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Volumn 398, Issue 4, 2010, Pages 600-613

Low-Level Expression of a Folding-Incompetent Protein in Escherichia coli: Search for the Molecular Determinants of Protein Aggregation In Vivo

Author keywords

Heterologous; Intrinsic aggregation propensity; Oligomers; Protein misfolding; Simulations

Indexed keywords

AMYLOID; ESCHERICHIA COLI PROTEIN; PROTEIN HYPF; UNCLASSIFIED DRUG; HYPF PROTEIN, E COLI; MUTANT PROTEIN; TRANSFERASE;

EID: 77951887037     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.03.030     Document Type: Article
Times cited : (18)

References (73)
  • 1
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 1999, 24:329-332.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75:333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B., Weissman J., Horwich A. Molecular chaperones and protein quality control. Cell 2006, 125:443-451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 4
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe D.J. Folding proteins in fatal ways. Nature 2003, 426:900-904.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 5
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: the importance of being unfolded
    • Uversky V.N., Fink A.L. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta 2004, 1698:131-153.
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 6
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly J.W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 1998, 8:101-106.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 7
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti F., Dobson C.M. Amyloid formation by globular proteins under native conditions. Nat. Chem. Biol. 2009, 5:15-22.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 8
    • 0034599720 scopus 로고    scopus 로고
    • Mutational analysis of the propensity for amyloid formation by a globular protein
    • Chiti F., Taddei N., Bucciantini M., White P., Ramponi G., Dobson C.M. Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J. 2000, 19:1441-1449.
    • (2000) EMBO J. , vol.19 , pp. 1441-1449
    • Chiti, F.1    Taddei, N.2    Bucciantini, M.3    White, P.4    Ramponi, G.5    Dobson, C.M.6
  • 9
    • 0033020141 scopus 로고    scopus 로고
    • Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains
    • Raffen R., Dieckman L.J., Szpunar M., Wunschl C., Pokkuluri P.R., Dave P., et al. Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains. Protein Sci. 1999, 8:509-517.
    • (1999) Protein Sci. , vol.8 , pp. 509-517
    • Raffen, R.1    Dieckman, L.J.2    Szpunar, M.3    Wunschl, C.4    Pokkuluri, P.R.5    Dave, P.6
  • 10
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth D.R., Sunde M., Bellotti V., Robinson C.V., Hutchinson W.L., Fraser P.E., et al. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 1997, 385:787-793.
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1    Sunde, M.2    Bellotti, V.3    Robinson, C.V.4    Hutchinson, W.L.5    Fraser, P.E.6
  • 12
    • 0038575395 scopus 로고    scopus 로고
    • A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation
    • Smith D.P., Jones S., Serpell L.C., Sunde M., Radford S.E. A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation. J. Mol. Biol. 2003, 330:943-954.
    • (2003) J. Mol. Biol. , vol.330 , pp. 943-954
    • Smith, D.P.1    Jones, S.2    Serpell, L.C.3    Sunde, M.4    Radford, S.E.5
  • 13
    • 0037795635 scopus 로고    scopus 로고
    • Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro
    • Stathopulos P.B., Rumfeldt J.A., Scholz G.A., Irani R.A., Frey H.E., Hallewell R.A., et al. Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro. Proc. Natl Acad. Sci. USA 2003, 100:7021-7026.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 7021-7026
    • Stathopulos, P.B.1    Rumfeldt, J.A.2    Scholz, G.A.3    Irani, R.A.4    Frey, H.E.5    Hallewell, R.A.6
  • 14
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti F., Stefani M., Taddei N., Ramponi G., Dobson C.M. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 2003, 424:805-808.
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 15
  • 16
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla A.M., Rousseau F., Schymkowitz J., Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 2004, 22:1302-1306.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 17
    • 3042584515 scopus 로고    scopus 로고
    • The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates
    • Tartaglia G.G., Cavalli A., Pellarin R., Caflisch A. The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates. Protein Sci. 2004, 13:1939-1941.
    • (2004) Protein Sci. , vol.13 , pp. 1939-1941
    • Tartaglia, G.G.1    Cavalli, A.2    Pellarin, R.3    Caflisch, A.4
  • 18
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases
    • Pawar A.P., Dubay K.F., Zurdo J., Chiti F., Vendruscolo M., Dobson C.M. Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 2005, 350:379-392.
    • (2005) J. Mol. Biol. , vol.350 , pp. 379-392
    • Pawar, A.P.1    Dubay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 19
    • 25844466604 scopus 로고    scopus 로고
    • Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences
    • Tartaglia G.G., Cavalli A., Pellarin R., Caflisch A. Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences. Protein Sci. 2005, 14:2723-2734.
    • (2005) Protein Sci. , vol.14 , pp. 2723-2734
    • Tartaglia, G.G.1    Cavalli, A.2    Pellarin, R.3    Caflisch, A.4
  • 20
    • 33644940173 scopus 로고    scopus 로고
    • Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities
    • de Groot N.S., Aviles F.X., Vendrell J., Ventura S. Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities. FEBS J. 2006, 273:658-668.
    • (2006) FEBS J. , vol.273 , pp. 658-668
    • de Groot, N.S.1    Aviles, F.X.2    Vendrell, J.3    Ventura, S.4
  • 22
    • 33744973540 scopus 로고    scopus 로고
    • Interaction-based evaluation of the propensity for amyloid formation with cross-beta structure
    • Saiki M., Konakahara T., Morii H. Interaction-based evaluation of the propensity for amyloid formation with cross-beta structure. Biochem. Biophys. Res. Commun. 2006, 343:1262-1271.
    • (2006) Biochem. Biophys. Res. Commun. , vol.343 , pp. 1262-1271
    • Saiki, M.1    Konakahara, T.2    Morii, H.3
  • 24
    • 33845978790 scopus 로고    scopus 로고
    • Insight into the structure of amyloid fibrils from the analysis of globular proteins
    • Trovato A., Chiti F., Maritan A., Seno F. Insight into the structure of amyloid fibrils from the analysis of globular proteins. PLoS Comput. Biol. 2006, e170:2.
    • (2006) PLoS Comput. Biol. , vol.170 , pp. 2
    • Trovato, A.1    Chiti, F.2    Maritan, A.3    Seno, F.4
  • 26
    • 34548756136 scopus 로고    scopus 로고
    • Identification of amyloid fibril-forming segments based on structure and residue-based statistical potential
    • Zhang Z., Chen H., Lai L. Identification of amyloid fibril-forming segments based on structure and residue-based statistical potential. Bioinformatics 2007, 23:2218-2225.
    • (2007) Bioinformatics , vol.23 , pp. 2218-2225
    • Zhang, Z.1    Chen, H.2    Lai, L.3
  • 27
    • 34247591802 scopus 로고    scopus 로고
    • A simple algorithm locates beta-strands in the amyloid fibril core of alpha-synuclein, Abeta, and tau using the amino acid sequence alone
    • Zibaee S., Makin O.S., Goedert M., Serpell L.C. A simple algorithm locates beta-strands in the amyloid fibril core of alpha-synuclein, Abeta, and tau using the amino acid sequence alone. Protein Sci. 2007, 16:906-918.
    • (2007) Protein Sci. , vol.16 , pp. 906-918
    • Zibaee, S.1    Makin, O.S.2    Goedert, M.3    Serpell, L.C.4
  • 33
    • 33646106328 scopus 로고    scopus 로고
    • Protein quality in bacterial inclusion bodies
    • Ventura S., Villaverde A. Protein quality in bacterial inclusion bodies. Trends Biotechnol. 2006, 24:179-185.
    • (2006) Trends Biotechnol. , vol.24 , pp. 179-185
    • Ventura, S.1    Villaverde, A.2
  • 34
    • 0035187228 scopus 로고    scopus 로고
    • Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain
    • Chiti F., Bucciantini M., Capanni C., Taddei N., Dobson C.M., Stefani M. Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain. Protein Sci. 2001, 10:2541-2547.
    • (2001) Protein Sci. , vol.10 , pp. 2541-2547
    • Chiti, F.1    Bucciantini, M.2    Capanni, C.3    Taddei, N.4    Dobson, C.M.5    Stefani, M.6
  • 35
    • 11144353842 scopus 로고    scopus 로고
    • Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils
    • Relini A., Torrassa S., Rolandi R., Gliozzi A., Rosano C., Canale C., et al. Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. J. Mol. Biol. 2004, 338:943-957.
    • (2004) J. Mol. Biol. , vol.338 , pp. 943-957
    • Relini, A.1    Torrassa, S.2    Rolandi, R.3    Gliozzi, A.4    Rosano, C.5    Canale, C.6
  • 36
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 2002, 416:507-511.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5    Zurdo, J.6
  • 38
    • 24344467958 scopus 로고    scopus 로고
    • Insights into the molecular basis of the differing susceptibility of varying cell types to the toxicity of amyloid aggregates
    • Cecchi C., Baglioni S., Fiorillo C., Pensalfini A., Liguri G., Nosi D., et al. Insights into the molecular basis of the differing susceptibility of varying cell types to the toxicity of amyloid aggregates. J. Cell Sci. 2005, 118:3459-3470.
    • (2005) J. Cell Sci. , vol.118 , pp. 3459-3470
    • Cecchi, C.1    Baglioni, S.2    Fiorillo, C.3    Pensalfini, A.4    Liguri, G.5    Nosi, D.6
  • 41
    • 14644406760 scopus 로고    scopus 로고
    • Amyloid formation from HypF-N under conditions in which the protein is initially in its native state
    • Marcon G., Plakoutsi G., Canale C., Relini A., Taddei N., Dobson C.M., et al. Amyloid formation from HypF-N under conditions in which the protein is initially in its native state. J. Mol. Biol. 2005, 347:323-335.
    • (2005) J. Mol. Biol. , vol.347 , pp. 323-335
    • Marcon, G.1    Plakoutsi, G.2    Canale, C.3    Relini, A.4    Taddei, N.5    Dobson, C.M.6
  • 42
    • 58149169040 scopus 로고    scopus 로고
    • Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation
    • Calloni G., Lendel C., Campioni S., Giannini S., Gliozzi A., Relini A., et al. Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation. J. Am. Chem. Soc. 2008, 130:13040-13050.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 13040-13050
    • Calloni, G.1    Lendel, C.2    Campioni, S.3    Giannini, S.4    Gliozzi, A.5    Relini, A.6
  • 44
    • 15444373859 scopus 로고    scopus 로고
    • Investigating the effects of mutations on protein aggregation in the cell
    • Calloni G., Zoffoli S., Stefani M., Dobson C.M., Chiti F. Investigating the effects of mutations on protein aggregation in the cell. J. Biol. Chem. 2005, 280:10607-10613.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10607-10613
    • Calloni, G.1    Zoffoli, S.2    Stefani, M.3    Dobson, C.M.4    Chiti, F.5
  • 45
    • 0029921234 scopus 로고    scopus 로고
    • C-terminal region contributes to muscle acylphosphatase three-dimensional structure stabilisation
    • Taddei N., Magherini F., Chiti F., Bucciantini M., Raugei G., Stefani M., Ramponi G. C-terminal region contributes to muscle acylphosphatase three-dimensional structure stabilisation. FEBS Lett. 1996, 384:172-176.
    • (1996) FEBS Lett. , vol.384 , pp. 172-176
    • Taddei, N.1    Magherini, F.2    Chiti, F.3    Bucciantini, M.4    Raugei, G.5    Stefani, M.6    Ramponi, G.7
  • 46
    • 0038047129 scopus 로고    scopus 로고
    • Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding
    • Calloni G., Taddei N., Plaxco K.W., Ramponi G., Stefani M., Chiti F. Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding. J. Mol. Biol. 2003, 330:577-591.
    • (2003) J. Mol. Biol. , vol.330 , pp. 577-591
    • Calloni, G.1    Taddei, N.2    Plaxco, K.W.3    Ramponi, G.4    Stefani, M.5    Chiti, F.6
  • 47
    • 54249116230 scopus 로고
    • Genetic regulatory mechanisms in the synthesis of proteins
    • Jacob F., Monod J. Genetic regulatory mechanisms in the synthesis of proteins. J. Mol. Biol. 1961, 3:318-356.
    • (1961) J. Mol. Biol. , vol.3 , pp. 318-356
    • Jacob, F.1    Monod, J.2
  • 48
    • 33846516797 scopus 로고    scopus 로고
    • The lactose repressor system: paradigms for regulation, allosteric behavior and protein folding
    • Wilson C.J., Zhan H., Swint-Kruse L., Matthews K.S. The lactose repressor system: paradigms for regulation, allosteric behavior and protein folding. Cell. Mol. Life Sci. 2007, 64:3-16.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 3-16
    • Wilson, C.J.1    Zhan, H.2    Swint-Kruse, L.3    Matthews, K.S.4
  • 49
    • 0018138536 scopus 로고
    • Sequence of the lacI gene
    • Farabaugh P.J. Sequence of the lacI gene. Nature 1978, 274:765-769.
    • (1978) Nature , vol.274 , pp. 765-769
    • Farabaugh, P.J.1
  • 50
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • Hartl F.U., Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2002, 295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 51
    • 33750008686 scopus 로고    scopus 로고
    • Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
    • Shiau A.K., Harris S.F., Southworth D.R., Agard D.A. Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 2006, 127:329-340.
    • (2006) Cell , vol.127 , pp. 329-340
    • Shiau, A.K.1    Harris, S.F.2    Southworth, D.R.3    Agard, D.A.4
  • 52
    • 33846945050 scopus 로고    scopus 로고
    • The small heat shock proteins and their clients
    • Nakamoto H., Vigh L. The small heat shock proteins and their clients. Cell. Mol. Life Sci. 2007, 64:294-306.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 294-306
    • Nakamoto, H.1    Vigh, L.2
  • 53
    • 26844539619 scopus 로고    scopus 로고
    • Novel insights into the mechanism of chaperone-assisted protein disaggregation
    • Weibezahn J., Schlieker C., Tessarz P., Mogk A., Bukau B. Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biol. Chem. 2005, 386:739-744.
    • (2005) Biol. Chem. , vol.386 , pp. 739-744
    • Weibezahn, J.1    Schlieker, C.2    Tessarz, P.3    Mogk, A.4    Bukau, B.5
  • 55
    • 40049110948 scopus 로고    scopus 로고
    • Mutations enhance the aggregation propensity of the Alzheimer's A beta peptide
    • Kim W., Hecht M.H. Mutations enhance the aggregation propensity of the Alzheimer's A beta peptide. J. Mol. Biol. 2008, 377:565-574.
    • (2008) J. Mol. Biol. , vol.377 , pp. 565-574
    • Kim, W.1    Hecht, M.H.2
  • 57
    • 48349090111 scopus 로고    scopus 로고
    • Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival
    • Wang Q., Johnson J.L., Agar N.Y., Agar J.N. Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival. PLoS Biol. 2008, e170:6.
    • (2008) PLoS Biol. , vol.170 , pp. 6
    • Wang, Q.1    Johnson, J.L.2    Agar, N.Y.3    Agar, J.N.4
  • 58
    • 0344395589 scopus 로고    scopus 로고
    • FT-IR study of heterologous protein expression in recombinant Escherichia coli strains
    • Ami D., Bonecchi L., Cali S., Orsini G., Tonon G., Doglia S.M. FT-IR study of heterologous protein expression in recombinant Escherichia coli strains. Biochim. Biophys. Acta 2003, 1624:6-10.
    • (2003) Biochim. Biophys. Acta , vol.1624 , pp. 6-10
    • Ami, D.1    Bonecchi, L.2    Cali, S.3    Orsini, G.4    Tonon, G.5    Doglia, S.M.6
  • 59
    • 20444363444 scopus 로고    scopus 로고
    • Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy
    • Ami D., Natalello A., Gatti-Lafranconi P., Lotti M., Doglia S.M. Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy. FEBS Lett. 2005, 579:3433-3436.
    • (2005) FEBS Lett. , vol.579 , pp. 3433-3436
    • Ami, D.1    Natalello, A.2    Gatti-Lafranconi, P.3    Lotti, M.4    Doglia, S.M.5
  • 60
    • 23044456332 scopus 로고    scopus 로고
    • Characterization of the aggregates formed during recombinant protein expression in bacteria
    • Schrödel A., de Marco A. Characterization of the aggregates formed during recombinant protein expression in bacteria. BMC Biochem. 2005, 6:10.
    • (2005) BMC Biochem. , vol.6 , pp. 10
    • Schrödel, A.1    de Marco, A.2
  • 61
    • 0028981336 scopus 로고
    • Alternative method to remove antibacterial antibodies from antisera used for screening of expression libraries
    • Gruber A., Zingales B. Alternative method to remove antibacterial antibodies from antisera used for screening of expression libraries. Biotechniques 1995, 19:30.
    • (1995) Biotechniques , vol.19 , pp. 30
    • Gruber, A.1    Zingales, B.2
  • 62
    • 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 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 63
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters: II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Muñoz V., Serrano L. Elucidating the folding problem of helical peptides using empirical parameters: II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 1995, 245:275-296.
    • (1995) J. Mol. Biol. , vol.245 , pp. 275-296
    • Muñoz, V.1    Serrano, L.2
  • 64
    • 0028834210 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters: III. Temperature and pH dependence
    • Muñoz V., Serrano L. Elucidating the folding problem of helical peptides using empirical parameters: III. Temperature and pH dependence. J. Mol. Biol. 1995, 245:297-308.
    • (1995) J. Mol. Biol. , vol.245 , pp. 297-308
    • Muñoz, V.1    Serrano, L.2
  • 65
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms
    • Muñoz V., Serrano L. Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers 1997, 41:495-509.
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Muñoz, V.1    Serrano, L.2
  • 66
    • 0032553332 scopus 로고    scopus 로고
    • Elucidating the folding problem of alpha-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters
    • Lacroix E., Viguera A.R., Serrano L. Elucidating the folding problem of alpha-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters. J. Mol. Biol. 1998, 284:173-191.
    • (1998) J. Mol. Biol. , vol.284 , pp. 173-191
    • Lacroix, E.1    Viguera, A.R.2    Serrano, L.3
  • 67
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • Flynn J.M., Neher S.B., Kim Y.I., Sauer R.T., Baker T.A. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell 2003, 11:671-683.
    • (2003) Mol. Cell , vol.11 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.I.3    Sauer, R.T.4    Baker, T.A.5
  • 68
    • 32544432878 scopus 로고    scopus 로고
    • ClpS is an essential component of the N-end rule pathway in Escherichia coli
    • Erbse A., Schmidt R., Bornemann T., Schneider-Mergener J., Mogk A., Zahn R., et al. ClpS is an essential component of the N-end rule pathway in Escherichia coli. Nature 2006, 439:753-756.
    • (2006) Nature , vol.439 , pp. 753-756
    • Erbse, A.1    Schmidt, R.2    Bornemann, T.3    Schneider-Mergener, J.4    Mogk, A.5    Zahn, R.6
  • 69
    • 32244435782 scopus 로고    scopus 로고
    • Two peptide sequences can function cooperatively to facilitate binding and unfolding by ClpA and degradation by ClpAP
    • Hoskins J.R., Wickner S. Two peptide sequences can function cooperatively to facilitate binding and unfolding by ClpA and degradation by ClpAP. Proc. Natl Acad. Sci. USA 2006, 103:909-914.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 909-914
    • Hoskins, J.R.1    Wickner, S.2
  • 70
    • 33645085050 scopus 로고    scopus 로고
    • The C-terminal end of LpxC is required for degradation by the FtsH protease
    • Führer F., Langklotz S., Narberhaus F. The C-terminal end of LpxC is required for degradation by the FtsH protease. Mol. Microbiol. 2006, 59:1025-1036.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1025-1036
    • Führer, F.1    Langklotz, S.2    Narberhaus, F.3
  • 71
    • 33644935094 scopus 로고    scopus 로고
    • Sequence requirements for Lon-dependent degradation of the Escherichia coli transcription activator SoxS: identification of the SoxS residues critical to proteolysis and specific inhibition of in vitro degradation by a peptide comprised of the N-terminal 21 amino acid residues
    • Shah I.M., Wolf R.E. Sequence requirements for Lon-dependent degradation of the Escherichia coli transcription activator SoxS: identification of the SoxS residues critical to proteolysis and specific inhibition of in vitro degradation by a peptide comprised of the N-terminal 21 amino acid residues. J. Mol. Biol. 2006, 357:718-731.
    • (2006) J. Mol. Biol. , vol.357 , pp. 718-731
    • Shah, I.M.1    Wolf, R.E.2
  • 72
    • 0032535038 scopus 로고    scopus 로고
    • Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis
    • Gonzalez M., Frank E.G., Levine A.S., Woodgate R. Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis. Genes Dev. 1998, 12:3889-3899.
    • (1998) Genes Dev. , vol.12 , pp. 3889-3899
    • Gonzalez, M.1    Frank, E.G.2    Levine, A.S.3    Woodgate, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.