pp. 133-137
    • Clos, J.1    Brandau, S.2
  • 28
    • 0023042283 scopus 로고
    • Use of bacteriophage T-7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F. W., Moffatt B. A. Use of bacteriophage T-7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:1986;113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 30
    • 0025283867 scopus 로고
    • Use of T7 RNA polymerase to direct expression of cloned genes
    • D. Goeddel. San Diego: Academic Press
    • Studier F. W., Rosenberg A. H., Dunn J. J., Dubendorff J. W. Use of T7 RNA polymerase to direct expression of cloned genes. Goeddel D. Methods in Enzymology. 1990;60-89 Academic Press, San Diego.
    • (1990) Methods in Enzymology , pp. 60-89
    • Studier, F.W.1    Rosenberg, A.H.2    Dunn, J.J.3    Dubendorff, J.W.4
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Analy. Biochem. 72:1976;248-254.
    • (1976) Analy. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0001656151 scopus 로고
    • The identification of a heat-shock protein complex in chloroplasts of barley leaves
    • Clarke A. K., Critchley C. The identification of a heat-shock protein complex in chloroplasts of barley leaves. Plant Physiol. 100:1992;2081-2089.
    • (1992) Plant Physiol. , vol.100 , pp. 2081-2089
    • Clarke, A.K.1    Critchley, C.2
  • 37
    • 0018781995 scopus 로고
    • Electrophoretic analysis of the unfolding of proteins by urea
    • Creighton T. E. Electrophoretic analysis of the unfolding of proteins by urea. J. Mol. Biol. 129:1979;235-264.
    • (1979) J. Mol. Biol. , vol.129 , pp. 235-264
    • Creighton, T.E.1
  • 38
    • 0001680919 scopus 로고
    • A reassessment of the use of herbicide binding to measure photosystem II reaction centers in plant thylakoids
    • Chow W. S., Hope A. B., Anderson J. M. A reassessment of the use of herbicide binding to measure photosystem II reaction centers in plant thylakoids. Photosynthesis Res. 24:1990;109-113.
    • (1990) Photosynthesis Res. , vol.24 , pp. 109-113
    • Chow, W.S.1    Hope, A.B.2    Anderson, J.M.3
  • 39
    • 0017701604 scopus 로고
    • Automatic identification of secondary structure in globular proteins
    • Levitt M., Greer J. Automatic identification of secondary structure in globular proteins. J. Mol. Biol. 114:1977;181-240.
    • (1977) J. Mol. Biol. , vol.114 , pp. 181-240
    • Levitt, M.1    Greer, J.2
  • 40
    • 0019871893 scopus 로고
    • Information content in the circular dichroism of proteins
    • Hennessey J. P. J., Johnson W. C. J. Information content in the circular dichroism of proteins. Biochemistry. 20:1981;1085-1094.
    • (1981) Biochemistry , vol.20 , pp. 1085-1094
    • Hennessey, J.P.J.1    Johnson, W.C.J.2
  • 41
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure pattern recognition of hydrogen bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure pattern recognition of hydrogen bonded and geometrical features. Biopolymers. 22:1983;2577-2638.
    • (1983) Biopolymers , vol.22 , pp. 2577-2638
    • Kabsch, W.1    Sander, C.2
  • 42
    • 0022555881 scopus 로고
    • Detection of folding intermediates using urea gradient electrophoresis
    • C.H.W. Hirs, & S.N. Timasheff. New York: Academic Press
    • Creighton T. E. Detection of folding intermediates using urea gradient electrophoresis. Hirs C. H.W., Timasheff S. N. Methods of Enzymology. 1986;156-172 Academic Press, New York.
    • (1986) Methods of Enzymology , pp. 156-172
    • Creighton, T.E.1
  • 43
    • 0020474627 scopus 로고
    • Effect on protein stability of reversing the charge on amino groups
    • Hollecker M., Creighton T. E. Effect on protein stability of reversing the charge on amino groups. Biochim. Biophys. Acta. 701:1982;395-404.
    • (1982) Biochim. Biophys. Acta , vol.701 , pp. 395-404
    • Hollecker, M.1    Creighton, T.E.2
  • 44
    • 0028127827 scopus 로고
    • Roles of molecular chaperones in protein folding
    • Ellis R. J. Roles of molecular chaperones in protein folding. Curr. Opin. Struct. Biol. 4:1994;117-122.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 117-122
    • Ellis, R.J.1
  • 45
    • 0029566336 scopus 로고
    • The role of molecular chaperones in protein folding
    • Hendrick J. P., Hartl F. U. The role of molecular chaperones in protein folding. FASEB J. 9:1995;1559-1569.
    • (1995) FASEB J. , vol.9 , pp. 1559-1569
    • Hendrick, J.P.1    Hartl, F.U.2
  • 46
    • 0030042460 scopus 로고    scopus 로고
    • Protein folding in the cell: Competing models of chaperonin function
    • Ellis R. J., Hartl F. U. Protein folding in the cell: Competing models of chaperonin function. FASEB J. 10:1996;20-26.
    • (1996) FASEB J. , vol.10 , pp. 20-26
    • Ellis, R.J.1    Hartl, F.U.2
  • 47
    • 0030750584 scopus 로고    scopus 로고
    • In vivo observation of polypeptide flux through the bacterial chaperonin system
    • Ewalt K. L., Hendrick J. P., Houry W. A., Hartl F. U. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell. 90:1997;491-500.
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewalt, K.L.1    Hendrick, J.P.2    Houry, W.A.3    Hartl, F.U.4
  • 48
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • Becker J., Craig E. A. Heat-shock proteins as molecular chaperones. Eur. J. Biochem. 219:1994;11-23.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 11-23
    • Becker, J.1    Craig, E.A.2
  • 49
    • 0029980091 scopus 로고    scopus 로고
    • Principles of chaperone-assisted protein folding: Differences betweenin vitroin vivo
    • Frydman J., Hartl F. U. Principles of chaperone-assisted protein folding: Differences betweenin vitroin vivo. Science. 272:1996;1497-1502.
    • (1996) Science , vol.272 , pp. 1497-1502
    • Frydman, J.1    Hartl, F.U.2
  • 50
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The hip-hop connection
    • Frydman J., Hohfeld J. Chaperones get in touch: The hip-hop connection. Trends Biochem. Sci. 22:1997;87-92.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 87-92
    • Frydman, J.1    Hohfeld, J.2
  • 51
    • 0031029286 scopus 로고    scopus 로고
    • Characterization of functional domains of the eukaryotic co-chaperone hip
    • Irmer H. I., Hoehfeld J. Characterization of functional domains of the eukaryotic co-chaperone hip. J. Biol. Chem. 272:1997;2230-2235.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2230-2235
    • Irmer, H.I.1    Hoehfeld, J.2
  • 52
    • 0028023344 scopus 로고
    • Structure and modifications of the junior chaperon alpha-crystallin: From lens transparency to molecular pathology
    • Groenen P. J. T. A., Merck K. B., De Jong W. W., Bloemendal H. Structure and modifications of the junior chaperon alpha-crystallin: From lens transparency to molecular pathology. Eur. J. Biochem. 225:1994;1-19.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 1-19
    • Groenen, P.J.T.A.1    Merck, K.B.2    De Jong, W.W.3    Bloemendal, H.4
  • 53
    • 0026483279 scopus 로고
    • Alpha crystallin can function as a molecular chaperone
    • Horwitz J. Alpha crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA. 89:1992;10449-10453.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 54
    • 0030826325 scopus 로고    scopus 로고
    • Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides
    • Leroux M. R., Melki R., Gordon B., Batelier G., Candido E. P. M. Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides. J. Biol. Chem. 272:1997;24646-24656.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24646-24656
    • Leroux, M.R.1    Melki, R.2    Gordon, B.3    Batelier, G.4    Candido, E.P.M.5
  • 56
    • 0025100372 scopus 로고
    • Threonine 204 of the chaperone protein HSC70 influences the structure of the active site but is not essential for ATP hydrolysis
    • Flaherty K. M., De Luca-Flaherty C., McKay D. B. Threonine 204 of the chaperone protein HSC70 influences the structure of the active site but is not essential for ATP hydrolysis. Nature. 346:1990;623.
    • (1990) Nature , vol.346 , pp. 623
    • Flaherty, K.M.1    De Luca-Flaherty, C.2    McKay, D.B.3
  • 58
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison C. J., Hayer Hartl M., Di Liberto M., Hartl F. U., Kuriyan J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science. 276:1997;431-435.
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer Hartl, M.2    Di Liberto, M.3    Hartl, F.U.4    Kuriyan, J.5
  • 59
    • 0030901877 scopus 로고    scopus 로고
    • A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone
    • Prodromou C., Roe S. M., Piper P. W., Pearl L. H. A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nature Struct. Biol. 4:1997;477-482.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 477-482
    • Prodromou, C.1    Roe, S.M.2    Piper, P.W.3    Pearl, L.H.4
  • 60
    • 0023723196 scopus 로고
    • Oligopeptide biases in protein sequences and their use in predicting protein coding regions in nucleotide sequences
    • McCaldon P., Argos P. Oligopeptide biases in protein sequences and their use in predicting protein coding regions in nucleotide sequences. Proteins-Struct.-Funct.-Genet. 4:1988;99-122.
    • (1988) Proteins-Struct.-Funct.-Genet. , vol.4 , pp. 99-122
    • McCaldon, P.1    Argos, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.