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Volumn 5, Issue 2, 2010, Pages

Protein aggregation profile of the bacterial cytosol

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; POLYPEPTIDE; PROTEOME; ESCHERICHIA COLI PROTEIN;

EID: 77949692501     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0009383     Document Type: Article
Times cited : (58)

References (83)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein Misfolding, Functional Amyloid, And Human Disease
    • Chiti F, Dobson CM (2006) Protein Misfolding, Functional Amyloid, And Human Disease. Annu Rev Biochem 75: 333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 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 CM (2003) Rationalization Of The Effects Of Mutations On Peptide And Protein Aggregation Rates. Nature 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
  • 3
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid Fibrils From Muscle Myoglobin
    • Fandrich M, Fletcher MA, Dobson CM (2001) Amyloid Fibrils From Muscle Myoglobin. Nature 410: 165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 8
    • 51049095117 scopus 로고    scopus 로고
    • Inclusion Bodies: Specificity In Their Aggregation Process And Amyloid-Like Structure
    • Morell M, Bravo R, Espargaro A, Sisquella X, Aviles FX, et al. (2008) Inclusion Bodies: Specificity In Their Aggregation Process And Amyloid-Like Structure. Biochim Biophys Acta 1783: 1815-1825.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 1815-1825
    • Morell, M.1    Bravo, R.2    Espargaro, A.3    Sisquella, X.4    Aviles, F.X.5
  • 9
    • 45749102914 scopus 로고    scopus 로고
    • The Zyggregator Method For Predicting Protein Aggregation Propensities
    • Tartaglia GG, Vendruscolo M (2008) The Zyggregator Method For Predicting Protein Aggregation Propensities. Chem Soc Rev 37: 1395-1401.
    • (2008) Chem Soc Rev , vol.37 , pp. 1395-1401
    • Tartaglia, G.G.1    Vendruscolo, M.2
  • 10
    • 33947517558 scopus 로고    scopus 로고
    • AGGRESCAN: A Server For The Prediction And Evaluation Of "Hot Spots" Of Aggregation In Polypeptides
    • Conchillo-Sole O, De Groot NS, Aviles FX, Vendrell J, Daura X, et al. (2007) AGGRESCAN: A Server For The Prediction And Evaluation Of "Hot Spots" Of Aggregation In Polypeptides. BMC Bioinformatics 8: 65.
    • (2007) BMC Bioinformatics , vol.8 , pp. 65
    • Conchillo-Sole, O.1    De Groot, N.S.2    Aviles, F.X.3    Vendrell, J.4    Daura, X.5
  • 11
    • 5044235541 scopus 로고    scopus 로고
    • Prediction Of Sequence-Dependent And Mutational Effects On The Aggregation Of Peptides And Proteins
    • Fernandez-Escamilla AM, Rousseau F, Schymkowitz J, Serrano L (2004) Prediction Of Sequence-Dependent And Mutational Effects On The Aggregation Of Peptides And Proteins. Nat Biotechnol 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
  • 12
    • 25844466604 scopus 로고    scopus 로고
    • Prediction Of Aggregation Rate And Aggregation-Prone Segments In Polypeptide Sequences
    • Tartaglia GG, Cavalli A, Pellarin R, Caflisch A (2005) Prediction Of Aggregation Rate And Aggregation-Prone Segments In Polypeptide Sequences. Protein Sci 14: 2723-2734.
    • (2005) Protein Sci , vol.14 , pp. 2723-2734
    • Tartaglia, G.G.1    Cavalli, A.2    Pellarin, R.3    Caflisch, A.4
  • 13
    • 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 OS, Goedert M, Serpell LC (2007) 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 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
  • 14
    • 63549101789 scopus 로고    scopus 로고
    • Bryan AW, Jr., Menke M, Cowen LJ, Lindquist SL, Berger B (2009) BETASCAN: Probable Beta-Amyloids Identified By Pairwise Probabilistic Analysis. Plos Comput Biol 5: E1000333.
    • Bryan AW, Jr., Menke M, Cowen LJ, Lindquist SL, Berger B (2009) BETASCAN: Probable Beta-Amyloids Identified By Pairwise Probabilistic Analysis. Plos Comput Biol 5: E1000333.
  • 15
    • 33645669165 scopus 로고    scopus 로고
    • Prediction Of Nucleating Sequences From Amyloidogenic Propensities Of Tau-Related Peptides
    • Rojas Quijano FA, Morrow D, Wise BM, Brancia FL, Goux WJ (2006) Prediction Of Nucleating Sequences From Amyloidogenic Propensities Of Tau-Related Peptides. Biochemistry 45: 4638-4652.
    • (2006) Biochemistry , vol.45 , pp. 4638-4652
    • Rojas Quijano, F.A.1    Morrow, D.2    Wise, B.M.3    Brancia, F.L.4    Goux, W.J.5
  • 16
    • 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 (2006) Insight Into The Structure Of Amyloid Fibrils From The Analysis Of Globular Proteins. Plos Comput Biol 2: E170.
    • (2006) Plos Comput Biol , vol.2
    • Trovato, A.1    Chiti, F.2    Maritan, A.3    Seno, F.4
  • 17
    • 33744973540 scopus 로고    scopus 로고
    • Interaction-Based Evaluation Of The Propensity For Amyloid Formation With Cross-Beta Structure
    • Saiki M, Konakahara T, Morii H (2006) Interaction-Based Evaluation Of The Propensity For Amyloid Formation With Cross-Beta Structure. Biochem Biophys Res Commun 343: 1262-1271.
    • (2006) Biochem Biophys Res Commun , vol.343 , pp. 1262-1271
    • Saiki, M.1    Konakahara, T.2    Morii, H.3
  • 20
    • 3342963982 scopus 로고    scopus 로고
    • Detecting Hidden Sequence Propensity For Amyloid Fibril Formation
    • Yoon S, Welsh WJ (2004) Detecting Hidden Sequence Propensity For Amyloid Fibril Formation. Protein Sci 13: 2149-2160.
    • (2004) Protein Sci , vol.13 , pp. 2149-2160
    • Yoon, S.1    Welsh, W.J.2
  • 21
    • 55449114544 scopus 로고    scopus 로고
    • Monsellier E, Ramazzotti M, Taddei N, Chiti F (2008) Aggregation Propensity Of The Human Proteome. Plos Comput Biol 4: E1000199.
    • Monsellier E, Ramazzotti M, Taddei N, Chiti F (2008) Aggregation Propensity Of The Human Proteome. Plos Comput Biol 4: E1000199.
  • 22
    • 4143133235 scopus 로고    scopus 로고
    • A Comparative Study Of The Relationship Between Protein Structure And Beta-Aggregation In Globular And Intrinsically Disordered Proteins
    • Linding R, Schymkowitz J, Rousseau F, Diella F, Serrano L (2004) A Comparative Study Of The Relationship Between Protein Structure And Beta-Aggregation In Globular And Intrinsically Disordered Proteins. J Mol Biol 342: 345-353.
    • (2004) J Mol Biol , vol.342 , pp. 345-353
    • Linding, R.1    Schymkowitz, J.2    Rousseau, F.3    Diella, F.4    Serrano, L.5
  • 23
    • 34249893672 scopus 로고    scopus 로고
    • Computational Analysis Of The S. Cerevisiae Proteome Reveals The Function And Cellular Localization Of The Least And Most Amyloidogenic Proteins
    • Tartaglia GG, Caflisch A (2007) Computational Analysis Of The S. Cerevisiae Proteome Reveals The Function And Cellular Localization Of The Least And Most Amyloidogenic Proteins. Proteins 68: 273-278.
    • (2007) Proteins , vol.68 , pp. 273-278
    • Tartaglia, G.G.1    Caflisch, A.2
  • 24
    • 25844505513 scopus 로고    scopus 로고
    • Organism Complexity Anti-Correlates With Proteomic Beta-Aggregation Propensity
    • Tartaglia GG, Pellarin R, Cavalli A, Caflisch A (2005) Organism Complexity Anti-Correlates With Proteomic Beta-Aggregation Propensity. Protein Sci 14: 2735-2740.
    • (2005) Protein Sci , vol.14 , pp. 2735-2740
    • Tartaglia, G.G.1    Pellarin, R.2    Cavalli, A.3    Caflisch, A.4
  • 25
    • 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 NS, Aviles FX, Vendrell J, Ventura S (2006) Mutagenesis Of The Central Hydrophobic Cluster In Abeta42 Alzheimer's Peptide. Side-Chain Properties Correlate With Aggregation Propensities. Febs J 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
  • 26
    • 2442553006 scopus 로고    scopus 로고
    • Short Amino Acid Stretches Can Mediate Amyloid Formation In Globular Proteins: The Src Homology 3 (SH3) Case
    • Ventura S, Zurdo J, Narayanan S, Parreno M, Mangues R, et al. (2004) Short Amino Acid Stretches Can Mediate Amyloid Formation In Globular Proteins: The Src Homology 3 (SH3) Case. Proc Natl Acad Sci U S A 101: 7258-7263.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 7258-7263
    • Ventura, S.1    Zurdo, J.2    Narayanan, S.3    Parreno, M.4    Mangues, R.5
  • 27
    • 29444444251 scopus 로고    scopus 로고
    • How Evolutionary Pressure Against Protein Aggregation Shaped Chaperone Specificity
    • Rousseau F, Serrano L, Schymkowitz JW (2006) How Evolutionary Pressure Against Protein Aggregation Shaped Chaperone Specificity. J Mol Biol 355: 1037-1047.
    • (2006) J Mol Biol , vol.355 , pp. 1037-1047
    • Rousseau, F.1    Serrano, L.2    Schymkowitz, J.W.3
  • 30
    • 72949113219 scopus 로고    scopus 로고
    • Correlation Between Mrna Expression Levels And Protein Aggregation Propensities In Subcellular Localisations
    • Tartaglia GG, Vendruscolo M (2009) Correlation Between Mrna Expression Levels And Protein Aggregation Propensities In Subcellular Localisations. Mol Biosyst 5: 1873-1876.
    • (2009) Mol Biosyst , vol.5 , pp. 1873-1876
    • Tartaglia, G.G.1    Vendruscolo, M.2
  • 31
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant Protein Folding And Misfolding In Escherichia Coli
    • Baneyx F, Mujacic M (2004) Recombinant Protein Folding And Misfolding In Escherichia Coli. Nat Biotechnol 22: 1399-1408.
    • (2004) Nat Biotechnol , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 32
    • 33745991934 scopus 로고    scopus 로고
    • Protein Activity In Bacterial Inclusion Bodies Correlates With Predicted Aggregation Rates
    • De Groot NS, Ventura S (2006) Protein Activity In Bacterial Inclusion Bodies Correlates With Predicted Aggregation Rates. J Biotechnol 125: 110-113.
    • (2006) J Biotechnol , vol.125 , pp. 110-113
    • De Groot, N.S.1    Ventura, S.2
  • 33
    • 33750991319 scopus 로고    scopus 로고
    • Effect Of Temperature On Protein Quality In Bacterial Inclusion Bodies
    • De Groot NS, Ventura S (2006) Effect Of Temperature On Protein Quality In Bacterial Inclusion Bodies. FEBS Lett 580: 6471-6476.
    • (2006) FEBS Lett , vol.580 , pp. 6471-6476
    • De Groot, N.S.1    Ventura, S.2
  • 34
    • 15844431346 scopus 로고    scopus 로고
    • Psortb V.2.0: Expanded Prediction Of Bacterial Protein Subcellular Localization And Insights Gained From Comparative Proteome Analysis
    • Gardy JL, Laird MR, Chen F, Rey S, Walsh CJ, et al. (2005) Psortb V.2.0: Expanded Prediction Of Bacterial Protein Subcellular Localization And Insights Gained From Comparative Proteome Analysis. Bioinformatics 21: 617-623.
    • (2005) Bioinformatics , vol.21 , pp. 617-623
    • Gardy, J.L.1    Laird, M.R.2    Chen, F.3    Rey, S.4    Walsh, C.J.5
  • 35
  • 36
    • 0033664358 scopus 로고    scopus 로고
    • RNA Expression Analysis Using A 30 Base Pair Resolution Escherichia Coli Genome Array
    • Selinger DW, Cheung KJ, Mei R, Johansson EM, Richmond CS, et al. (2000) RNA Expression Analysis Using A 30 Base Pair Resolution Escherichia Coli Genome Array. Nat Biotechnol 18: 1262-1268.
    • (2000) Nat Biotechnol , vol.18 , pp. 1262-1268
    • Selinger, D.W.1    Cheung, K.J.2    Mei, R.3    Johansson, E.M.4    Richmond, C.S.5
  • 37
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially Modified Protein Abundance Index (Empai) For Estimation Of Absolute Protein Amount In Proteomics By The Number Of Sequenced Peptides Per Protein
    • Ishihama Y, Oda Y, Tabata T, Sato T, Nagasu T, et al. (2005) Exponentially Modified Protein Abundance Index (Empai) For Estimation Of Absolute Protein Amount In Proteomics By The Number Of Sequenced Peptides Per Protein. Mol Cell Proteomics 4: 1265-1272.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5
  • 38
    • 34547634728 scopus 로고    scopus 로고
    • Ph Of The Cytoplasm And Periplasm Of Escherichia Coli: Rapid Measurement By Green Fluorescent Protein Fluorimetry
    • Wilks JC, Slonczewski JL (2007) Ph Of The Cytoplasm And Periplasm Of Escherichia Coli: Rapid Measurement By Green Fluorescent Protein Fluorimetry. J Bacteriol 189: 5601-5607.
    • (2007) J Bacteriol , vol.189 , pp. 5601-5607
    • Wilks, J.C.1    Slonczewski, J.L.2
  • 39
    • 0037059069 scopus 로고    scopus 로고
    • Studies Of The Aggregation Of Mutant Proteins In Vitro Provide Insights Into The Genetics Of Amyloid Diseases
    • Chiti F, Calamai M, Taddei N, Stefani M, Ramponi G, et al. (2002) Studies Of The Aggregation Of Mutant Proteins In Vitro Provide Insights Into The Genetics Of Amyloid Diseases. Proc Natl Acad Sci U S A 99 Suppl 4: 16419-16426.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.SUPPL. 4 , pp. 16419-16426
    • Chiti, F.1    Calamai, M.2    Taddei, N.3    Stefani, M.4    Ramponi, G.5
  • 40
    • 35748957119 scopus 로고    scopus 로고
    • Thermal Aggregation Of Bovine Serum Albumin At Different Ph: Comparison With Human Serum Albumin
    • Vetri V, Librizzi F, Leone M, Militello V (2007) Thermal Aggregation Of Bovine Serum Albumin At Different Ph: Comparison With Human Serum Albumin. Eur Biophys J 36: 717-725.
    • (2007) Eur Biophys J , vol.36 , pp. 717-725
    • Vetri, V.1    Librizzi, F.2    Leone, M.3    Militello, V.4
  • 41
    • 1242271236 scopus 로고    scopus 로고
    • Aggregation Kinetics Of Bovine Serum Albumin Studied By FTIR Spectroscopy And Light Scattering
    • Militello V, Casarino C, Emanuele A, Giostra A, Pullara F, et al. (2004) Aggregation Kinetics Of Bovine Serum Albumin Studied By FTIR Spectroscopy And Light Scattering. Biophys Chem 107: 175-187.
    • (2004) Biophys Chem , vol.107 , pp. 175-187
    • Militello, V.1    Casarino, C.2    Emanuele, A.3    Giostra, A.4    Pullara, F.5
  • 42
    • 50049085538 scopus 로고    scopus 로고
    • Effects Of Surface-To-Volume Ratio Of Proteins On Hydrophilic Residues: Decrease In Occurrence And Increase In Buried Fraction
    • Shirota M, Ishida T, Kinoshita K (2008) Effects Of Surface-To-Volume Ratio Of Proteins On Hydrophilic Residues: Decrease In Occurrence And Increase In Buried Fraction. Protein Sci 17: 1596-1602.
    • (2008) Protein Sci , vol.17 , pp. 1596-1602
    • Shirota, M.1    Ishida, T.2    Kinoshita, K.3
  • 43
    • 34548174652 scopus 로고    scopus 로고
    • Supercharging Proteins Can Impart Unusual Resilience
    • Lawrence MS, Phillips KJ, Liu DR (2007) Supercharging Proteins Can Impart Unusual Resilience. J Am Chem Soc 129: 10110-10112.
    • (2007) J Am Chem Soc , vol.129 , pp. 10110-10112
    • Lawrence, M.S.1    Phillips, K.J.2    Liu, D.R.3
  • 44
    • 34948823398 scopus 로고    scopus 로고
    • Chemical Biology: More Charges Against Aggregation
    • Vendruscolo M, Dobson CM (2007) Chemical Biology: More Charges Against Aggregation. Nature 449: 555.
    • (2007) Nature , vol.449 , pp. 555
    • Vendruscolo, M.1    Dobson, C.M.2
  • 46
    • 0020475449 scopus 로고
    • A Simple Method For Displaying The Hydropathic Character Of A Protein
    • Kyte J, Doolittle RF (1982) A Simple Method For Displaying The Hydropathic Character Of A Protein. J Mol Biol 157: 105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 47
  • 48
    • 71149108056 scopus 로고    scopus 로고
    • Correlation Of Mrna And Protein In Complex Biological Samples
    • Maier T, Guell M, Serrano L (2009) Correlation Of Mrna And Protein In Complex Biological Samples. FEBS Lett 583: 3966-3973.
    • (2009) FEBS Lett , vol.583 , pp. 3966-3973
    • Maier, T.1    Guell, M.2    Serrano, L.3
  • 49
    • 0023650543 scopus 로고
    • The Codon Adaptation Index-A Measure Of Directional Synonymous Codon Usage Bias, And Its Potential Applications
    • Sharp PM, Li WH (1987) The Codon Adaptation Index-A Measure Of Directional Synonymous Codon Usage Bias, And Its Potential Applications. Nucleic Acids Res 15: 1281-1295.
    • (1987) Nucleic Acids Res , vol.15 , pp. 1281-1295
    • Sharp, P.M.1    Li, W.H.2
  • 50
    • 0038476173 scopus 로고    scopus 로고
    • Revisiting The Codon Adaptation Index From A Whole-Genome Perspective: Analyzing The Relationship Between Gene Expression And Codon Occurrence In Yeast Using A Variety Of Models
    • Jansen R, Bussemaker HJ, Gerstein M (2003) Revisiting The Codon Adaptation Index From A Whole-Genome Perspective: Analyzing The Relationship Between Gene Expression And Codon Occurrence In Yeast Using A Variety Of Models. Nucleic Acids Res 31: 2242-2251.
    • (2003) Nucleic Acids Res , vol.31 , pp. 2242-2251
    • Jansen, R.1    Bussemaker, H.J.2    Gerstein, M.3
  • 51
    • 64049102839 scopus 로고    scopus 로고
    • Tartaglia GG, Pechmann S, Dobson CM, Vendruscolo M (2009) A Relationship Between Mrna Expression Levels And Protein Solubility In E. Coli. J Mol Biol 388: 381-389.
    • Tartaglia GG, Pechmann S, Dobson CM, Vendruscolo M (2009) A Relationship Between Mrna Expression Levels And Protein Solubility In E. Coli. J Mol Biol 388: 381-389.
  • 52
    • 34247882072 scopus 로고    scopus 로고
    • Life On The Edge: A Link Between Gene Expression Levels And Aggregation Rates Of Human Proteins
    • Tartaglia GG, Pechmann S, Dobson CM, Vendruscolo M (2007) Life On The Edge: A Link Between Gene Expression Levels And Aggregation Rates Of Human Proteins. Trends Biochem Sci 32: 204-206.
    • (2007) Trends Biochem Sci , vol.32 , pp. 204-206
    • Tartaglia, G.G.1    Pechmann, S.2    Dobson, C.M.3    Vendruscolo, M.4
  • 53
    • 16244386921 scopus 로고    scopus 로고
    • The Optimal Size Of A Globular Protein Domain: A Simple Sphere-Packing Model
    • Shen M-Y, Davis FP, Sali A (2005) The Optimal Size Of A Globular Protein Domain: A Simple Sphere-Packing Model. Chemical Physics Letters 405: 224-228.
    • (2005) Chemical Physics Letters , vol.405 , pp. 224-228
    • Shen, M.-Y.1    Davis, F.P.2    Sali, A.3
  • 54
    • 0017294711 scopus 로고
    • Accessible Area, Packing Volumes And Interaction Surfaces Of Globular Proteins
    • Teller DC (1976) Accessible Area, Packing Volumes And Interaction Surfaces Of Globular Proteins. Nature 260: 729-731.
    • (1976) Nature , vol.260 , pp. 729-731
    • Teller, D.C.1
  • 55
    • 0347949638 scopus 로고    scopus 로고
    • On Hydrophobicity And Conformational Specificity In Proteins
    • Sandelin E (2004) On Hydrophobicity And Conformational Specificity In Proteins. Biophys J 86: 23-30.
    • (2004) Biophys J , vol.86 , pp. 23-30
    • Sandelin, E.1
  • 56
    • 0033738980 scopus 로고    scopus 로고
    • On Hydrophobicity Correlations In Protein Chains
    • Irback A, Sandelin E (2000) On Hydrophobicity Correlations In Protein Chains. Biophys J 79: 2252-2258.
    • (2000) Biophys J , vol.79 , pp. 2252-2258
    • Irback, A.1    Sandelin, E.2
  • 58
    • 0035964177 scopus 로고    scopus 로고
    • Polar Residues In The Protein Core Of Escherichia Coli Thioredoxin Are Important For Fold Specificity
    • Bolon DN, Mayo SL (2001) Polar Residues In The Protein Core Of Escherichia Coli Thioredoxin Are Important For Fold Specificity. Biochemistry 40: 10047-10053.
    • (2001) Biochemistry , vol.40 , pp. 10047-10053
    • Bolon, D.N.1    Mayo, S.L.2
  • 59
    • 34347376906 scopus 로고    scopus 로고
    • The Relationships Between The Isoelectric Point And: Length Of Proteins, Taxonomy And Ecology Of Organisms
    • Kiraga J, Mackiewicz P, Mackiewicz D, Kowalczuk M, Biecek P, et al. (2007) The Relationships Between The Isoelectric Point And: Length Of Proteins, Taxonomy And Ecology Of Organisms. BMC Genomics 8: 163.
    • (2007) BMC Genomics , vol.8 , pp. 163
    • Kiraga, J.1    Mackiewicz, P.2    Mackiewicz, D.3    Kowalczuk, M.4    Biecek, P.5
  • 60
    • 0042510944 scopus 로고    scopus 로고
    • Contact Order Revisited: Influence Of Protein Size On The Folding Rate
    • Ivankov DN, Garbuzynskiy SO, Alm E, Plaxco KW, Baker D, et al. (2003) Contact Order Revisited: Influence Of Protein Size On The Folding Rate. Protein Sci 12: 2057-2062.
    • (2003) Protein Sci , vol.12 , pp. 2057-2062
    • Ivankov, D.N.1    Garbuzynskiy, S.O.2    Alm, E.3    Plaxco, K.W.4    Baker, D.5
  • 61
    • 0034194396 scopus 로고    scopus 로고
    • Chaperone Substrates Inside The Cell
    • Ellis RJ (2000) Chaperone Substrates Inside The Cell. Trends Biochem Sci 25: 210-212.
    • (2000) Trends Biochem Sci , vol.25 , pp. 210-212
    • Ellis, R.J.1
  • 62
    • 0033521588 scopus 로고    scopus 로고
    • In Vivo Newly Translated Polypeptides Are Sequestered In A Protected Folding Environment
    • Thulasiraman V, Yang CF, Frydman J (1999) In Vivo Newly Translated Polypeptides Are Sequestered In A Protected Folding Environment. EMBO J 18: 85-95.
    • (1999) EMBO J , vol.18 , pp. 85-95
    • Thulasiraman, V.1    Yang, C.F.2    Frydman, J.3
  • 63
    • 0033578722 scopus 로고    scopus 로고
    • Myosin II Folding Is Mediated By A Molecular Chaperonin
    • Srikakulam R, Winkelmann DA (1999) Myosin II Folding Is Mediated By A Molecular Chaperonin. J Biol Chem 274: 27265-27273.
    • (1999) J Biol Chem , vol.274 , pp. 27265-27273
    • Srikakulam, R.1    Winkelmann, D.A.2
  • 64
    • 34547631623 scopus 로고    scopus 로고
    • Prevention Of Amyloid-Like Aggregation As A Driving Force Of Protein Evolution
    • Monsellier E, Chiti F (2007) Prevention Of Amyloid-Like Aggregation As A Driving Force Of Protein Evolution. EMBO Rep 8: 737-742.
    • (2007) EMBO Rep , vol.8 , pp. 737-742
    • Monsellier, E.1    Chiti, F.2
  • 66
    • 0141504252 scopus 로고    scopus 로고
    • Experimental Determination And System Level Analysis Of Essential Genes In Escherichia Coli MG1655
    • Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, et al. (2003) Experimental Determination And System Level Analysis Of Essential Genes In Escherichia Coli MG1655. J Bacteriol 185: 5673-5684.
    • (2003) J Bacteriol , vol.185 , pp. 5673-5684
    • Gerdes, S.Y.1    Scholle, M.D.2    Campbell, J.W.3    Balazsi, G.4    Ravasz, E.5
  • 67
    • 31544450286 scopus 로고    scopus 로고
    • Construction Of Escherichia Coli K-12 In-Frame, Single-Gene Knockout Mutants: The Keio Collection
    • Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, et al. (2006) Construction Of Escherichia Coli K-12 In-Frame, Single-Gene Knockout Mutants: The Keio Collection. Mol Syst Biol 2: 2006 0008.
    • (2006) Mol Syst Biol , vol.2 , pp. 0008
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5
  • 68
    • 47649121227 scopus 로고    scopus 로고
    • Natural Selection Against Protein Aggregation On Self-Interacting And Essential Proteins In Yeast, Fly, And Worm
    • Chen Y, Dokholyan NV (2008) Natural Selection Against Protein Aggregation On Self-Interacting And Essential Proteins In Yeast, Fly, And Worm. Mol Biol Evol 25: 1530-1533.
    • (2008) Mol Biol Evol , vol.25 , pp. 1530-1533
    • Chen, Y.1    Dokholyan, N.V.2
  • 69
    • 33645753974 scopus 로고    scopus 로고
    • Conservation Of Intrinsic Disorder In Protein Domains And Families: II. Functions Of Conserved Disorder
    • Chen JW, Romero P, Uversky VN, Dunker AK (2006) Conservation Of Intrinsic Disorder In Protein Domains And Families: II. Functions Of Conserved Disorder. J Proteome Res 5: 888-898.
    • (2006) J Proteome Res , vol.5 , pp. 888-898
    • Chen, J.W.1    Romero, P.2    Uversky, V.N.3    Dunker, A.K.4
  • 71
    • 0034066471 scopus 로고    scopus 로고
    • Membrane Proteins And Proteomics: Un Amour Impossible?
    • Santoni V, Molloy M, Rabilloud T (2000) Membrane Proteins And Proteomics: Un Amour Impossible? Electrophoresis 21: 1054-1070.
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 72
    • 0036810483 scopus 로고    scopus 로고
    • Protein Folding And Degradation In Bacteria: To Degrade Or Not To Degrade? That Is The Question
    • Dougan DA, Mogk A, Bukau B (2002) Protein Folding And Degradation In Bacteria: To Degrade Or Not To Degrade? That Is The Question. Cell Mol Life Sci 59: 1607-1616.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1607-1616
    • Dougan, D.A.1    Mogk, A.2    Bukau, B.3
  • 73
    • 1642410141 scopus 로고    scopus 로고
    • Periplasmic Proteins Of Escherichia Coli Are Highly Resistant To Aggregation: Reappraisal For Roles Of Molecular Chaperones In Periplasm
    • Liu Y, Fu X, Shen J, Zhang H, Hong W, et al. (2004) Periplasmic Proteins Of Escherichia Coli Are Highly Resistant To Aggregation: Reappraisal For Roles Of Molecular Chaperones In Periplasm. Biochem Biophys Res Commun 316: 795-801.
    • (2004) Biochem Biophys Res Commun , vol.316 , pp. 795-801
    • Liu, Y.1    Fu, X.2    Shen, J.3    Zhang, H.4    Hong, W.5
  • 74
    • 0035910270 scopus 로고    scopus 로고
    • Predicting Transmembrane Protein Topology With A Hidden Markov Model: Application To Complete Genomes
    • Krogh A, Larsson B, Von Heijne G, Sonnhammer EL (2001) Predicting Transmembrane Protein Topology With A Hidden Markov Model: Application To Complete Genomes. J Mol Biol 305: 567-580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 75
    • 9144257282 scopus 로고    scopus 로고
    • The Funcat, A Functional Annotation Scheme For Systematic Classification Of Proteins From Whole Genomes
    • Ruepp A, Zollner A, Maier D, Albermann K, Hani J, et al. (2004) The Funcat, A Functional Annotation Scheme For Systematic Classification Of Proteins From Whole Genomes. Nucleic Acids Res 32: 5539-5545.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5539-5545
    • Ruepp, A.1    Zollner, A.2    Maier, D.3    Albermann, K.4    Hani, J.5
  • 78
    • 62949231327 scopus 로고    scopus 로고
    • Hydrophobic Peptides: Novel Regulators Within Bacterial Membrane
    • Alix E, Blanc-Potard AB (2009) Hydrophobic Peptides: Novel Regulators Within Bacterial Membrane. Mol Microbiol 72: 5-11.
    • (2009) Mol Microbiol , vol.72 , pp. 5-11
    • Alix, E.1    Blanc-Potard, A.B.2
  • 79
    • 0026779245 scopus 로고
    • Crystal Structures Explain Functional Properties Of Two E. Coli Porins
    • Cowan SW, Schirmer T, Rummel G, Steiert M, Ghosh R, et al. (1992) Crystal Structures Explain Functional Properties Of Two E. Coli Porins. Nature 358: 727-733.
    • (1992) Nature , vol.358 , pp. 727-733
    • Cowan, S.W.1    Schirmer, T.2    Rummel, G.3    Steiert, M.4    Ghosh, R.5
  • 80
    • 0031857538 scopus 로고    scopus 로고
    • General And Specific Porins From Bacterial Outer Membranes
    • Schirmer T (1998) General And Specific Porins From Bacterial Outer Membranes. J Struct Biol 121: 101-109.
    • (1998) J Struct Biol , vol.121 , pp. 101-109
    • Schirmer, T.1
  • 81
    • 60749102331 scopus 로고    scopus 로고
    • Membrane Protein Architects: The Role Of The BAM Complex In Outer Membrane Protein Assembly
    • Knowles TJ, Scott-Tucker A, Overduin M, Henderson IR (2009) Membrane Protein Architects: The Role Of The BAM Complex In Outer Membrane Protein Assembly. Nat Rev Microbiol 7: 206-214.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 206-214
    • Knowles, T.J.1    Scott-Tucker, A.2    Overduin, M.3    Henderson, I.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.