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Volumn 71, Issue 4, 1996, Pages 2213-2221

Chaperonins GroEL and GroES: Views from atomic force microscopy

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONIN; HEAT SHOCK PROTEIN;

EID: 0029836392     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79422-5     Document Type: Article
Times cited : (75)

References (64)
  • 1
    • 0028169935 scopus 로고
    • Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer
    • Azem, A., M. Kessel, and P. Goloubinoff. 1994. Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer. Science. 265:653-656.
    • (1994) Science , vol.265 , pp. 653-656
    • Azem, A.1    Kessel, M.2    Goloubinoff, P.3
  • 2
    • 0029664944 scopus 로고    scopus 로고
    • The 2.4A crystal structure of the bacterial chaperonin GroEL complexed with ATPγS
    • Boisvert, D. C., J. Wang, Z. Otwinowski, A. L. Horwich, and P. B. Sigler. 1996. The 2.4A crystal structure of the bacterial chaperonin GroEL complexed with ATPγS. Nat. Struct. Biol. 3:170-177.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 170-177
    • Boisvert, D.C.1    Wang, J.2    Otwinowski, Z.3    Horwich, A.L.4    Sigler, P.B.5
  • 4
    • 0022981315 scopus 로고
    • Purification and properties of the GroES morphogenetic protein of Escherichia coli
    • Chandrasekhar, G. N., K. Tilley, C. Woolford, R. Hendrix, and C. Georgopoulos. 1986. Purification and properties of the GroES morphogenetic protein of Escherichia coli. J. Biol. Chem. 261:12414-12419.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12414-12419
    • Chandrasekhar, G.N.1    Tilley, K.2    Woolford, C.3    Hendrix, R.4    Georgopoulos, C.5
  • 5
    • 0028027055 scopus 로고
    • Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy
    • Chen, S., A. M. Roseman, A. S. Hunter, S. P. Wood, S. G. Burson, N. A. Ran.son, A. R. Clarke, and H. R. Saibil. 1994. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature. 371:261-264.
    • (1994) Nature , vol.371 , pp. 261-264
    • Chen, S.1    Roseman, A.M.2    Hunter, A.S.3    Wood, S.P.4    Burson, S.G.5    Ran.son, N.A.6    Clarke, A.R.7    Saibil, H.R.8
  • 7
    • 0024554107 scopus 로고
    • The GroES and GroEL heat shock gene products of E. coli are essential for bacterial growth at all temperatures
    • Fayet, O., T. Ziegelhoffer, and C. Georgopoulos, 1989. The GroES and GroEL heat shock gene products of E. coli are essential for bacterial growth at all temperatures. J. Bacteriol. 171:1379-1385.
    • (1989) J. Bacteriol. , vol.171 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.3
  • 8
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes beta actin folding
    • Gao, Y., J. O. Thomas, R. L. Chow, G. H. Lee, and N. J. Cowan. 1992. A cytoplasmic chaperonin that catalyzes beta actin folding. Cell. 69:1043-1050.
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 10
    • 0025995773 scopus 로고
    • Refolding of barnase in the presence of GroE
    • Gray, T. E., and A. R. Fersht. 1991. Refolding of barnase in the presence of GroE. FEBS Lett. 292:254-258.
    • (1991) FEBS Lett. , vol.292 , pp. 254-258
    • Gray, T.E.1    Fersht, A.R.2
  • 11
    • 0028364295 scopus 로고
    • Biomolecular imaging with the atomic force microscope
    • Hansma, H. G., and J. Hoh. 1994. Biomolecular imaging with the atomic force microscope. Annu. Rev. Biophys. Biomol. Struct. 23:115-128.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 115-128
    • Hansma, H.G.1    Hoh, J.2
  • 13
    • 0028559575 scopus 로고
    • Transmission electron microscopy of GroEL, GroES, and the symmetrical GroEL/ES complex
    • Harris, J. R., A. Pluckthun, and R. Zahn. 1994. Transmission electron microscopy of GroEL, GroES, and the symmetrical GroEL/ES complex. J. Struct. Biol. 112:216-230.
    • (1994) J. Struct. Biol. , vol.112 , pp. 216-230
    • Harris, J.R.1    Pluckthun, A.2    Zahn, R.3
  • 14
    • 0018791204 scopus 로고
    • Purification and properties of GroE, a host protein involved in bacteriophage assembly
    • Hendrix, R. 1979. Purification and properties of GroE, a host protein involved in bacteriophage assembly. J. Mol. Biol. 129:375-392.
    • (1979) J. Mol. Biol. , vol.129 , pp. 375-392
    • Hendrix, R.1
  • 16
    • 0027184721 scopus 로고
    • Molecular chaperone function of heat shock proteins
    • Hendrick, J. P., and F. U. Hartl. 1993. Molecular chaperone function of heat shock proteins. Annu. Rev. Biochem. 62:349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 17
    • 0026095474 scopus 로고
    • Atomic force microscopy and dissection of gap junctions
    • Hoh, J., R. Lal, S. A. John, J.-P. Revel, and M. F. Arnsdorf. 1991. Atomic force microscopy and dissection of gap junctions. Science. 253:1405-1408.
    • (1991) Science , vol.253 , pp. 1405-1408
    • Hoh, J.1    Lal, R.2    John, S.A.3    Revel, J.-P.4    Arnsdorf, M.F.5
  • 18
    • 0018791259 scopus 로고
    • Isolation and characterization of the host protein GroE involved in bacteriophage lambda assembly
    • Hohn, T., B. Hohn, A. Engel, M. Wurtz, and P. R. Smith. 1979. Isolation and characterization of the host protein GroE involved in bacteriophage lambda assembly. J. Mol. Biol. 129:359-373.
    • (1979) J. Mol. Biol. , vol.129 , pp. 359-373
    • Hohn, T.1    Hohn, B.2    Engel, A.3    Wurtz, M.4    Smith, P.R.5
  • 19
    • 0024396544 scopus 로고
    • Identification and electron microscopic analysis of a chaperonin oligomer from Neurospora crassa mitochodria
    • Hutchinson, E. G., W. Tichelaar, G. Hofhaus, H. Weiss, and K. Leonard. 1989. Identification and electron microscopic analysis of a chaperonin oligomer from Neurospora crassa mitochodria. EMBO J. 8:1485-1490.
    • (1989) EMBO J. , vol.8 , pp. 1485-1490
    • Hutchinson, E.G.1    Tichelaar, W.2    Hofhaus, G.3    Weiss, H.4    Leonard, K.5
  • 20
    • 0030067634 scopus 로고    scopus 로고
    • The crystal structure of the GroES co-chaperonin at 2.8A resolution
    • Hunt, J. F., A. J. Weaver, S. Landry, L. Gierasch, and J. Deisenhofer. 1996. The crystal structure of the GroES co-chaperonin at 2.8A resolution. Nature. 379:37-45.
    • (1996) Nature , vol.379 , pp. 37-45
    • Hunt, J.F.1    Weaver, A.J.2    Landry, S.3    Gierasch, L.4    Deisenhofer, J.5
  • 22
    • 0027419011 scopus 로고
    • Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for teh mechanism of assisted folding
    • Jackson, G., R. A. Stainforth, D. J. Halsall, T. Atkinson, J. J. Holbrook, A. R. Clarke, and S. G. Burson. 1993. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for teh mechanism of assisted folding. Biochemistry. 32:2554-2563.
    • (1993) Biochemistry , vol.32 , pp. 2554-2563
    • Jackson, G.1    Stainforth, R.A.2    Halsall, D.J.3    Atkinson, T.4    Holbrook, J.J.5    Clarke, A.R.6    Burson, S.G.7
  • 23
    • 0029088986 scopus 로고
    • The role of ATP hydrolysis in the function of chaperonin GroEL: Dynamic complex formation with GroES
    • Kawata, Y., K. Hongo, K. Nosaka, Y. Furutsu, T. Mizobata, and J. Nagai. 1995. The role of ATP hydrolysis in the function of chaperonin GroEL: dynamic complex formation with GroES. FEBS Lett. 369:283-286.
    • (1995) FEBS Lett. , vol.369 , pp. 283-286
    • Kawata, Y.1    Hongo, K.2    Nosaka, K.3    Furutsu, Y.4    Mizobata, T.5    Nagai, J.6
  • 24
    • 0028157680 scopus 로고
    • Biological applications of atomic force microscopy
    • Lal, R. and S. A. John. 1994. Biological applications of atomic force microscopy. Am. J. Physiol. 266:C1-23.
    • (1994) Am. J. Physiol. , vol.266
    • Lal, R.1    John, S.A.2
  • 25
    • 0028228564 scopus 로고
    • Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding
    • Landry, S. J. and L. M. Gierasch. 1994. Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding. Annu. Rev, Biophys. Biomol. Struct. 23:645-669.
    • (1994) Annu. Rev, Biophys. Biomol. Struct. , vol.23 , pp. 645-669
    • Landry, S.J.1    Gierasch, L.M.2
  • 27
    • 0027092285 scopus 로고
    • Chaperonin mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity
    • Langer, T., G. Pfeifer, J. Martin, W. Baumeister, and F. U. Hartl. 1992. Chaperonin mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO J. 11:4757-4765.
    • (1992) EMBO J. , vol.11 , pp. 4757-4765
    • Langer, T.1    Pfeifer, G.2    Martin, J.3    Baumeister, W.4    Hartl, F.U.5
  • 28
    • 0028340341 scopus 로고
    • The formation of symmetrical GroEL-GroES complexes in the presence of ATP
    • Llorca, O., S. Marco, J. L. Carrascosa, and J. M. Valpuesta. 1994. The formation of symmetrical GroEL-GroES complexes in the presence of ATP. FEBS Lett. 345:181-186.
    • (1994) FEBS Lett. , vol.345 , pp. 181-186
    • Llorca, O.1    Marco, S.2    Carrascosa, J.L.3    Valpuesta, J.M.4
  • 29
    • 0028774727 scopus 로고
    • GroEL structure: A new chapter on assisted folding
    • Lorimer, G. H., 1994. GroEL structure: a new chapter on assisted folding. Structure. 2:1125-1128.
    • (1994) Structure , vol.2 , pp. 1125-1128
    • Lorimer, G.H.1
  • 31
    • 0030031059 scopus 로고    scopus 로고
    • Structure of the heat shock protein chaperonin 10 of Mycobacterium leprae
    • Mande, S. C., V. Mehra, B. R. Bloom, and W. G. J. Hol. 1996. Structure of the heat shock protein chaperonin 10 of Mycobacterium leprae. Science. 271:203-207.
    • (1996) Science , vol.271 , pp. 203-207
    • Mande, S.C.1    Mehra, V.2    Bloom, B.R.3    Hol, W.G.J.4
  • 32
    • 0030043488 scopus 로고    scopus 로고
    • Lord of the rings: GroES structure
    • Mayhew, M., and F. U. Hartl. 1996. Lord of the rings: GroES structure. Science. 271:161-162.
    • (1996) Science , vol.271 , pp. 161-162
    • Mayhew, M.1    Hartl, F.U.2
  • 33
    • 0023673510 scopus 로고
    • A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the E. coli GroEL gene
    • McMullin, T. W., and R. L. Hallberg. 1988. A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the E. coli GroEL gene. Mol. Cell Biol. 8:371-380.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 371-380
    • McMullin, T.W.1    Hallberg, R.L.2
  • 34
    • 0029069245 scopus 로고
    • Atomic force microscopy of cholera toxin B oligomer bound to bilayers of biologically relevant lipids
    • Mou, J., J. Yang, and Z. Shao. 1995a. Atomic force microscopy of cholera toxin B oligomer bound to bilayers of biologically relevant lipids. J. Mol. Biol. 248:507-512.
    • (1995) J. Mol. Biol. , vol.248 , pp. 507-512
    • Mou, J.1    Yang, J.2    Shao, Z.3
  • 35
    • 0029127492 scopus 로고
    • High resolution atomic force microscopy of DNA: The pitch of the double helix
    • Mou, J., D. M. Czajkowsky, Y. Zhang, and Z. Shao. 1995b. High resolution atomic force microscopy of DNA: the pitch of the double helix. FEBS Lett. 371:279-282.
    • (1995) FEBS Lett. , vol.371 , pp. 279-282
    • Mou, J.1    Czajkowsky, D.M.2    Zhang, Y.3    Shao, Z.4
  • 36
    • 0030029859 scopus 로고    scopus 로고
    • High resolution surface structure of E. coli GroES oligomer by atomic force microscopy
    • Mou, J., D. M. Czajkowsky, S. Sheng, R. Ho, and Z. Shao. 1996. High resolution surface structure of E. coli GroES oligomer by atomic force microscopy. FEBS Lett. 381:161-164.
    • (1996) FEBS Lett. , vol.381 , pp. 161-164
    • Mou, J.1    Czajkowsky, D.M.2    Sheng, S.3    Ho, R.4    Shao, Z.5
  • 37
    • 0028957621 scopus 로고
    • Imaging purple membranes in aqueous-solution at subnanometer resolution by atomic force microscopy
    • Muller, D. J., F. A. Schabert, G. Buldt, and A. Engel. 1995. Imaging purple membranes in aqueous-solution at subnanometer resolution by atomic force microscopy. Biophys. J. 68:1681-1686.
    • (1995) Biophys. J. , vol.68 , pp. 1681-1686
    • Muller, D.J.1    Schabert, F.A.2    Buldt, G.3    Engel, A.4
  • 38
    • 0026736892 scopus 로고
    • Imaging the ordered array of water-soluble protein ferritin with the atomic force microscope
    • Ohnishi, S., M. Hara, T. Furuno, and H. Sasabe. 1992. Imaging the ordered array of water-soluble protein ferritin with the atomic force microscope. Biophys. J. 63:1425-1431.
    • (1992) Biophys. J. , vol.63 , pp. 1425-1431
    • Ohnishi, S.1    Hara, M.2    Furuno, T.3    Sasabe, H.4
  • 40
    • 0028031337 scopus 로고
    • Direct observation of enzyme activity with the atomic force microscope
    • Radmacher, M., M. Fritz, H. G. Hansma, and P. K. Hansma. 1994. Direct observation of enzyme activity with the atomic force microscope. Science. 265:1577-1579.
    • (1994) Science , vol.265 , pp. 1577-1579
    • Radmacher, M.1    Fritz, M.2    Hansma, H.G.3    Hansma, P.K.4
  • 42
    • 0029643915 scopus 로고    scopus 로고
    • The lid that shapes the pot: Structure and function of the chaperonin GroES
    • Saibil, H. R., 1996. The lid that shapes the pot: structure and function of the chaperonin GroES. Structure. 4:1-4.
    • (1996) Structure , vol.4 , pp. 1-4
    • Saibil, H.R.1
  • 43
    • 0028986125 scopus 로고
    • Native E. coli Ompf porin surfaces probed by atomic force microscopy
    • Schabert, F. A., C. Henn, and A. Engel. 1995. Native E. coli Ompf porin surfaces probed by atomic force microscopy. Science. 268:92-94.
    • (1995) Science , vol.268 , pp. 92-94
    • Schabert, F.A.1    Henn, C.2    Engel, A.3
  • 45
  • 46
    • 0028787279 scopus 로고
    • Stereo representation of atomic force micrographs: Optimizing the view
    • Shao, Z., and A. P. Somlyo. 1995. Stereo representation of atomic force micrographs: optimizing the view. J. Microsc. (Oxf.) 180:186-188.
    • (1995) J. Microsc. (Oxf.) , vol.180 , pp. 186-188
    • Shao, Z.1    Somlyo, A.P.2
  • 47
    • 0029021712 scopus 로고
    • Progress in high resolution atomic force microscopy in biology
    • Shao, Z., and J. Yang. 1995. Progress in high resolution atomic force microscopy in biology. Q. Rev. Biophys. 28:195-251.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 195-251
    • Shao, Z.1    Yang, J.2
  • 48
    • 0029563227 scopus 로고
    • Biological atomic force microscopy: From microns to nanometers and beyond
    • Shao, Z., J. Yang, and A. P. Somlyo. 1995. Biological atomic force microscopy: from microns to nanometers and beyond. Anna. Rev. Cell Dev. Biol. 11:241-265.
    • (1995) Anna. Rev. Cell Dev. Biol. , vol.11 , pp. 241-265
    • Shao, Z.1    Yang, J.2    Somlyo, A.P.3
  • 49
    • 0029734665 scopus 로고    scopus 로고
    • Biological atomic force microscopy: What is achieved and what is needed
    • Shao, Z., J. Mou, D. M. Czajkowsky, J. Yang, and J. Y. Yuan. 1996. Biological atomic force microscopy: what is achieved and what is needed. Adv. Phys. 45:1-86.
    • (1996) Adv. Phys. , vol.45 , pp. 1-86
    • Shao, Z.1    Mou, J.2    Czajkowsky, D.M.3    Yang, J.4    Yuan, J.Y.5
  • 50
    • 0029653879 scopus 로고
    • Unliganded GroEL at 2.8 A structure and functional implications
    • Sigler, P. B., and A. L. Horwich. 1995. Unliganded GroEL at 2.8 A structure and functional implications. Philos. Trans. R. Soc. Lond-Biol. Sci. 348:113-119.
    • (1995) Philos. Trans. R. Soc. Lond-Biol. Sci. , vol.348 , pp. 113-119
    • Sigler, P.B.1    Horwich, A.L.2
  • 51
    • 0029643911 scopus 로고    scopus 로고
    • Solution structure of GroEL and its complex with rhodanese from small angle neutron scattering
    • Thiyagarajan, P., S. J. Henderson, and A. Joachimiak. 1996. Solution structure of GroEL and its complex with rhodanese from small angle neutron scattering. Structure. 4:79-88.
    • (1996) Structure , vol.4 , pp. 79-88
    • Thiyagarajan, P.1    Henderson, S.J.2    Joachimiak, A.3
  • 52
    • 0345483102 scopus 로고
    • Identification of a second E. coli groE gene whose product is necessary for bacteriophage morphogenesis
    • Tilly, K., H. Murialdo, and C. Georgeopoulos. 1981. Identification of a second E. coli groE gene whose product is necessary for bacteriophage morphogenesis. Proc Natl. Acad. Sci. U.S.A. 78:1629-1633.
    • (1981) Proc Natl. Acad. Sci. U.S.A. , vol.78 , pp. 1629-1633
    • Tilly, K.1    Murialdo, H.2    Georgeopoulos, C.3
  • 53
    • 0028136474 scopus 로고
    • Mass analysis of biological macromolecular complexes by STEM
    • Thomas, D., P. Schultz, A. C. Steven, and J. S. Wall. 1994. Mass analysis of biological macromolecular complexes by STEM. Biol. Cell. 80:181-192.
    • (1994) Biol. Cell. , vol.80 , pp. 181-192
    • Thomas, D.1    Schultz, P.2    Steven, A.C.3    Wall, J.S.4
  • 54
    • 0027250447 scopus 로고
    • Hydrolysis of adenosine 5′-triphosphate by E. coli GroEL: Effects of GroES and potassium ion
    • Todd, M. J., P. V. Viitanen, and G. H. Lorimer. 1993. Hydrolysis of adenosine 5′-triphosphate by E. coli GroEL: effects of GroES and potassium ion. Biochemistry. 32:8560-8567.
    • (1993) Biochemistry , vol.32 , pp. 8560-8567
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 55
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
    • Todd, M., P. Viitanen, and G. H. Lorimer. 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.1    Viitanen, P.2    Lorimer, G.H.3
  • 56
    • 0028815428 scopus 로고
    • GroES and the chaperonin assisted protein folding cycle: GroES has no affinity for nucleotides
    • Todd, M. J., O. Boudkin, E. Freire, and G. H. Lorimer. 1995. GroES and the chaperonin assisted protein folding cycle: GroES has no affinity for nucleotides. FEBS Lett. 359:123-125.
    • (1995) FEBS Lett. , vol.359 , pp. 123-125
    • Todd, M.J.1    Boudkin, O.2    Freire, E.3    Lorimer, G.H.4
  • 57
    • 0025748752 scopus 로고
    • A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
    • Trent, J. D., E. Nimmesgern, J. S. Wall, F. U. Hartl, and A. L. Horwich. 1991. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature. 354:490-493.
    • (1991) Nature , vol.354 , pp. 490-493
    • Trent, J.D.1    Nimmesgern, E.2    Wall, J.S.3    Hartl, F.U.4    Horwich, A.L.5
  • 59
    • 0030056969 scopus 로고    scopus 로고
    • Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
    • Weissman, J. S., H. S. Rye, W. A. Fenton, J. M. Beechem, and A. L. Horwich, 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
  • 60
    • 0027406608 scopus 로고
    • New approach for atomic force microscopy of membrane proteins: The imaging of cholera toxin
    • Yang, J., L. K. Tamm, T. W. Tillack, and Z. Shao. 1993. New approach for atomic force microscopy of membrane proteins: the imaging of cholera toxin. J. Mol. Biol. 229:286-290.
    • (1993) J. Mol. Biol. , vol.229 , pp. 286-290
    • Yang, J.1    Tamm, L.K.2    Tillack, T.W.3    Shao, Z.4
  • 61
    • 0028013352 scopus 로고
    • Structure and stability of pertussis toxin studied by in situ atomic force microscopy
    • Yang, J., J. Mou, and Z. Shao. 1994a. Structure and stability of pertussis toxin studied by in situ atomic force microscopy. FEBS Lett. 338:89-92.
    • (1994) FEBS Lett. , vol.338 , pp. 89-92
    • Yang, J.1    Mou, J.2    Shao, Z.3
  • 62
    • 0028212033 scopus 로고
    • Molecular resolution atomic force microscopy of soluble proteins in solution
    • Yang, J., J. Mou, and Z. Shao. 1994b. Molecular resolution atomic force microscopy of soluble proteins in solution. Biochim. Biophvs. Acta. 1199:105-114.
    • (1994) Biochim. Biophvs. Acta , vol.1199 , pp. 105-114
    • Yang, J.1    Mou, J.2    Shao, Z.3
  • 63
    • 0030043696 scopus 로고    scopus 로고
    • The effect of deformation on the lateral resolution of atomic force microscopy
    • Yang, J., J. Mou, J. Y. Yuan, and Z. Shao. 1996. The effect of deformation on the lateral resolution of atomic force microscopy. J. Microsc. (Oxf.). 182:106-113.
    • (1996) J. Microsc. (Oxf.) , vol.182 , pp. 106-113
    • Yang, J.1    Mou, J.2    Yuan, J.Y.3    Shao, Z.4
  • 64
    • 0029088389 scopus 로고
    • Monomer-heptamer equilibrium of the E. coli chaperonin GroES
    • Zondlo, J., K. E. Fisher, Z. Lin, K. R. Ducote, and E. Eisenstein. 1995. Monomer-heptamer equilibrium of the E. coli chaperonin GroES. Biochemistry. 34:10334-10339.
    • (1995) Biochemistry , vol.34 , pp. 10334-10339
    • Zondlo, J.1    Fisher, K.E.2    Lin, Z.3    Ducote, K.R.4    Eisenstein, E.5


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