메뉴 건너뛰기




Volumn 105, Issue 38, 2008, Pages 14400-14405

Burst analysis spectroscopy: A versatile single-particle approach for studying distributions of protein aggregates and fluorescent assemblies

Author keywords

Aggregation; Fluorescence spectroscopy; Microfluidics.

Indexed keywords

CARBOXYLASE; CHAPERONIN; OXYGENASE; RIBULOSEBISPHOSPHATE CARBOXYLASE;

EID: 55749100687     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0805969105     Document Type: Article
Times cited : (22)

References (30)
  • 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
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT (1996) Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26:267-298.
    • (1996) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 3
    • 33748742268 scopus 로고    scopus 로고
    • Is any measurement method optimal for all aggregate sizes and types?
    • Philo JS (2006) Is any measurement method optimal for all aggregate sizes and types? AAPS J 8:E564-E571.
    • (2006) AAPS J , vol.8
    • Philo, J.S.1
  • 5
    • 0034625009 scopus 로고    scopus 로고
    • Ultrasensitive detection of pathological prion protein aggregates by dual-color scanning for intensely fluorescent targets
    • Bieschke J, et al. (2000) Ultrasensitive detection of pathological prion protein aggregates by dual-color scanning for intensely fluorescent targets. Proc Natl Acad Sci USA 97:5468-5473.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5468-5473
    • Bieschke, J.1
  • 6
    • 33749508090 scopus 로고    scopus 로고
    • Direct observation of amyloid growth monitored by total internal reflection fluorescence microscopy
    • Ban T, Goto Y (2006) Direct observation of amyloid growth monitored by total internal reflection fluorescence microscopy. Methods Enzymol 413:91-102.
    • (2006) Methods Enzymol , vol.413 , pp. 91-102
    • Ban, T.1    Goto, Y.2
  • 7
    • 21344466724 scopus 로고    scopus 로고
    • Single particle detection and characterization of synuclein coaggregation
    • Giese A, et al. (2005) Single particle detection and characterization of synuclein coaggregation. Biochem Biophys Res Commun 333:1202-1210.
    • (2005) Biochem Biophys Res Commun , vol.333 , pp. 1202-1210
    • Giese, A.1
  • 8
    • 0346734134 scopus 로고    scopus 로고
    • Probing protein oligomerization in living cells with fluorescence fluctuation spectroscopy
    • Chen Y, Wei LN, Muller JD (2003) Probing protein oligomerization in living cells with fluorescence fluctuation spectroscopy. Proc Natl Acad Sci USA 100:15492-15497.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15492-15497
    • Chen, Y.1    Wei, L.N.2    Muller, J.D.3
  • 9
    • 0034033145 scopus 로고    scopus 로고
    • Resolving heterogeneity on the single molecular level with the photon-counting histogram
    • Muller JD, Chen Y, Gratton E (2000) Resolving heterogeneity on the single molecular level with the photon-counting histogram. Biophys J 78:474-486.
    • (2000) Biophys J , vol.78 , pp. 474-486
    • Muller, J.D.1    Chen, Y.2    Gratton, E.3
  • 10
    • 0033598837 scopus 로고    scopus 로고
    • Fluorescence-intensity distribution analysis and its application in biomolecular detection technology
    • Kask P, Palo K, Ullmann D, Gall K (1999) Fluorescence-intensity distribution analysis and its application in biomolecular detection technology. Proc Natl Acad Sci USA 96:13756-13761.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13756-13761
    • Kask, P.1    Palo, K.2    Ullmann, D.3    Gall, K.4
  • 11
    • 0344603641 scopus 로고    scopus 로고
    • The photon counting histogram in fluorescence fluctuation spectroscopy
    • Chen Y, Muller JD, So PT, Gratton E (1999) The photon counting histogram in fluorescence fluctuation spectroscopy. Biophys J 77:553-567.
    • (1999) Biophys J , vol.77 , pp. 553-567
    • Chen, Y.1    Muller, J.D.2    So, P.T.3    Gratton, E.4
  • 12
    • 0035853637 scopus 로고    scopus 로고
    • Data registration and selective single-molecule analysis using multi-parameter fluorescence detection
    • Eggeling C, et al. (2001) Data registration and selective single-molecule analysis using multi-parameter fluorescence detection. J Biotechnol 86:163-180.
    • (2001) J Biotechnol , vol.86 , pp. 163-180
    • Eggeling, C.1
  • 13
    • 0035690197 scopus 로고    scopus 로고
    • Principles of single molecule multiparameter fluorescence spectroscopy
    • Kuhnemuth R, Seidel CAM (2001) Principles of single molecule multiparameter fluorescence spectroscopy. Single Molecules 2:251-254.
    • (2001) Single Molecules , vol.2 , pp. 251-254
    • Kuhnemuth, R.1    Seidel, C.A.M.2
  • 14
    • 0030895059 scopus 로고    scopus 로고
    • Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution
    • Schwille P, Meyer-Almes FJ, Rigler R (1997) Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution. Biophys J 72:1878-1886.
    • (1997) Biophys J , vol.72 , pp. 1878-1886
    • Schwille, P.1    Meyer-Almes, F.J.2    Rigler, R.3
  • 15
    • 31744436399 scopus 로고    scopus 로고
    • Fluorescence cross-correlation spectroscopy in living cells
    • Bacia K, Kim SA, Schwille P (2006) Fluorescence cross-correlation spectroscopy in living cells. Nat Methods 3:83-89.
    • (2006) Nat Methods , vol.3 , pp. 83-89
    • Bacia, K.1    Kim, S.A.2    Schwille, P.3
  • 16
    • 0024222682 scopus 로고
    • Particle counting by fluorescence correlation spectroscopy - simultaneous measurement of aggregation and diffusion of molecules in solutions and in membranes
    • Meyer T, Schindler H (1988) Particle counting by fluorescence correlation spectroscopy - simultaneous measurement of aggregation and diffusion of molecules in solutions and in membranes. Biophys J 54:983-993.
    • (1988) Biophys J , vol.54 , pp. 983-993
    • Meyer, T.1    Schindler, H.2
  • 17
    • 0029977148 scopus 로고    scopus 로고
    • Scanning two-photon fluctuation correlation spectroscopy: Particle counting measurements for detection of molecular aggregation
    • Berland KM, So PTC, Chen Y, Mantulin WW, Gratton E (1996) Scanning two-photon fluctuation correlation spectroscopy: Particle counting measurements for detection of molecular aggregation. Biophys J 71:410-420.
    • (1996) Biophys J , vol.71 , pp. 410-420
    • Berland, K.M.1    So, P.T.C.2    Chen, Y.3    Mantulin, W.W.4    Gratton, E.5
  • 18
    • 84975594445 scopus 로고
    • Analysis of confocal laser-microscope optics for 3-D fluorescence correlation spectroscopy
    • Qian H, Elson EL (1991) Analysis of confocal laser-microscope optics for 3-D fluorescence correlation spectroscopy. Applied Optics 30:1185-1195.
    • (1991) Applied Optics , vol.30 , pp. 1185-1195
    • Qian, H.1    Elson, E.L.2
  • 19
    • 0036789423 scopus 로고    scopus 로고
    • Focal volume optics and experimental artifacts in confocal fluorescence correlation spectroscopy
    • Hess ST, Webb WW (2002) Focal volume optics and experimental artifacts in confocal fluorescence correlation spectroscopy. Biophys J 83:2300-2317.
    • (2002) Biophys J , vol.83 , pp. 2300-2317
    • Hess, S.T.1    Webb, W.W.2
  • 20
    • 2442531436 scopus 로고
    • Aggregation kinetics
    • Meakin P (1992) Aggregation kinetics. Phys Scr 46:295-331.
    • (1992) Phys Scr , vol.46 , pp. 295-331
    • Meakin, P.1
  • 21
    • 0024820705 scopus 로고
    • Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
    • Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH (1989) Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP. Nature 342:884-889.
    • (1989) Nature , vol.342 , pp. 884-889
    • Goloubinoff, P.1    Christeller, J.T.2    Gatenby, A.A.3    Lorimer, G.H.4
  • 22
    • 4944221602 scopus 로고    scopus 로고
    • Expansion and compression of a protein folding intermediate by GroEL
    • Lin Z, Rye HS (2004) Expansion and compression of a protein folding intermediate by GroEL. Mol Cell 16:23-34.
    • (2004) Mol Cell , vol.16 , pp. 23-34
    • Lin, Z.1    Rye, H.S.2
  • 23
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • Collins SR, Douglass A, Vale RD, Weissman JS (2004) Mechanism of prion propagation: Amyloid growth occurs by monomer addition. PLoS Biol 2:e321.
    • (2004) PLoS Biol , vol.2
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 24
    • 2942722444 scopus 로고    scopus 로고
    • Hsp 104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • Shorter J, Lindquist S (2004) Hsp 104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304:1793-1797.
    • (2004) Science , vol.304 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 25
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • Patino MM, Liu JJ, Glover JR, Lindquist S (1996) Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273:622-626.
    • (1996) Science , vol.273 , pp. 622-626
    • Patino, M.M.1    Liu, J.J.2    Glover, J.R.3    Lindquist, S.4
  • 26
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1
    • Naiki H, Higuchi K, Hosokawa M, Takeda T (1989) Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal Biochem 177:244-249.
    • (1989) Anal Biochem , vol.177 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 27
    • 33644855448 scopus 로고    scopus 로고
    • An in vitro fluorescence screen to identify antivirals that disrupt hepatitis B virus capsid assembly
    • Stray SJ, Johnson JM, Kopek BG, Zlotnick A (2006) An in vitro fluorescence screen to identify antivirals that disrupt hepatitis B virus capsid assembly. Nat Biotechnol 24:358-362.
    • (2006) Nat Biotechnol , vol.24 , pp. 358-362
    • Stray, S.J.1    Johnson, J.M.2    Kopek, B.G.3    Zlotnick, A.4
  • 28
    • 33745787907 scopus 로고    scopus 로고
    • Dynamic pathways for viral capsid assembly
    • Hagan MF, Chandler D (2006) Dynamic pathways for viral capsid assembly. Biophys J 91:42-54.
    • (2006) Biophys J , vol.91 , pp. 42-54
    • Hagan, M.F.1    Chandler, D.2
  • 29
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state
    • Pallitto MM, Murphy RM (2001) A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state. Biophys J 81:1805-1822.
    • (2001) Biophys J , vol.81 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 30
    • 0000265413 scopus 로고    scopus 로고
    • Molecular shot noise, burst size distribution, and single-molecule detection in fluid flow: Effects of multiple occupancy
    • Enderlein J, Robbins DL, Ambrose WP, Keller RA (1998) Molecular shot noise, burst size distribution, and single-molecule detection in fluid flow: Effects of multiple occupancy. J Phys Chem A 102:6089-6094.
    • (1998) J Phys Chem A , vol.102 , pp. 6089-6094
    • Enderlein, J.1    Robbins, D.L.2    Ambrose, W.P.3    Keller, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.