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Volumn 18, Issue 11, 2004, Pages 1169-1175

The role of structural disorder in the function of RNA and protein chaperones

Author keywords

Chaperone evolution; Chaperone function; Entropy transfer; Intrinsically unstructured protein

Indexed keywords

ALPHA CRYSTALLIN; ALPHA SYNUCLEIN; CASEIN; CHAPERONE; CHAPERONIN; HEAT SHOCK PROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; LA ANTIGEN; NUCLEOLIN; PRION PROTEIN; PROTEIN DNAK; PROTEOME; REV PROTEIN; RIBOSOME PROTEIN; RNA;

EID: 3442902456     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.04-1584rev     Document Type: Review
Times cited : (473)

References (65)
  • 1
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P. E., and Dyson, H. J. (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321-331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 2
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. (2002) Natively unfolded proteins: a point where biology waits for physics. Protein Sci. 11, 739-756
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 3
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. (2002) Intrinsically unstructured proteins. Trends Biochem. Sci. 27, 527-533
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 7
    • 0036408751 scopus 로고    scopus 로고
    • Intrinsic disorder in cell-signaling and cancer-associated proteins
    • Iakoucheva, L., Brown, C., Lawson, J., Obradovic, Z., and Dunker, A. (2002) Intrinsic disorder in cell-signaling and cancer-associated proteins. J. Mol. Biol. 323, 573-584
    • (2002) J. Mol. Biol. , vol.323 , pp. 573-584
    • Iakoucheva, L.1    Brown, C.2    Lawson, J.3    Obradovic, Z.4    Dunker, A.5
  • 8
    • 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
  • 9
    • 0033231417 scopus 로고    scopus 로고
    • Chaperone-percolator model: A possible molecular mechanism of Anfinsen-cage-type chaperones
    • Csermely, P. (1999) Chaperone-percolator model: a possible molecular mechanism of Anfinsen-cage-type chaperones. Bioessays 21, 959-965
    • (1999) Bioessays , vol.21 , pp. 959-965
    • Csermely, P.1
  • 10
    • 0030907672 scopus 로고    scopus 로고
    • Proteins, RNAs and chaperones in enzyme evolution: A folding perspective
    • Csermely, P. (1997) Proteins, RNAs and chaperones in enzyme evolution: a folding perspective. Trends Biochem. Sci. 22, 147-149
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 147-149
    • Csermely, P.1
  • 12
    • 36849148382 scopus 로고
    • The RNA world
    • Gilbert, W. (1986) The RNA world. Nature (London) 319, 618
    • (1986) Nature (London) , vol.319 , pp. 618
    • Gilbert, W.1
  • 15
    • 0032479475 scopus 로고    scopus 로고
    • Origins of globular structure in proteins
    • Doi, N., and Yanagawa, H. (1998) Origins of globular structure in proteins. FEBS Lett. 430, 150-153
    • (1998) FEBS Lett. , vol.430 , pp. 150-153
    • Doi, N.1    Yanagawa, H.2
  • 16
    • 0029009727 scopus 로고
    • The molecular chaperonin cpn60 displays local flexibility that is reduced after binding with an unfolded protein
    • Gorovits, B. M., and Horowitz, P. M. (1995) The molecular chaperonin cpn60 displays local flexibility that is reduced after binding with an unfolded protein. J. Biol. Chem. 270, 13057-13062
    • (1995) J. Biol. Chem. , vol.270 , pp. 13057-13062
    • Gorovits, B.M.1    Horowitz, P.M.2
  • 17
    • 0029842722 scopus 로고    scopus 로고
    • Immobilization of the C-terminal extension of bovine alphaA-crystallin reduces chaperone-like activity
    • Smulders, R., Carver, J. A., Lindner, R. A., van Boekel, M. A., Bloemendal, H., and dejong, W. W. (1996) Immobilization of the C-terminal extension of bovine alphaA-crystallin reduces chaperone-like activity. J. Biol. Chem. 271, 29060-29066
    • (1996) J. Biol. Chem. , vol.271 , pp. 29060-29066
    • Smulders, R.1    Carver, J.A.2    Lindner, R.A.3    Van Boekel, M.A.4    Bloemendal, H.5    Dejong, W.W.6
  • 18
    • 0032760261 scopus 로고    scopus 로고
    • An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function
    • Weikl, T., Abelmann, K., and Buchner, J. (1999) An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function. J. Mol. Biol. 293, 685-691
    • (1999) J. Mol. Biol. , vol.293 , pp. 685-691
    • Weikl, T.1    Abelmann, K.2    Buchner, J.3
  • 20
    • 0033060521 scopus 로고    scopus 로고
    • Molecular chaperone-like properties of an unfolded protein, alpha(s)-casein
    • Bhattacharyya, J., and Das, K. P. (1999) Molecular chaperone-like properties of an unfolded protein, alpha(s)-casein. J. Biol. Chem. 274, 15505-15509
    • (1999) J. Biol. Chem. , vol.274 , pp. 15505-15509
    • Bhattacharyya, J.1    Das, K.P.2
  • 21
    • 0037137224 scopus 로고    scopus 로고
    • Structural and functional implications of C-terminal regions of alpha-synuclein
    • Kirn, T. D., Paik, S. R., and Yang, C. H. (2002) Structural and functional implications of C-terminal regions of alpha-synuclein. Biochemistry 41, 13782-13790
    • (2002) Biochemistry , vol.41 , pp. 13782-13790
    • Kirn, T.D.1    Paik, S.R.2    Yang, C.H.3
  • 22
    • 0037047371 scopus 로고    scopus 로고
    • Distinct roles of the N-terminal-binding domain and the C-terminal-solubilizing domain of alpha-synuclein, a molecular chaperone
    • Park, S. M., Jung, H. Y., Kim, T. D., Park, J. H., Yang, C. H., and Kim, J. (2002) Distinct roles of the N-terminal-binding domain and the C-terminal-solubilizing domain of alpha-synuclein, a molecular chaperone. J. Biol. Chem. 277, 28512-28520
    • (2002) J. Biol. Chem. , vol.277 , pp. 28512-28520
    • Park, S.M.1    Jung, H.Y.2    Kim, T.D.3    Park, J.H.4    Yang, C.H.5    Kim, J.6
  • 23
    • 0025188665 scopus 로고
    • Renaturation of complementary DNA strands mediated by purified mammalian heterogeneous nuclear ribonucleoprotein A1 protein: Implications for a mechanism for rapid molecular assembly
    • Pontius, B. W., and Berg, P. (1990) Renaturation of complementary DNA strands mediated by purified mammalian heterogeneous nuclear ribonucleoprotein A1 protein: implications for a mechanism for rapid molecular assembly. Proc. Natl. Acad. Sci. USA 87, 8403-8407
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8403-8407
    • Pontius, B.W.1    Berg, P.2
  • 24
    • 0026749685 scopus 로고
    • Determination of the structure of the nucleocapsid protein NCp7 from the human immunodeficiency virus type 1 by 1H NMR
    • Morellet, N., Jullian, N., De Rocquigny, H., Maigret, B., Darlix, J. L., and Roques, B. P. (1992) Determination of the structure of the nucleocapsid protein NCp7 from the human immunodeficiency virus type 1 by 1H NMR. EMBO J. 11, 3059-3065
    • (1992) EMBO J. , vol.11 , pp. 3059-3065
    • Morellet, N.1    Jullian, N.2    De Rocquigny, H.3    Maigret, B.4    Darlix, J.L.5    Roques, B.P.6
  • 25
    • 0033579503 scopus 로고    scopus 로고
    • Characterization of active reverse transcriptase and nucleoprotein complexes of the yeast retrotransposon Ty3 in vitro
    • Cristofari, G., Gabus, C., Ficheux, D., Bona, M., Le Grice, S. F., and Darlix, J. L. (1999) Characterization of active reverse transcriptase and nucleoprotein complexes of the yeast retrotransposon Ty3 in vitro. J. Biol. Chem. 274, 36643-36648
    • (1999) J. Biol. Chem. , vol.274 , pp. 36643-36648
    • Cristofari, G.1    Gabus, C.2    Ficheux, D.3    Bona, M.4    Le Grice, S.F.5    Darlix, J.L.6
  • 27
    • 0037675852 scopus 로고    scopus 로고
    • Mutual induced fit binding of Xenopus ribosomal protein L5 to 5S rRNA
    • DiNitto, J. P., and Huber, P. W. (2003) Mutual induced fit binding of Xenopus ribosomal protein L5 to 5S rRNA. J. Mol. Biol. 330, 979-992
    • (2003) J. Mol. Biol. , vol.330 , pp. 979-992
    • DiNitto, J.P.1    Huber, P.W.2
  • 28
    • 0033784534 scopus 로고    scopus 로고
    • Induced fit in RNA-protein recognition
    • Williamson, J. R. (2000) Induced fit in RNA-protein recognition. Nat. Struct. Biol. 7, 834-837
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 834-837
    • Williamson, J.R.1
  • 29
    • 0035838382 scopus 로고    scopus 로고
    • Current topics in RNA-protein recognition: Control of specificity and biological function through induced fit and conformational capture
    • Leulliot, N., and Varani, G. (2001) Current topics in RNA-protein recognition: control of specificity and biological function through induced fit and conformational capture. Biochemistry 40, 7947-7956
    • (2001) Biochemistry , vol.40 , pp. 7947-7956
    • Leulliot, N.1    Varani, G.2
  • 30
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P. B., and Steitz, T. A. (2000) The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289, 905-920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 31
    • 0031614914 scopus 로고    scopus 로고
    • Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein
    • Mogridge, J., Legault, P., Li, J., Van Oene, M. D., Kay, L. E., and Greenblatt, J. (1998) Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein. Mol. Cell 1, 265-275
    • (1998) Mol. Cell , vol.1 , pp. 265-275
    • Mogridge, J.1    Legault, P.2    Li, J.3    Van Oene, M.D.4    Kay, L.E.5    Greenblatt, J.6
  • 32
    • 0038646814 scopus 로고    scopus 로고
    • Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element
    • Jacks, A., Babon, J., Kelly, G., Manolaridis, I., Cary, P. D., Curry, S., and Conte, M. R. (2003) Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element. Structure (Cambridge) 11, 833-843
    • (2003) Structure (Cambridge) , vol.11 , pp. 833-843
    • Jacks, A.1    Babon, J.2    Kelly, G.3    Manolaridis, I.4    Cary, P.D.5    Curry, S.6    Conte, M.R.7
  • 34
    • 0029163563 scopus 로고
    • RNA chaperones and the RNA folding problem
    • Herschlag, D. (1995) RNA chaperones and the RNA folding problem. J. Biol. Chem. 270, 20871-20874
    • (1995) J. Biol. Chem. , vol.270 , pp. 20871-20874
    • Herschlag, D.1
  • 35
    • 0037188887 scopus 로고    scopus 로고
    • RNA chaperones exist and DEAD box proteins get a life
    • Lorsch, J. R. (2002) RNA chaperones exist and DEAD box proteins get a life. Cell 109, 797-800
    • (2002) Cell , vol.109 , pp. 797-800
    • Lorsch, J.R.1
  • 36
    • 0027311259 scopus 로고
    • Close encounters: Why unstructured, polymeric domains can increase rates of specific macromolecular association
    • Pontius, B. W. (1993) Close encounters: why unstructured, polymeric domains can increase rates of specific macromolecular association. Trends Biochem. Sci. 18, 181-186
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 181-186
    • Pontius, B.W.1
  • 37
    • 0033169013 scopus 로고    scopus 로고
    • Assaying RNA chaperone activity in vivo using a novel RNA folding trap
    • Clodi, E., Semrad, K, and Schroeder, R. (1999) Assaying RNA chaperone activity in vivo using a novel RNA folding trap. EMBO J. 18, 3776-3782
    • (1999) EMBO J. , vol.18 , pp. 3776-3782
    • Clodi, E.1    Semrad, K.2    Schroeder, R.3
  • 38
    • 0029770039 scopus 로고    scopus 로고
    • Cloning, expression, and chaperone-like activity of human alphaA-crystallin
    • Andley, U. P., Mathur, S., Griest, T. A., and Petrash J. M. (1996) Cloning, expression, and chaperone-like activity of human alphaA-crystallin. J. Biol. Chem. 271, 31973-31980
    • (1996) J. Biol. Chem. , vol.271 , pp. 31973-31980
    • Andley, U.P.1    Mathur, S.2    Griest, T.A.3    Petrash, J.M.4
  • 39
    • 0032533361 scopus 로고    scopus 로고
    • Structural alterations of alpha-crystallin during its chaperone action
    • Lindner, R. A., Kapur, A., Mariani, M., Titmuss, S. J., and Carver, J. A. (1998) Structural alterations of alpha-crystallin during its chaperone action. Eur. J. Biochem. 258, 170-183
    • (1998) Eur. J. Biochem. , vol.258 , pp. 170-183
    • Lindner, R.A.1    Kapur, A.2    Mariani, M.3    Titmuss, S.J.4    Carver, J.A.5
  • 40
    • 0037195949 scopus 로고    scopus 로고
    • Role of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activity
    • Pasta, S. Y., Raman, B., Ramakrishna, T., and Rao Ch, M. (2002) Role of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activity. J. Biol. Chem. 277, 45821-45828
    • (2002) J. Biol. Chem. , vol.277 , pp. 45821-45828
    • Pasta, S.Y.1    Raman, B.2    Ramakrishna, T.3    Rao, Ch.M.4
  • 43
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review
    • Csermely, P., Schnaider, T., Soti, C., Prohaszka, Z., and Nardai, G. (1998) The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol. Ther. 79, 129-168
    • (1998) Pharmacol. Ther. , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohaszka, Z.4    Nardai, G.5
  • 44
    • 0042665942 scopus 로고    scopus 로고
    • Disulfide bonds convert small heat shock protein Hsp16.3 from a chaperone to a non-chaperone: Implications for the evolution of cysteine in molecular chaperones
    • Fu, X., Li, W., Mao, Q., and Chang, Z. (2003) Disulfide bonds convert small heat shock protein Hsp16.3 from a chaperone to a non-chaperone: implications for the evolution of cysteine in molecular chaperones. Biochem. Biophys. Res. Commun. 308, 627-635
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 627-635
    • Fu, X.1    Li, W.2    Mao, Q.3    Chang, Z.4
  • 45
    • 0029662315 scopus 로고    scopus 로고
    • Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: Conformational disorder mediates binding diversity
    • Kriwacki, R. W., Hengst, L., Tennant, L., Reed, S. I., and Wright, P. E. (1996) Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc. Natl. Acad. Sci. USA 93, 11504-11509
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4    Wright, P.E.5
  • 46
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker, B. A., Portman, J. J., and Wolynes, P. G. (2000) Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc. Natl. Acad. Sci. USA 97, 8868-8873
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 47
    • 0035096292 scopus 로고    scopus 로고
    • Recognition between flexible protein molecules: Induced and assisted folding
    • Demchenko, A. P. (2001) Recognition between flexible protein molecules: induced and assisted folding. J. Mol. Recognit. 14, 42-61
    • (2001) J. Mol. Recognit. , vol.14 , pp. 42-61
    • Demchenko, A.P.1
  • 48
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J., and Wright, P. E. (2002) Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 12, 54-60
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 49
    • 0035929161 scopus 로고    scopus 로고
    • AFM force measurements on microtubule-associated proteins: The projection domain exerts a long-range repulsive force
    • Mukhopadhyay, R., and Hoh, J. H. (2001) AFM force measurements on microtubule-associated proteins: the projection domain exerts a long-range repulsive force. FEBS Lett. 505, 374-378
    • (2001) FEBS Lett. , vol.505 , pp. 374-378
    • Mukhopadhyay, R.1    Hoh, J.H.2
  • 50
    • 0030708555 scopus 로고    scopus 로고
    • Entropic exclusion by neurofilament sidearms: A mechanism for maintaining interfilament spacing
    • Brown, H. G., and Hoh, J. H. (1997) Entropic exclusion by neurofilament sidearms: a mechanism for maintaining interfilament spacing. Biochemistry 36, 15035-15040
    • (1997) Biochemistry , vol.36 , pp. 15035-15040
    • Brown, H.G.1    Hoh, J.H.2
  • 51
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout, M. P., Aitchison, J. D., Suprapto, A., Hjertaas, K., Zhao, Y., and Chait, B. T. (2000) The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148, 635-651
    • (2000) J. Cell Biol. , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 52
    • 0036712305 scopus 로고    scopus 로고
    • RNA chaperone StpA loosens interactions of the tertiary structure in the td group I intron in vivo
    • Waldsich, C., Grossberger, R., and Schroeder, R. (2002) RNA chaperone StpA loosens interactions of the tertiary structure in the td group I intron in vivo. Genes Dev. 16, 2300-2312
    • (2002) Genes Dev. , vol.16 , pp. 2300-2312
    • Waldsich, C.1    Grossberger, R.2    Schroeder, R.3
  • 53
    • 0036298272 scopus 로고    scopus 로고
    • HIV-1 nucleocapsid protein activates transient melting of least stable parts of the secondary structure of TAR and its complementary sequence
    • Bernacchi, S., Stoylov, S., Piemont, E., Ficheux, D., Roques, B. P., Darlix, J. L., and Mely, Y. (2002) HIV-1 nucleocapsid protein activates transient melting of least stable parts of the secondary structure of TAR and its complementary sequence. J. Mol. Biol. 317, 385-399
    • (2002) J. Mol. Biol. , vol.317 , pp. 385-399
    • Bernacchi, S.1    Stoylov, S.2    Piemont, E.3    Ficheux, D.4    Roques, B.P.5    Darlix, J.L.6    Mely, Y.7
  • 54
    • 0036307597 scopus 로고    scopus 로고
    • HIV-1 nucleocapsid protein as a nucleic acid chaperone: Spectroscopic study of its helix-destabilizing properties, structural binding specificity, and annealing activity
    • Urbaneja, M. A., Wu, M., Casas-Finet, J. R., and Karpel, R. L. (2002) HIV-1 nucleocapsid protein as a nucleic acid chaperone: spectroscopic study of its helix-destabilizing properties, structural binding specificity, and annealing activity. J. Mol. Biol. 318, 749-764
    • (2002) J. Mol. Biol. , vol.318 , pp. 749-764
    • Urbaneja, M.A.1    Wu, M.2    Casas-Finet, J.R.3    Karpel, R.L.4
  • 55
    • 0037459094 scopus 로고    scopus 로고
    • Destabilization of the HIV-1 complementary sequence of TAR by the nucleocapsid protein through activation of conformational fluctuations
    • Azoulay, J., Clamme, J. P., Darlix, J. L., Roques, B. P., and Mely, Y. (2003) Destabilization of the HIV-1 complementary sequence of TAR by the nucleocapsid protein through activation of conformational fluctuations. J. Mol. Biol. 326, 691-700
    • (2003) J. Mol. Biol. , vol.326 , pp. 691-700
    • Azoulay, J.1    Clamme, J.P.2    Darlix, J.L.3    Roques, B.P.4    Mely, Y.5
  • 56
    • 0035936695 scopus 로고    scopus 로고
    • Heteronuclear NMR studies of the interaction of tRNA(Lys)3 with HIV-1 nucleocapsid protein
    • Tisne, C., Roques, B. P., and Dardel, F. (2001) Heteronuclear NMR studies of the interaction of tRNA(Lys)3 with HIV-1 nucleocapsid protein. J. Mol. Biol. 306, 443-454
    • (2001) J. Mol. Biol. , vol.306 , pp. 443-454
    • Tisne, C.1    Roques, B.P.2    Dardel, F.3
  • 59
    • 0033524418 scopus 로고    scopus 로고
    • EPR mapping of interactions between spin-labeled variants of human carbonic anhydrase II and GroEL: Evidence for increased flexibility of the hydrophobic core by the interaction
    • Persson, M., Hammarstrom, P., Lindgren, M., Jonsson, B. H., Svensson, M., and Carlsson, U. (1999) EPR mapping of interactions between spin-labeled variants of human carbonic anhydrase II and GroEL: Evidence for increased flexibility of the hydrophobic core by the interaction. Biochemistry 38, 432-441
    • (1999) Biochemistry , vol.38 , pp. 432-441
    • Persson, M.1    Hammarstrom, P.2    Lindgren, M.3    Jonsson, B.H.4    Svensson, M.5    Carlsson, U.6
  • 60
    • 0030916948 scopus 로고    scopus 로고
    • Protein-facilitated RNA folding
    • Weeks, K. M. (1997) Protein-facilitated RNA folding. Curr. Opin. Struct. Biol. 7, 336-342
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 336-342
    • Weeks, K.M.1
  • 61
    • 0032079494 scopus 로고    scopus 로고
    • A ribosomal function is necessary for efficient splicing of the T4 phage thymidylate synthase intron in vivo
    • Semrad, K., and Schroeder, R. (1998) A ribosomal function is necessary for efficient splicing of the T4 phage thymidylate synthase intron in vivo. Genes Dev. 12, 1327-1337
    • (1998) Genes Dev. , vol.12 , pp. 1327-1337
    • Semrad, K.1    Schroeder, R.2
  • 62
    • 0037077127 scopus 로고    scopus 로고
    • A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing
    • Mohr, S., Stryker, J. M., and Lambowitz, A. M. (2002) A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing. Cell 109, 769-779
    • (2002) Cell , vol.109 , pp. 769-779
    • Mohr, S.1    Stryker, J.M.2    Lambowitz, A.M.3
  • 63
    • 0035949631 scopus 로고    scopus 로고
    • Another function for the mitochondrial ribosomal RNA: Protein folding
    • Sulijoadikusumo, I., Horikoshi, N., and Usheva, A. (2001) Another function for the mitochondrial ribosomal RNA: protein folding. Biochemistry 40, 11559-11564
    • (2001) Biochemistry , vol.40 , pp. 11559-11564
    • Sulijoadikusumo, I.1    Horikoshi, N.2    Usheva, A.3
  • 65


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.