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Volumn 8, Issue 7, 2013, Pages

Macromolecular Crowding as a Suppressor of Human IAPP Fibril Formation and Cytotoxicity

Author keywords

[No Author keywords available]

Indexed keywords

AMYLIN;

EID: 84880844306     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0069652     Document Type: Article
Times cited : (57)

References (56)
  • 1
    • 0035815743 scopus 로고    scopus 로고
    • The Influence of Macromolecular Crowding and Macromolecular Confinement on Biochemical Reactions in Physiological Media
    • Minton AP, (2001) The Influence of Macromolecular Crowding and Macromolecular Confinement on Biochemical Reactions in Physiological Media. J Biol Chem 276: 10577-10580.
    • (2001) J Biol Chem , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 2
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: obvious but underappreciated
    • Ellis RJ, (2001) Macromolecular crowding: obvious but underappreciated. Trends Biochem Sci 26: 597-604.
    • (2001) Trends Biochem Sci , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 3
    • 77950792003 scopus 로고    scopus 로고
    • Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm
    • McGuffee SR, Elcock AH, (2010) Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm. PLoS Comput Biol 6: e1000694.
    • (2010) PLoS Comput Biol , vol.6
    • McGuffee, S.R.1    Elcock, A.H.2
  • 4
    • 77955699308 scopus 로고    scopus 로고
    • Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria
    • Jiao M, Li H-T, Chen J, Minton AP, Liang Y, (2010) Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria. Biophys J 99: 914-923.
    • (2010) Biophys J , vol.99 , pp. 914-923
    • Jiao, M.1    Li, H.-T.2    Chen, J.3    Minton, A.P.4    Liang, Y.5
  • 5
    • 84865735110 scopus 로고    scopus 로고
    • Contrasting factors on the kinetic path to protein complex formation diminish the effects of crowding agents
    • Phillip Y, Harel M, Khait R, Qin S, Zhou H-X, et al. (2012) Contrasting factors on the kinetic path to protein complex formation diminish the effects of crowding agents. Biophys J 103: 1011-1019.
    • (2012) Biophys J , vol.103 , pp. 1011-1019
    • Phillip, Y.1    Harel, M.2    Khait, R.3    Qin, S.4    Zhou, H.-X.5
  • 6
    • 0032762645 scopus 로고    scopus 로고
    • Crowding Effects on EcoRV Kinetics and Binding
    • Wenner JR, Bloomfield VA, (1999) Crowding Effects on EcoRV Kinetics and Binding. Biophys J 77: 3234-3241.
    • (1999) Biophys J , vol.77 , pp. 3234-3241
    • Wenner, J.R.1    Bloomfield, V.A.2
  • 8
    • 0038043286 scopus 로고    scopus 로고
    • Small-angle X-ray scattering studies of moderately concentrated dextran solution
    • Hirata Y, Sano Y, Aoki M, Shohji H, Katoh S, et al. (2003) Small-angle X-ray scattering studies of moderately concentrated dextran solution. Carbohydr Polym 53: 331-335.
    • (2003) Carbohydr Polym , vol.53 , pp. 331-335
    • Hirata, Y.1    Sano, Y.2    Aoki, M.3    Shohji, H.4    Katoh, S.5
  • 9
    • 38149048416 scopus 로고    scopus 로고
    • The Effective Hard Particle Model Provides a Simple, Robust, and Broadly Applicable Description of Nonideal Behavior in Concentrated Solutions of Bovine Serum Albumin and Other Nonassociating Proteins
    • Minton AP, (2007) The Effective Hard Particle Model Provides a Simple, Robust, and Broadly Applicable Description of Nonideal Behavior in Concentrated Solutions of Bovine Serum Albumin and Other Nonassociating Proteins. J Pharm Sci 96: 3466-3469.
    • (2007) J Pharm Sci , vol.96 , pp. 3466-3469
    • Minton, A.P.1
  • 10
    • 0034349193 scopus 로고    scopus 로고
    • Protein-Protein Interactions in Aqueous Ammonium Sulfate Solutions. Lysozyme and Bovine Serum Albumin (BSA)
    • Moon YU, Curtis RA, Anderson CO, Blanch HW, Prausnitz JM, (2000) Protein-Protein Interactions in Aqueous Ammonium Sulfate Solutions. Lysozyme and Bovine Serum Albumin (BSA). J Solution Chem 29: 699-717.
    • (2000) J Solution Chem , vol.29 , pp. 699-717
    • Moon, Y.U.1    Curtis, R.A.2    Anderson, C.O.3    Blanch, H.W.4    Prausnitz, J.M.5
  • 11
    • 0035853141 scopus 로고    scopus 로고
    • Direct observation of the enhancement of noncooperative protein self-assembly by macromolecular crowding: Indefinite linear self-association of bacterial cell division protein FtsZ
    • Rivas G, Fernández JA, Minton AP, (2001) Direct observation of the enhancement of noncooperative protein self-assembly by macromolecular crowding: Indefinite linear self-association of bacterial cell division protein FtsZ. Proc Natl Acad Sci U S A 98: 3150-3155.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 3150-3155
    • Rivas, G.1    Fernández, J.A.2    Minton, A.P.3
  • 12
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM, (2003) Protein folding and misfolding. Nature 426: 884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 13
    • 0025753852 scopus 로고
    • The Molecular Pathology of Alzheimer's Disease
    • Selkoe DJ, (1991) The Molecular Pathology of Alzheimer's Disease. Neuron 6: 487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 14
    • 79954535899 scopus 로고    scopus 로고
    • Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus
    • Westermark P, Andersson A, Westermark GT, (2011) Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus. Physiol Rev 91: 795-826.
    • (2011) Physiol Rev , vol.91 , pp. 795-826
    • Westermark, P.1    Andersson, A.2    Westermark, G.T.3
  • 15
    • 77953442000 scopus 로고    scopus 로고
    • Interaction of hIAPP with Model Raft Membranes and Pancreatic β-Cells: Cytotoxicity of hIAPP Oligomers
    • Weise K, Radovan D, Gohlke A, Opitz N, Winter R, (2010) Interaction of hIAPP with Model Raft Membranes and Pancreatic β-Cells: Cytotoxicity of hIAPP Oligomers. ChemBioChem 11: 1280-1290.
    • (2010) ChemBioChem , vol.11 , pp. 1280-1290
    • Weise, K.1    Radovan, D.2    Gohlke, A.3    Opitz, N.4    Winter, R.5
  • 16
    • 84863983553 scopus 로고    scopus 로고
    • The Effect of Aβ on IAPP Aggregation in the Presence of an Isolated β-Cell Membrane
    • Seeliger J, Weise K, Opitz N, Winter R, (2012) The Effect of Aβ on IAPP Aggregation in the Presence of an Isolated β-Cell Membrane. J Mol Biol 421: 348-363.
    • (2012) J Mol Biol , vol.421 , pp. 348-363
    • Seeliger, J.1    Weise, K.2    Opitz, N.3    Winter, R.4
  • 18
    • 4544252011 scopus 로고    scopus 로고
    • The effect of macromolecular crowding on protein aggregation and amyloid fibril formation
    • Munishkina LA, Cooper EM, Uversky VN, Fink AL, (2004) The effect of macromolecular crowding on protein aggregation and amyloid fibril formation. J Mol Recognit 17: 456-464.
    • (2004) J Mol Recognit , vol.17 , pp. 456-464
    • Munishkina, L.A.1    Cooper, E.M.2    Uversky, V.N.3    Fink, A.L.4
  • 19
    • 50149096820 scopus 로고    scopus 로고
    • Guiding Protein Aggregation with Macromolecular Crowding
    • Munishkina LA, Ahmad A, Fink AL, Uversky VN, (2008) Guiding Protein Aggregation with Macromolecular Crowding. Biochemistry 47: 8993-9006.
    • (2008) Biochemistry , vol.47 , pp. 8993-9006
    • Munishkina, L.A.1    Ahmad, A.2    Fink, A.L.3    Uversky, V.N.4
  • 20
    • 0037040878 scopus 로고    scopus 로고
    • Macromolecular Crowding Accelerates Amyloid Formation by Human Apolipoprotein C-II
    • Hatters DM, Minton AP, Howlett GJ, (2002) Macromolecular Crowding Accelerates Amyloid Formation by Human Apolipoprotein C-II. J Biol Chem 277: 7824-7830.
    • (2002) J Biol Chem , vol.277 , pp. 7824-7830
    • Hatters, D.M.1    Minton, A.P.2    Howlett, G.J.3
  • 21
    • 84860446148 scopus 로고    scopus 로고
    • The Contrasting Effect of Macromolecular Crowding on Amyloid Fibril Formation
    • Ma Q, Fan J-B, Zhou Z, Zhou B-R, Meng S-R, et al. (2012) The Contrasting Effect of Macromolecular Crowding on Amyloid Fibril Formation. PloS ONE 7: e36288.
    • (2012) PloS ONE , vol.7
    • Ma, Q.1    Fan, J.-B.2    Zhou, Z.3    Zhou, B.-R.4    Meng, S.-R.5
  • 22
    • 71049123175 scopus 로고    scopus 로고
    • Crowded Cell-like Environment Accelerates the Nucleation Step of Amyloidogenic Protein Misfolding
    • Zhou Z, Fan J-B, Zhu H-L, Shewmaker F, Yan X, et al. (2009) Crowded Cell-like Environment Accelerates the Nucleation Step of Amyloidogenic Protein Misfolding. J Biol Chem 284: 30148-30158.
    • (2009) J Biol Chem , vol.284 , pp. 30148-30158
    • Zhou, Z.1    Fan, J.-B.2    Zhu, H.-L.3    Shewmaker, F.4    Yan, X.5
  • 23
    • 79251538929 scopus 로고    scopus 로고
    • Crowding Alone Cannot Account for Cosolute Effect on Amyloid Aggregation
    • Sukenik S, Politi R, Ziserman L, Danino D, Friedler A, et al. (2011) Crowding Alone Cannot Account for Cosolute Effect on Amyloid Aggregation. PloS ONE 6: e15608.
    • (2011) PloS ONE , vol.6
    • Sukenik, S.1    Politi, R.2    Ziserman, L.3    Danino, D.4    Friedler, A.5
  • 24
    • 84870015758 scopus 로고    scopus 로고
    • Effects of Molecular Crowding on the Dynamics of Intrinsically Disordered Proteins
    • Cino EA, Karttunen M, Choy W-Y, (2012) Effects of Molecular Crowding on the Dynamics of Intrinsically Disordered Proteins. PloS ONE 7: e49876.
    • (2012) PloS ONE , vol.7
    • Cino, E.A.1    Karttunen, M.2    Choy, W.-Y.3
  • 25
    • 84868325436 scopus 로고    scopus 로고
    • Combined Effects of Agitation, Macromolecular Crowding, and Interfaces on Amyloidogenesis
    • Lee CF, Bird S, Shaw M, Jean L, Vaux DJ, (2012) Combined Effects of Agitation, Macromolecular Crowding, and Interfaces on Amyloidogenesis. J Biol Chem 287: 38006-38019.
    • (2012) J Biol Chem , vol.287 , pp. 38006-38019
    • Lee, C.F.1    Bird, S.2    Shaw, M.3    Jean, L.4    Vaux, D.J.5
  • 26
    • 0023579739 scopus 로고
    • Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients
    • Cooper GJS, Willis AC, Clark A, Turner RC, Sim RB, et al. (1987) Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci U S A 84: 8628-8632.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 8628-8632
    • Cooper, G.J.S.1    Willis, A.C.2    Clark, A.3    Turner, R.C.4    Sim, R.B.5
  • 27
    • 0023192941 scopus 로고
    • Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells
    • Westermark P, Wernstedt C, Wilander E, Hayden DW, O'Brien TD, et al. (1987) Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc Natl Acad Sci U S A 84: 3881-3885.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 3881-3885
    • Westermark, P.1    Wernstedt, C.2    Wilander, E.3    Hayden, D.W.4    O'Brien, T.D.5
  • 28
    • 44649150510 scopus 로고    scopus 로고
    • Recent Insights in Islet Amyloid Polypeptide-Induced Membrane Disruption and Its Role in β-Cell Death in Type 2 Diabetes Mellitus
    • Article ID 421287
    • Khemtémourian L, Killian JA, Höppener JWM, Engel MFM, (2008) Recent Insights in Islet Amyloid Polypeptide-Induced Membrane Disruption and Its Role in β-Cell Death in Type 2 Diabetes Mellitus. Exp Diabetes Res pp. Article ID 421287.
    • (2008) Exp Diabetes Res
    • Khemtémourian, L.1    Killian, J.A.2    Höppener, J.W.M.3    Engel, M.F.M.4
  • 29
    • 67349142581 scopus 로고    scopus 로고
    • Membrane permeabilization by Islet Amyloid Polypeptide
    • Engel MFM, (2009) Membrane permeabilization by Islet Amyloid Polypeptide. Chem Phys Lipids 160: 1-10.
    • (2009) Chem Phys Lipids , vol.160 , pp. 1-10
    • Engel, M.F.M.1
  • 30
    • 84880787353 scopus 로고    scopus 로고
    • Interaction of hIAPP and Its Precursors with Model and Biological Membranes
    • Jelinek R, editor, Weinheim, Germany: Wiley-VCH
    • Weise K, Mishra R, Jha S, Sellin D, Radovan D, et al. (2011) Interaction of hIAPP and Its Precursors with Model and Biological Membranes. In: Jelinek R, editor. Lipids and Cellular Membranes in Amyloid Diseases. Weinheim, Germany: Wiley-VCH. pp. 93-120.
    • (2011) Lipids and Cellular Membranes in Amyloid Diseases , pp. 93-120
    • Weise, K.1    Mishra, R.2    Jha, S.3    Sellin, D.4    Radovan, D.5
  • 32
    • 67349227494 scopus 로고    scopus 로고
    • Amyloidogenic Propensities and Conformational Properties of ProIAPP and IAPP in the Presence of Lipid Bilayer Membranes
    • Jha S, Sellin D, Seidel R, Winter R, (2009) Amyloidogenic Propensities and Conformational Properties of ProIAPP and IAPP in the Presence of Lipid Bilayer Membranes. J Mol Biol 389: 907-920.
    • (2009) J Mol Biol , vol.389 , pp. 907-920
    • Jha, S.1    Sellin, D.2    Seidel, R.3    Winter, R.4
  • 33
    • 79955954237 scopus 로고    scopus 로고
    • Comparing the structural properties of human and rat islet amyloid polypeptide by MD computer simulations
    • Andrews MN, Winter R, (2011) Comparing the structural properties of human and rat islet amyloid polypeptide by MD computer simulations. Biophys Chem 156: 43-50.
    • (2011) Biophys Chem , vol.156 , pp. 43-50
    • Andrews, M.N.1    Winter, R.2
  • 34
    • 77953710075 scopus 로고    scopus 로고
    • Suppression of IAPP fibrillation at anionic lipid membranes via IAPP-derived amyloid inhibitors and insulin
    • Sellin D, Yan L-M, Kapurniotu A, Winter R, (2010) Suppression of IAPP fibrillation at anionic lipid membranes via IAPP-derived amyloid inhibitors and insulin. Biophys Chem 150: 73-79.
    • (2010) Biophys Chem , vol.150 , pp. 73-79
    • Sellin, D.1    Yan, L.-M.2    Kapurniotu, A.3    Winter, R.4
  • 35
    • 11144222595 scopus 로고    scopus 로고
    • The binding of thioflavin-T to amyloid fibrils: localisation and implications
    • Krebs MRH, Bromley EHC, Donald AM, (2005) The binding of thioflavin-T to amyloid fibrils: localisation and implications. J Struct Biol 149: 30-37.
    • (2005) J Struct Biol , vol.149 , pp. 30-37
    • Krebs, M.R.H.1    Bromley, E.H.C.2    Donald, A.M.3
  • 36
    • 70449702059 scopus 로고    scopus 로고
    • Mechanism of amyloidogenesis: nucleation-dependent fibrillation versus double-concerted fibrillation
    • Bhak G, Choe Y-J, Paik SR, (2009) Mechanism of amyloidogenesis: nucleation-dependent fibrillation versus double-concerted fibrillation. BMB reports 42: 541-551.
    • (2009) BMB Reports , vol.42 , pp. 541-551
    • Bhak, G.1    Choe, Y.-J.2    Paik, S.R.3
  • 37
    • 70349560017 scopus 로고    scopus 로고
    • NMR Spectroscopic Investigation of Early Events in IAPP Amyloid Fibril Formation
    • Mishra R, Geyer M, Winter R, (2009) NMR Spectroscopic Investigation of Early Events in IAPP Amyloid Fibril Formation. ChemBioChem 10: 1769-1772.
    • (2009) ChemBioChem , vol.10 , pp. 1769-1772
    • Mishra, R.1    Geyer, M.2    Winter, R.3
  • 38
    • 77958454277 scopus 로고    scopus 로고
    • Stable and Metastable States of Human Amylin in Solution
    • Reddy AS, Wang L, Singh S, Ling YL, Buchanan L, et al. (2010) Stable and Metastable States of Human Amylin in Solution. Biophys J 99: 2208-2216.
    • (2010) Biophys J , vol.99 , pp. 2208-2216
    • Reddy, A.S.1    Wang, L.2    Singh, S.3    Ling, Y.L.4    Buchanan, L.5
  • 39
  • 40
    • 84985735713 scopus 로고
    • Excluded Volume as a Determinant of Macromolecular Structure and Reactivity
    • Minton AP, (1981) Excluded Volume as a Determinant of Macromolecular Structure and Reactivity. Biopolymers 20: 2093-2120.
    • (1981) Biopolymers , vol.20 , pp. 2093-2120
    • Minton, A.P.1
  • 41
    • 0027318513 scopus 로고
    • Macromolecular Crowding: Biochemical, Biophysical, and Physiological Consequences
    • Zimmerman SB, Minton AP, (1993) Macromolecular Crowding: Biochemical, Biophysical, and Physiological Consequences. Annu Rev Biophys Biomol Struct 22: 27-65.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 42
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • Minton AP, (2000) Implications of macromolecular crowding for protein assembly. Curr Opin Struct Biol 10: 34-39.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 43
    • 79952745066 scopus 로고    scopus 로고
    • Modest Protein-Crowder Attractive Interactions Can Counteract Enhancement of Protein Association by Intermolecular Excluded Volume Interactions
    • Rosen J, Kim YC, Mittal J, (2011) Modest Protein-Crowder Attractive Interactions Can Counteract Enhancement of Protein Association by Intermolecular Excluded Volume Interactions. J Phys Chem B 115: 2683-2689.
    • (2011) J Phys Chem B , vol.115 , pp. 2683-2689
    • Rosen, J.1    Kim, Y.C.2    Mittal, J.3
  • 44
    • 84864479275 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on the structural stability of human α-lactalbumin
    • Zhang D, Wu L, Chen J, Liang Y, (2012) Effects of macromolecular crowding on the structural stability of human α-lactalbumin. Acta Biochim Biophys Sin 44: 703-711.
    • (2012) Acta Biochim Biophys Sin , vol.44 , pp. 703-711
    • Zhang, D.1    Wu, L.2    Chen, J.3    Liang, Y.4
  • 45
    • 84872904773 scopus 로고    scopus 로고
    • Quantitative Assessment of the Relative Contributions of Steric Repulsion and Chemical Interactions to Macromolecular Crowding
    • Minton AP, (2013) Quantitative Assessment of the Relative Contributions of Steric Repulsion and Chemical Interactions to Macromolecular Crowding. Biopolymers 99: 239-244.
    • (2013) Biopolymers , vol.99 , pp. 239-244
    • Minton, A.P.1
  • 46
    • 84862296190 scopus 로고    scopus 로고
    • Serum Albumin Prevents Protein Aggregation and Amyloid Formation and Retains Chaperone-like Activity in the Presence of Physiological Ligands
    • Finn TE, Nunez AC, Sunde M, Easterbrook-Smith SB, (2012) Serum Albumin Prevents Protein Aggregation and Amyloid Formation and Retains Chaperone-like Activity in the Presence of Physiological Ligands. J Biol Chem 287: 21530-21540.
    • (2012) J Biol Chem , vol.287 , pp. 21530-21540
    • Finn, T.E.1    Nunez, A.C.2    Sunde, M.3    Easterbrook-Smith, S.B.4
  • 48
    • 67651098677 scopus 로고    scopus 로고
    • Aggregation of Amyloidogenic Peptides near Hydrophobic and Hydrophilic Surfaces
    • Brovchenko I, Singh G, Winter R, (2009) Aggregation of Amyloidogenic Peptides near Hydrophobic and Hydrophilic Surfaces. Langmuir 25: 8111-8116.
    • (2009) Langmuir , vol.25 , pp. 8111-8116
    • Brovchenko, I.1    Singh, G.2    Winter, R.3
  • 49
    • 0842291578 scopus 로고    scopus 로고
    • Glucose Sensitivity and Metabolism-Secretion Coupling Studied during Two-Year Continuous Culture in INS-1E Insulinoma Cells
    • Merglen A, Theander S, Rubi B, Chaffard G, Wollheim CB, et al. (2004) Glucose Sensitivity and Metabolism-Secretion Coupling Studied during Two-Year Continuous Culture in INS-1E Insulinoma Cells. Endocrinology 145: 667-678.
    • (2004) Endocrinology , vol.145 , pp. 667-678
    • Merglen, A.1    Theander, S.2    Rubi, B.3    Chaffard, G.4    Wollheim, C.B.5
  • 50
    • 0035918550 scopus 로고    scopus 로고
    • Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism
    • Nielsen L, Khurana R, Coats A, Frokjaer S, Brange J, et al. (2001) Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism. Biochemistry 40: 6036-6046.
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5
  • 51
    • 0031861817 scopus 로고    scopus 로고
    • Analysis of fluorophore diffusion by continuous distributions of diffusion coefficients: application to photobleaching measurements of multicomponent and anomalous diffusion
    • Periasamy N, Verkman a S, (1998) Analysis of fluorophore diffusion by continuous distributions of diffusion coefficients: application to photobleaching measurements of multicomponent and anomalous diffusion. Biophys J 75: 557-567.
    • (1998) Biophys J , vol.75 , pp. 557-567
    • Periasamy, N.1    Verkman, S.2
  • 52
    • 0024006767 scopus 로고
    • Tracer diffusion of globular proteins in concentrated protein solutions
    • Muramatsu N, Minton AP, (1988) Tracer diffusion of globular proteins in concentrated protein solutions. Proc Natl Acad Sci U S A 85: 2984-2988.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 2984-2988
    • Muramatsu, N.1    Minton, A.P.2
  • 53
    • 36849107354 scopus 로고
    • Measurement of the Rotational Diffusion Coefficient of Lysozyme by Depolarized Light Scattering: Configuration of Lysozyme in Solution
    • Dubin SB, (1971) Measurement of the Rotational Diffusion Coefficient of Lysozyme by Depolarized Light Scattering: Configuration of Lysozyme in Solution. J Chem Phys 54: 5158-5164.
    • (1971) J Chem Phys , vol.54 , pp. 5158-5164
    • Dubin, S.B.1
  • 54
    • 35348851499 scopus 로고    scopus 로고
    • Macromolecular crowding increases structural content of folded proteins
    • Perham M, Stagg L, Wittung-Stafshede P, (2007) Macromolecular crowding increases structural content of folded proteins. FEBS Lett 581: 5065-5069.
    • (2007) FEBS Lett , vol.581 , pp. 5065-5069
    • Perham, M.1    Stagg, L.2    Wittung-Stafshede, P.3
  • 55
    • 0034254189 scopus 로고    scopus 로고
    • Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell
    • Berg B Van Den, Wain R, Dobson CM, Ellis RJ, (2000) Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell. EMBO J 19: 3870-3875.
    • (2000) EMBO J , vol.19 , pp. 3870-3875
    • Van Den Berg, B.1    Wain, R.2    Dobson, C.M.3    Ellis, R.J.4
  • 56
    • 0027317178 scopus 로고
    • Fluorescence correlation spectroscopy with high count rate and low background: analysis of translational diffusion
    • Rigler R, Mets Ü, Widengren J, Kask P, (1993) Fluorescence correlation spectroscopy with high count rate and low background: analysis of translational diffusion. Eur Biophys J 22: 169-175.
    • (1993) Eur Biophys J , vol.22 , pp. 169-175
    • Rigler, R.1    Mets, Ü.2    Widengren, J.3    Kask, P.4


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