메뉴 건너뛰기




Volumn 379, Issue 3, 1998, Pages 301-309

Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein folding

Author keywords

Chaperonin; GroEl; Hsp60; Hsp70; Mitochondrial protein import; Protein folding in vivo

Indexed keywords

CHAPERONE; CHAPERONIN; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; LUCIFERASE; POLYPEPTIDE; PROTEIN; SIGNAL PEPTIDE;

EID: 0031896846     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1998.379.3.301     Document Type: Article
Times cited : (31)

References (53)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C.B. (1973). Principles that govern the folding of protein chains. Science 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0030598919 scopus 로고    scopus 로고
    • Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding
    • Buchberger, A., Schröder, H., Hesterkamp, T., Schönfeld, H.-J., and Bukau, B. (1996). Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J. Mol. Biol. 261, 328-333.
    • (1996) J. Mol. Biol. , vol.261 , pp. 328-333
    • Buchberger, A.1    Schröder, H.2    Hesterkamp, T.3    Schönfeld, H.-J.4    Bukau, B.5
  • 4
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis, J. (1987). Proteins as molecular chaperones. Nature 328, 378-379.
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 5
    • 0027925677 scopus 로고
    • The general concept of molecular chaperones
    • Ellis, R.J. (1993). The general concept of molecular chaperones. Philos. Trans. R. Soc. Lond. Biol. 339, 257-261.
    • (1993) Philos. Trans. R. Soc. Lond. Biol. , vol.339 , pp. 257-261
    • Ellis, R.J.1
  • 6
    • 0030042460 scopus 로고    scopus 로고
    • Protein folding in the cell: Competing models of chaperonin function
    • Ellis, R.J., and Hartl, F.U. (1996). Protein folding in the cell: Competing models of chaperonin function. FASEB J. 10, 20-26.
    • (1996) FASEB J. , vol.10 , pp. 20-26
    • Ellis, R.J.1    Hartl, F.U.2
  • 7
    • 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., and Hartl, F.U. (1997). In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 90, 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
  • 8
    • 0029980091 scopus 로고    scopus 로고
    • Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
    • Frydman, J., and Hartl, F.U. (1996). Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms. Science 272, 1497-1502.
    • (1996) Science , vol.272 , pp. 1497-1502
    • Frydman, J.1    Hartl, F.U.2
  • 9
    • 0027077442 scopus 로고
    • Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
    • Frydman, J., Nimmesgern, E., Erdjument-Bromage, H., Wall, J.S., Tempst, P., and Hartl, F.U. (1992). Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J. 11, 4767-4778.
    • (1992) EMBO J. , vol.11 , pp. 4767-4778
    • Frydman, J.1    Nimmesgern, E.2    Erdjument-Bromage, H.3    Wall, J.S.4    Tempst, P.5    Hartl, F.U.6
  • 10
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman, J., Nimmesgern, E., Ohtsuka, K., and Hartl, F.U. (1994). Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370, 111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.U.4
  • 12
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos, C., and Welch, W.J. (1993). Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9, 601-634.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 13
  • 14
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 15
    • 0023663892 scopus 로고
    • Successive translocation into and out of the mitochondrial matrix: Targeting of proteins to the intermembrane space by a bipartite signal peptide
    • Hartl, F.U., Ostermann, J., Guiard, B., and Neupert, W. (1987). Successive translocation into and out of the mitochondrial matrix: Targeting of proteins to the intermembrane space by a bipartite signal peptide. Cell 51, 1027-1037.
    • (1987) Cell , vol.51 , pp. 1027-1037
    • Hartl, F.U.1    Ostermann, J.2    Guiard, B.3    Neupert, W.4
  • 16
    • 0029858706 scopus 로고    scopus 로고
    • Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis
    • Hayer-Hartl, M.K., Weber, F., and Hartl, F.U. (1996). Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. EMBO J. 15, 6111-6121.
    • (1996) EMBO J. , vol.15 , pp. 6111-6121
    • Hayer-Hartl, M.K.1    Weber, F.2    Hartl, F.U.3
  • 17
    • 0027425585 scopus 로고
    • Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides
    • Hendrick, J.P., Langer, T., Davis, T.A., Hartl, F.U., and Wiedmann, M. (1993). Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proc. Natl. Acad. Sci. USA 90, 10216-10220.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10216-10220
    • Hendrick, J.P.1    Langer, T.2    Davis, T.A.3    Hartl, F.U.4    Wiedmann, M.5
  • 18
    • 0028022670 scopus 로고
    • Post-translational protein import and folding
    • Höhfeld, J., and Hartl, F.U. (1994a). Post-translational protein import and folding. Current Op. Cell Biol. 6, 499-509.
    • (1994) Current Op. Cell Biol. , vol.6 , pp. 499-509
    • Höhfeld, J.1    Hartl, F.U.2
  • 19
    • 0028234368 scopus 로고
    • Role of the chaperonin cofactor HsplO in protein folding and sorting in yeast mitochondria
    • Höhfeld, J., and Hartl, F.U. (1994b). Role of the chaperonin cofactor HsplO in protein folding and sorting in yeast mitochondria. J. Cell Biol. 126, 305-315.
    • (1994) J. Cell Biol. , vol.126 , pp. 305-315
    • Höhfeld, J.1    Hartl, F.U.2
  • 20
    • 0028064780 scopus 로고
    • Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES
    • Kandror, O., Busconi, L., Sherman, M., and Goldberg, A.L. (1994). Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES. J. Biol. Chem. 269, 23575-23582.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23575-23582
    • Kandror, O.1    Busconi, L.2    Sherman, M.3    Goldberg, A.L.4
  • 21
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang, P.J., Ostermann, J., Shilling, J., Neupert, W., Craig, E.A., and Pfanner, N. (1990). Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature 348, 137-143.
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.J.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 22
    • 0027988581 scopus 로고
    • Chaperone-dependent folding and activation of ribosome-bound nascent rhodanese. Analysis by fluorescence
    • Kudlicki, W., Odom, O.W., Kramer, G., and Hardesty, B. (1994). Chaperone-dependent folding and activation of ribosome-bound nascent rhodanese. Analysis by fluorescence. J. Mol. Biol. 244, 319-331.
    • (1994) J. Mol. Biol. , vol.244 , pp. 319-331
    • Kudlicki, W.1    Odom, O.W.2    Kramer, G.3    Hardesty, B.4
  • 23
    • 7844224374 scopus 로고    scopus 로고
    • R.J. Ellis, ed., (San Diego, USA: Academic Press Inc.)
    • Langer, T., and Neupert, W. (1996). In: Chaperonins, R.J. Ellis, ed., (San Diego, USA: Academic Press Inc.), pp. 91-106.
    • (1996) Chaperonins , pp. 91-106
    • Langer, T.1    Neupert, W.2
  • 24
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M.K., and Hartl, F.U. (1992). Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356, 683-689.
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 25
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C., and Zylicz, M. (1991). Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. USA 88, 2874-2878.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 26
    • 0026070260 scopus 로고
    • Sequential action of mitochondrial chaperones in protein import into the matrix
    • Manning-Krieg, U.C., Scherer, P.E., and Schatz, G. (1991). Sequential action of mitochondrial chaperones in protein import into the matrix. EMBO J. 10, 3273-3280.
    • (1991) EMBO J. , vol.10 , pp. 3273-3280
    • Manning-Krieg, U.C.1    Scherer, P.E.2    Schatz, G.3
  • 27
    • 0031030690 scopus 로고    scopus 로고
    • The effect of macromolecular crowding on chaperonin-mediated protein folding
    • Martin, J. and Hartl, F.U. (1997). The effect of macromolecular crowding on chaperonin-mediated protein folding. Proc. Natl. Acad. Sci. USA 94, 1107-1112.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1107-1112
    • Martin, J.1    Hartl, F.U.2
  • 28
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
    • Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A.L., and Hartl, F.U. (1991) Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 352, 36-42.
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Horwich, A.L.5    Hartl, F.U.6
  • 29
    • 0026446343 scopus 로고
    • Prevention of protein denaturation under heat stress by the chaperonin Hsp60
    • Martin, J., Horwich, A.L., and Hartl, F.U. (1992). Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Science 258, 995-998.
    • (1992) Science , vol.258 , pp. 995-998
    • Martin, J.1    Horwich, A.L.2    Hartl, F.U.3
  • 30
    • 0027427326 scopus 로고
    • The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
    • Martin, J., Mayhew, M., Langer, T., and Hartl, F.U. (1993). The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature 366, 228-233.
    • (1993) Nature , vol.366 , pp. 228-233
    • Martin, J.1    Mayhew, M.2    Langer, T.3    Hartl, F.U.4
  • 32
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert, W. (1997). Protein import into mitochondria. A. Rev. Biochemistry 66, 863-917.
    • (1997) A. Rev. Biochemistry , vol.66 , pp. 863-917
    • Neupert, W.1
  • 33
    • 0027424461 scopus 로고
    • ATP-dependent protein refolding activity in reticulocyte lysate. Evidence for the participation of different chaperone components
    • Nimmesgern, E., and Hartl, F.U. (1993). ATP-dependent protein refolding activity in reticulocyte lysate. Evidence for the participation of different chaperone components. FEBS Lett. 331, 25-30.
    • (1993) FEBS Lett. , vol.331 , pp. 25-30
    • Nimmesgern, E.1    Hartl, F.U.2
  • 34
    • 0024458504 scopus 로고
    • Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
    • Ostermann, J., Horwich, A.L., Neupert, W., and Hartl, F.-U. (1989). Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature 341, 125-130.
    • (1989) Nature , vol.341 , pp. 125-130
    • Ostermann, J.1    Horwich, A.L.2    Neupert, W.3    Hartl, F.-U.4
  • 36
    • 0030040712 scopus 로고    scopus 로고
    • Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation
    • Pripbuus, C., Westermann, B., Schmitt, M., Langer, T., Neupert, W., and Schwarz, E. (1996). Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation. FEBS Lett. 380, 142-146.
    • (1996) FEBS Lett. , vol.380 , pp. 142-146
    • Pripbuus, C.1    Westermann, B.2    Schmitt, M.3    Langer, T.4    Neupert, W.5    Schwarz, E.6
  • 37
    • 0028948314 scopus 로고
    • Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60
    • Rassow, J., Mohrs, K., Koidl, S., Barthelmess, I.B., Pfanner, N., and Tropschug, M. (1995a). Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60. Mol. Cell. Biol. 15, 2654-2662.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2654-2662
    • Rassow, J.1    Mohrs, K.2    Koidl, S.3    Barthelmess, I.B.4    Pfanner, N.5    Tropschug, M.6
  • 38
    • 0028965273 scopus 로고
    • Partner proteins determine multiple functions of Hsp70
    • Rassow, J., Voos, W., and Pfanner, N. (1995b). Partner proteins determine multiple functions of Hsp70. Trends Cell Biol. 5, 207-212.
    • (1995) Trends Cell Biol. , vol.5 , pp. 207-212
    • Rassow, J.1    Voos, W.2    Pfanner, N.3
  • 39
    • 0028282446 scopus 로고
    • Fusion proteins containing the cytochrome b2 presequence are sorted to the mitochondrial intermembrane space independently of hsp60
    • Rospert, S., Muller, S., Schatz, G., and Glick, B.S. (1994). Fusion proteins containing the cytochrome b2 presequence are sorted to the mitochondrial intermembrane space independently of hsp60. J. Biol. Chem. 269, 17279-17288.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17279-17288
    • Rospert, S.1    Muller, S.2    Schatz, G.3    Glick, B.S.4
  • 40
  • 41
    • 0028284879 scopus 로고
    • Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
    • Rowley, N., Prip, B.C., Westermann, B., Brown, C., Schwarz, E., Barrell, B., and Neupert, W. (1994). Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77, 249-259.
    • (1994) Cell , vol.77 , pp. 249-259
    • Rowley, N.1    Prip, B.C.2    Westermann, B.3    Brown, C.4    Schwarz, E.5    Barrell, B.6    Neupert, W.7
  • 42
    • 0027427986 scopus 로고
    • DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schröder, H., Langer, T., Hartl, F.U., and Bukau, B. (1993). DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12, 4137-4144.
    • (1993) EMBO J. , vol.12 , pp. 4137-4144
    • Schröder, H.1    Langer, T.2    Hartl, F.U.3    Bukau, B.4
  • 43
    • 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 Hieter, P. (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
  • 44
    • 0027958293 scopus 로고
    • Mitochondrial molecular chaperones: Their role in protein translocation
    • Stuart, R., Cyr, D.M., Craig, E.A., and Neupert, W. (1994). Mitochondrial molecular chaperones: their role in protein translocation. Trends in Biochem. Sci. 19, 87-92.
    • (1994) Trends in Biochem. Sci. , vol.19 , pp. 87-92
    • Stuart, R.1    Cyr, D.M.2    Craig, E.A.3    Neupert, W.4
  • 45
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE
    • Szabo, A., Langer, T., Schroder, H., Flanagan, J., Bukau, B., and Hartl, F.U. (1994). The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc. Natl. Acad. Sci. USA 91, 10345-10349.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10345-10349
    • Szabo, A.1    Langer, T.2    Schroder, H.3    Flanagan, J.4    Bukau, B.5    Hartl, F.U.6
  • 46
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
    • Todd, M.J., Viitanen, P.V., and Lorimer, G.H. (1994). Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science 265, 659-666.
    • (1994) Science , vol.265 , pp. 659-666
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 47
    • 0030006212 scopus 로고    scopus 로고
    • Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism
    • Todd, M.J., Lorimer, G.H., and Thirumalai, D. (1996). Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism. Proc. Natl. Acad. Sci. USA 93, 4030-4035.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4030-4035
    • Todd, M.J.1    Lorimer, G.H.2    Thirumalai, D.3
  • 48
    • 0020338406 scopus 로고
    • The imported preprotein of the proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa: Molecular cloning and sequencing of them RNA
    • Viebrock, A., Perz and Sebald, W. (1982). The imported preprotein of the proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa: Molecular cloning and sequencing of them RNA. EMBO J. 1, 565-571.
    • (1982) EMBO J. , vol.1 , pp. 565-571
    • Viebrock, A.1    Perz2    Sebald, W.3
  • 49
    • 0027946910 scopus 로고
    • Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria
    • Wagner, I., Arit, H., van Dyck, L., Langer, T., and Neupert, W. (1994). Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J. 13, 5135-5145.
    • (1994) EMBO J. , vol.13 , pp. 5135-5145
    • Wagner, I.1    Arit, H.2    Van Dyck, L.3    Langer, T.4    Neupert, W.5
  • 50
    • 0027933369 scopus 로고
    • GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
    • Weissman, J.S., Kashi, Y., Fenton, W.A., and Horwich, A.L. (1994). GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell 78, 693-702.
    • (1994) Cell , vol.78 , pp. 693-702
    • Weissman, J.S.1    Kashi, Y.2    Fenton, W.A.3    Horwich, A.L.4
  • 51
    • 0030056969 scopus 로고    scopus 로고
    • Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
    • Weissman, J.S., Rye, H.S., Fenton, W.A., Beechem, J.M., and Horwich, A.L. (1996). Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 84, 481-490.
    • (1996) Cell , vol.84 , pp. 481-490
    • Weissman, J.S.1    Rye, H.S.2    Fenton, W.A.3    Beechem, J.M.4    Horwich, A.L.5
  • 52
    • 0029020451 scopus 로고
    • The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria
    • Westermann, B., Pripbuus, C., Neupert, W., and Schwarz, E. (1995) The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria. EMBO J. 14, 3452-3460.
    • (1995) EMBO J. , vol.14 , pp. 3452-3460
    • Westermann, B.1    Pripbuus, C.2    Neupert, W.3    Schwarz, E.4
  • 53
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmermann, S.B., and Minton, A.P. (1993). Macromolecular crowding: Biochemical, biophysical, and physiological consequences. A. Rev. Biophys. Biomol. Struct. 22, 27-65.
    • (1993) A. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmermann, S.B.1    Minton, A.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.