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Volumn 23, Issue 3, 2005, Pages 157-162

Painting protein misfolding in the cell in real time with an atomic-scale brush

Author keywords

[No Author keywords available]

Indexed keywords

BIOTECHNOLOGY; CELLS; DISEASES; FLUORESCENCE; GENES; MOLECULAR BIOLOGY; REACTION KINETICS; REAL TIME SYSTEMS; SPECTROSCOPIC ANALYSIS;

EID: 13944269200     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibtech.2005.01.008     Document Type: Review
Times cited : (6)

References (44)
  • 1
    • 4444282070 scopus 로고    scopus 로고
    • Studying the interactome with the yeast two-hybrid system and mass spectrometry
    • B. Causier Studying the interactome with the yeast two-hybrid system and mass spectrometry Mass Spectrom. Rev. 23 2004 350 367
    • (2004) Mass Spectrom. Rev. , vol.23 , pp. 350-367
    • Causier, B.1
  • 2
    • 0036143190 scopus 로고    scopus 로고
    • Imaging into the future: Visualizing gene expression and protein interactions with fluorescent proteins
    • P.V. Roessel, and A.H. Brand Imaging into the future: visualizing gene expression and protein interactions with fluorescent proteins Nat. Cell Biol. 4 2002 15 20
    • (2002) Nat. Cell Biol. , vol.4 , pp. 15-20
    • Roessel, P.V.1    Brand, A.H.2
  • 3
    • 0141706507 scopus 로고    scopus 로고
    • Biotechnological applications of green fluorescent protein
    • J.C. March Biotechnological applications of green fluorescent protein Appl. Microbiol. Biotechnol. 62 2003 303 315
    • (2003) Appl. Microbiol. Biotechnol. , vol.62 , pp. 303-315
    • March, J.C.1
  • 4
    • 0036489443 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP): Applications, structure, and related photophysical behavior
    • M. Zimmer Green fluorescent protein (GFP): applications, structure, and related photophysical behavior Chem. Rev. 102 2002 759 781
    • (2002) Chem. Rev. , vol.102 , pp. 759-781
    • Zimmer, M.1
  • 5
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • R.Y. Tsien The green fluorescent protein Annu. Rev. Biochem. 67 1998 509 544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 6
    • 1542336956 scopus 로고    scopus 로고
    • The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins
    • V.V. Verkhusha, and K.A. Lukyanov The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins Nat. Biotechnol. 22 2004 289 296
    • (2004) Nat. Biotechnol. , vol.22 , pp. 289-296
    • Verkhusha, V.V.1    Lukyanov, K.A.2
  • 7
    • 0036308719 scopus 로고    scopus 로고
    • Mutations that reduce aggregation of the Alzheimer's Aβ42 peptide: An unbiased search for the sequence determinants of Aβ amyloidogenesis
    • C. Wurth Mutations that reduce aggregation of the Alzheimer's Aβ42 peptide: an unbiased search for the sequence determinants of Aβ amyloidogenesis J. Mol. Biol. 319 2002 1279 1290
    • (2002) J. Mol. Biol. , vol.319 , pp. 1279-1290
    • Wurth, C.1
  • 8
    • 0028921834 scopus 로고
    • Improved green fluorescence
    • R. Heim Improved green fluorescence Nature 373 1995 663 664
    • (1995) Nature , vol.373 , pp. 663-664
    • Heim, R.1
  • 9
    • 0036138545 scopus 로고    scopus 로고
    • Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed)
    • B.J. Bevis, and B.S. Glick Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed) Nat. Biotechnol. 20 2002 83 87
    • (2002) Nat. Biotechnol. , vol.20 , pp. 83-87
    • Bevis, B.J.1    Glick, B.S.2
  • 10
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • T. Nagai A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications Nat. Biotechnol. 20 2002 87 90
    • (2002) Nat. Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1
  • 11
    • 3042511548 scopus 로고    scopus 로고
    • Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP
    • O. Zapata-Hommer, and O. Griesbeck Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP BMC Biotechnol. 3 2003 5 10
    • (2003) BMC Biotechnol. , vol.3 , pp. 5-10
    • Zapata-Hommer, O.1    Griesbeck, O.2
  • 12
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • B.A. Griffin Specific covalent labeling of recombinant protein molecules inside live cells Science 281 1998 269 272
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1
  • 13
    • 0034581376 scopus 로고    scopus 로고
    • Fluorescent labeling of recombinant proteins in living cells with FlAsH
    • B.A. Griffin Fluorescent labeling of recombinant proteins in living cells with FlAsH Methods Enzymol. 327 2000 565 578
    • (2000) Methods Enzymol. , vol.327 , pp. 565-578
    • Griffin, B.A.1
  • 14
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications
    • S.R. Adams New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications J. Am. Chem. Soc. 124 2002 6063 6076
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6063-6076
    • Adams, S.R.1
  • 15
    • 1442264894 scopus 로고    scopus 로고
    • A new protein conformation indicator based on biarsenical fluorescein with an extended benzoic acid moiety
    • J. Nakanishi A new protein conformation indicator based on biarsenical fluorescein with an extended benzoic acid moiety Anal. Sci. 20 2004 273 278
    • (2004) Anal. Sci. , vol.20 , pp. 273-278
    • Nakanishi, J.1
  • 16
    • 0035387683 scopus 로고    scopus 로고
    • Imaging of conformational changes of proteins with a new environment-sensitive fluorescent probe designed for site-specific labeling of recombinant proteins in live cells
    • J. Nakanisi Imaging of conformational changes of proteins with a new environment-sensitive fluorescent probe designed for site-specific labeling of recombinant proteins in live cells Anal. Chem. 73 2001 2920 2928
    • (2001) Anal. Chem. , vol.73 , pp. 2920-2928
    • Nakanisi, J.1
  • 17
    • 0033996150 scopus 로고    scopus 로고
    • A novel method of affinity-purifying proteins using a bis-arsenical fluorescein
    • K.S. Thorn A novel method of affinity-purifying proteins using a bis-arsenical fluorescein Protein Sci. 9 2000 213 217
    • (2000) Protein Sci. , vol.9 , pp. 213-217
    • Thorn, K.S.1
  • 18
    • 0037134035 scopus 로고    scopus 로고
    • Multicolor and electron microscopic imaging of connexin trafficking
    • G. Gaietta Multicolor and electron microscopic imaging of connexin trafficking Science 296 2002 503 507
    • (2002) Science , vol.296 , pp. 503-507
    • Gaietta, G.1
  • 19
    • 0035069295 scopus 로고    scopus 로고
    • The potential of nucleic acid repair in functional genomics
    • M.C. Rice The potential of nucleic acid repair in functional genomics Nat. Biotechnol. 19 2001 321 326
    • (2001) Nat. Biotechnol. , vol.19 , pp. 321-326
    • Rice, M.C.1
  • 20
    • 0347568469 scopus 로고    scopus 로고
    • Genetically targeted chromophore-assisted light inactivation
    • O. Tour Genetically targeted chromophore-assisted light inactivation Nat. Biotechnol. 21 2003 1505 1508
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1505-1508
    • Tour, O.1
  • 21
    • 0037028010 scopus 로고    scopus 로고
    • Transgenically encoded protein photoinactivation (FlAsH-FALI): Acute inactivation of synaptotagmin I
    • K.W. Marek, and G.W. Davis Transgenically encoded protein photoinactivation (FlAsH-FALI): acute inactivation of synaptotagmin I Neuron 36 2002 805 813
    • (2002) Neuron , vol.36 , pp. 805-813
    • Marek, K.W.1    Davis, G.W.2
  • 22
    • 0346734116 scopus 로고    scopus 로고
    • In vivo oligomerization and raft localization of Ebola virus protein VP40 during vesicular budding
    • R.G. Panchal In vivo oligomerization and raft localization of Ebola virus protein VP40 during vesicular budding Proc. Natl. Acad. Sci. U. S. A. 100 2003 15936 15941
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 15936-15941
    • Panchal, R.G.1
  • 23
    • 0036772580 scopus 로고    scopus 로고
    • Preparative protein refolding
    • A.P.J. Middelbert Preparative protein refolding Trends Biotechnol. 20 2002 437 443
    • (2002) Trends Biotechnol. , vol.20 , pp. 437-443
    • Middelbert, A.P.J.1
  • 24
    • 2942703968 scopus 로고    scopus 로고
    • Protein misfolding in neurodegenerative diseases
    • E.I. Agorogiannis Protein misfolding in neurodegenerative diseases Neuropathol. Appl. Neurobiol. 30 2004 215 224
    • (2004) Neuropathol. Appl. Neurobiol. , vol.30 , pp. 215-224
    • Agorogiannis, E.I.1
  • 25
    • 0035116442 scopus 로고    scopus 로고
    • Growth arrest of individual senile plaques in a model of Alzheimer's disease observed by in vivo multiphoton microscopy
    • R.H. Christie Growth arrest of individual senile plaques in a model of Alzheimer's disease observed by in vivo multiphoton microscopy J. Neurosci. 21 2001 858 864
    • (2001) J. Neurosci. , vol.21 , pp. 858-864
    • Christie, R.H.1
  • 26
    • 0035404388 scopus 로고    scopus 로고
    • A close association of torsinA and α-synuclein in Lewy bodies: A fluorescence resonance energy transfer study
    • N. Sharma A close association of torsinA and α-synuclein in Lewy bodies: a fluorescence resonance energy transfer study Am. J. Pathol. 159 2001 339 344
    • (2001) Am. J. Pathol. , vol.159 , pp. 339-344
    • Sharma, N.1
  • 27
    • 0035818579 scopus 로고    scopus 로고
    • Specificity in intracellular protein aggregation and inclusion body formation
    • R.S. Rajan Specificity in intracellular protein aggregation and inclusion body formation Proc. Natl. Acad. Sci. U. S. A. 98 2001 13060 13065
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 13060-13065
    • Rajan, R.S.1
  • 28
    • 0036797242 scopus 로고    scopus 로고
    • Polyglutamine protein aggregates are dynamic
    • S. Kim Polyglutamine protein aggregates are dynamic Nat. Cell Biol. 4 2002 826 831
    • (2002) Nat. Cell Biol. , vol.4 , pp. 826-831
    • Kim, S.1
  • 29
    • 0037947662 scopus 로고    scopus 로고
    • A cell-based assay for aggregation inhibitors as therapeutics of polyglutamine-repeat disease and validation in Drosophila
    • B.L. Apostol A cell-based assay for aggregation inhibitors as therapeutics of polyglutamine-repeat disease and validation in Drosophila Proc. Natl. Acad. Sci. U. S. A. 100 2003 5950 5955
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5950-5955
    • Apostol, B.L.1
  • 30
    • 0037093734 scopus 로고    scopus 로고
    • Time course of polyglutamine aggregate body formation and cell death: Enhanced growth in nucleus and an interval for cell death
    • I. Toyoshima Time course of polyglutamine aggregate body formation and cell death: enhanced growth in nucleus and an interval for cell death J. Neurosci. Res. 68 2002 442 448
    • (2002) J. Neurosci. Res. , vol.68 , pp. 442-448
    • Toyoshima, I.1
  • 31
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • M. Bucciantini Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases Nature 416 2002 507 511
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1
  • 32
    • 0036841958 scopus 로고    scopus 로고
    • Protein aggregation in disease: A role for folding intermediates forming specific multimeric interactions
    • A. Horwich Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions J. Clin. Invest. 110 2002 1221 1232
    • (2002) J. Clin. Invest. , vol.110 , pp. 1221-1232
    • Horwich, A.1
  • 33
    • 0028917406 scopus 로고
    • Protein aggregation kinetics in an Escherichia coli strain overexpressing a Salmonella typhimurium CheY mutant gene
    • J. Klein, and P. Dhurjati Protein aggregation kinetics in an Escherichia coli strain overexpressing a Salmonella typhimurium CheY mutant gene Appl. Environ. Microbiol. 61 1995 1220 1225
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1220-1225
    • Klein, J.1    Dhurjati, P.2
  • 34
    • 0034518308 scopus 로고    scopus 로고
    • Kinetics of heat-shock response and inclusion body formation during temperature-induced production of basic fibroblast growth factor in high-cell-density cultures of recombinant Escherichia coli
    • F. Hoffmann, and U. Rinas Kinetics of heat-shock response and inclusion body formation during temperature-induced production of basic fibroblast growth factor in high-cell-density cultures of recombinant Escherichia coli Biotechnol. Prog. 16 2000 1000 1007
    • (2000) Biotechnol. Prog. , vol.16 , pp. 1000-1007
    • Hoffmann, F.1    Rinas, U.2
  • 35
    • 0034761941 scopus 로고    scopus 로고
    • Initial process of polyglutamine aggregate formation in vivo
    • Y. Kimura Initial process of polyglutamine aggregate formation in vivo Genes Cells 6 2001 887 897
    • (2001) Genes Cells , vol.6 , pp. 887-897
    • Kimura, Y.1
  • 36
    • 0347004717 scopus 로고    scopus 로고
    • Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling
    • Z. Ignatova, and L.M. Gierasch Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling Proc. Natl. Acad. Sci. U. S. A. 101 2004 523 528
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 523-528
    • Ignatova, Z.1    Gierasch, L.M.2
  • 37
    • 0034682867 scopus 로고    scopus 로고
    • Multiple roles of prolyl residues in structure and folding
    • S.J. Eyles, and L.M. Gierasch Multiple roles of prolyl residues in structure and folding J. Mol. Biol. 301 2000 737 747
    • (2000) J. Mol. Biol. , vol.301 , pp. 737-747
    • Eyles, S.J.1    Gierasch, L.M.2
  • 38
    • 0034802605 scopus 로고    scopus 로고
    • 2 binds not only to CCXXCC motifs but also non-specifically to endogenous cysteine-rich proteins
    • 2 binds not only to CCXXCC motifs but also non-specifically to endogenous cysteine-rich proteins Pflugers Arch. 442 2001 859 866
    • (2001) Pflugers Arch. , vol.442 , pp. 859-866
    • Stroffekova, K.1
  • 39
    • 0034995488 scopus 로고    scopus 로고
    • In vitro and in vivo nucleotide exchange directed by chimeric RNA/DNA oligonucleotides in Saccharomyces cerevisiae
    • M.C. Rice In vitro and in vivo nucleotide exchange directed by chimeric RNA/DNA oligonucleotides in Saccharomyces cerevisiae Mol. Microbiol. 40 2001 857 868
    • (2001) Mol. Microbiol. , vol.40 , pp. 857-868
    • Rice, M.C.1
  • 41
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • A. Keppler A general method for the covalent labeling of fusion proteins with small molecules in vivo Nat. Biotechnol. 21 2003 86 89
    • (2003) Nat. Biotechnol. , vol.21 , pp. 86-89
    • Keppler, A.1
  • 42
    • 1842582037 scopus 로고    scopus 로고
    • Reversible site-selective labeling of membrane proteins in live cells
    • E.G. Guignet Reversible site-selective labeling of membrane proteins in live cells Nat. Biotechnol. 22 2004 440 444
    • (2004) Nat. Biotechnol. , vol.22 , pp. 440-444
    • Guignet, E.G.1
  • 43
    • 0344874141 scopus 로고    scopus 로고
    • Cell-permeable small molecule probes for site-specific labeling of proteins
    • D.S.Y. Yeo Cell-permeable small molecule probes for site-specific labeling of proteins Chem. Commun (Camb) 23 2003 2870 2871
    • (2003) Chem. Commun (Camb) , vol.23 , pp. 2870-2871
    • Yeo, D.S.Y.1
  • 44
    • 0029125852 scopus 로고
    • Crystal structure of cellular retinoic acid-binding protein 1 shows increased access to the binding cavity due to formation of an intermolecular beta sheet
    • J.R. Thompson Crystal structure of cellular retinoic acid-binding protein 1 shows increased access to the binding cavity due to formation of an intermolecular beta sheet J. Mol. Biol. 252 1995 433 446
    • (1995) J. Mol. Biol. , vol.252 , pp. 433-446
    • Thompson, J.R.1


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