메뉴 건너뛰기




Volumn 101, Issue 2, 2011, Pages 504-511

Study of receptor-chaperone interactions using the optical technique of spectroscopic ellipsometry

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; CELL SURFACE RECEPTOR; CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; OEP61 PROTEIN, ARABIDOPSIS;

EID: 80052458128     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.06.011     Document Type: Article
Times cited : (11)

References (34)
  • 1
    • 52149083091 scopus 로고    scopus 로고
    • The method of total internal reflection ellipsometry for thin film characterization and sensing
    • A. Nabok, and A. Tsargorodskaya The method of total internal reflection ellipsometry for thin film characterization and sensing Thin Solid Films. 516 2008 8993 9001
    • (2008) Thin Solid Films. , vol.516 , pp. 8993-9001
    • Nabok, A.1    Tsargorodskaya, A.2
  • 2
    • 78649741153 scopus 로고    scopus 로고
    • Detection of β-amyloid peptide (1-16) and amyloid precursor protein (APP770) using spectroscopic ellipsometry and QCM techniques: A step forward towards Alzheimers disease diagnostics
    • M.K. Mustafa, and A. Nabok A. Tsargorodskaya Detection of β-amyloid peptide (1-16) and amyloid precursor protein (APP770) using spectroscopic ellipsometry and QCM techniques: a step forward towards Alzheimers disease diagnostics Biosens. Bioelectron. 26 2010 1332 1336
    • (2010) Biosens. Bioelectron. , vol.26 , pp. 1332-1336
    • Mustafa, M.K.1    Nabok, A.2    Tsargorodskaya, A.3
  • 3
    • 34848844644 scopus 로고    scopus 로고
    • The study of genomic DNA adsorption and subsequent interactions using total internal reflection ellipsometry
    • DOI 10.1016/j.bios.2007.04.020, PII S0956566307002503
    • A. Nabok, and A. Tsargorodskaya P.J. Higson The study of DNA hybridization using total internal reflection ellipsometry Biosens. Bioelectr. 23 2007 377 383 (Pubitemid 47499029)
    • (2007) Biosensors and Bioelectronics , vol.23 , Issue.3 , pp. 377-383
    • Nabok, A.1    Tsargorodskaya, A.2    Davis, F.3    Higson, S.P.J.4
  • 4
    • 19744367038 scopus 로고    scopus 로고
    • Total internal reflection ellipsometry and SPR detection of low molecular weight environmental toxins
    • DOI 10.1016/j.apsusc.2004.11.084, PII S0169433204015983, 9th European Conferences on Organised Films (ECOF2004)
    • A.V. Nabok, and A. Tsargorodskaya N.F. Starodub Total internal reflection ellipsometry and SPR detection of low molecular weight environmental toxins Appl. Surf. Sci. 246 2005 381 386 (Pubitemid 40743422)
    • (2005) Applied Surface Science , vol.246 , Issue.4 , pp. 381-386
    • Nabok, A.V.1    Tsargorodskaya, A.2    Hassan, A.K.3    Starodub, N.F.4
  • 5
    • 33845389630 scopus 로고    scopus 로고
    • Registration of T-2 mycotoxin with total internal reflection ellipsometry and QCM impedance methods
    • DOI 10.1016/j.bios.2006.03.010, PII S0956566306001035
    • A.V. Nabok, and A. Tsargorodskaya O. Gojster Registration of T-2 mycotoxin with total internal reflection ellipsometry and QCM impedance methods Biosens. Bioelectron. 22 2007 885 890 (Pubitemid 44894866)
    • (2007) Biosensors and Bioelectronics , vol.22 , Issue.6 , pp. 885-890
    • Nabok, A.V.1    Tsargorodskaya, A.2    Holloway, A.3    Starodub, N.F.4    Gojster, O.5
  • 6
    • 79955648317 scopus 로고    scopus 로고
    • Detection of low molecular weight toxins using optical phase detection techniques
    • A. Nabok, and A. Tsargorodskaya A. Szekacs Detection of low molecular weight toxins using optical phase detection techniques Sens. Actuators B Chem. 154 2010 232 237
    • (2010) Sens. Actuators B Chem. , vol.154 , pp. 232-237
    • Nabok, A.1    Tsargorodskaya, A.2    Szekacs, A.3
  • 7
    • 34547794231 scopus 로고    scopus 로고
    • Specific binding of large aggregates of amphiphilic molecules to the respective antibodies
    • DOI 10.1021/la700414z
    • A.V. Nabok, and A. Tsargorodskaya A. Demchenko Specific binding of large aggregates of amphiphilic molecules to the respective antibodies Langmuir. 23 2007 8485 8490 (Pubitemid 47237840)
    • (2007) Langmuir , vol.23 , Issue.16 , pp. 8485-8490
    • Nabok, A.1    Tsargorodskaya, A.2    Holloway, A.3    Starodub, N.F.4    Demchenko, A.5
  • 8
    • 2542644040 scopus 로고    scopus 로고
    • Total internal reflection ellipsometry: Principles and applications
    • H. Arwin, M. Poksinski, and K. Johansen Total internal reflection ellipsometry: principles and applications Appl. Opt. 43 2004 3028 3036
    • (2004) Appl. Opt. , vol.43 , pp. 3028-3036
    • Arwin, H.1    Poksinski, M.2    Johansen, K.3
  • 10
    • 4644258895 scopus 로고    scopus 로고
    • Optical enzyme sensors based upon silicon planar waveguide coated with composite polyelectrolyte film
    • A.V. Nabok, S. Haron, and A.K. Ray Optical enzyme sensors based upon silicon planar waveguide coated with composite polyelectrolyte film Appl. Surf. Sci. 238 2004 423 428
    • (2004) Appl. Surf. Sci. , vol.238 , pp. 423-428
    • Nabok, A.V.1    Haron, S.2    Ray, A.K.3
  • 11
    • 0035412115 scopus 로고    scopus 로고
    • Immobilization of biocomponents for immune optical sensors
    • N.F. Starodub, and A.V. Nabok A.K. Hassan Immobilization of biocomponents for immune optical sensors Ukr. Biochem. J. 73 2001 55 64
    • (2001) Ukr. Biochem. J. , vol.73 , pp. 55-64
    • Starodub, N.F.1    Nabok, A.V.2    Hassan, A.K.3
  • 12
    • 28544442609 scopus 로고    scopus 로고
    • Protein translocation across biological membranes
    • DOI 10.1126/science.1113752
    • W. Wickner, and R. Schekman Protein translocation across biological membranes Science. 310 2005 1452 1456 (Pubitemid 41746334)
    • (2005) Science , vol.310 , Issue.5753 , pp. 1452-1456
    • Wickner, W.1    Schekman, R.2
  • 13
    • 33646593202 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64
    • S. Qbadou, and T. Becker E. Schleiff The molecular chaperone Hsp90 delivers precursor proteins to the chloroplast import receptor Toc64 EMBO J. 25 2006 1836 1847
    • (2006) EMBO J. , vol.25 , pp. 1836-1847
    • Qbadou, S.1    Becker, T.2    Schleiff, E.3
  • 14
    • 1642532372 scopus 로고    scopus 로고
    • A plant outer mitochondrial membrane protein with high amino acid sequence identity to a chloroplast protein import receptor
    • DOI 10.1016/S0014-5793(03)01457-1
    • O. Chew, and R. Lister J. Whelan A plant outer mitochondrial membrane protein with high amino acid sequence identity to a chloroplast protein import receptor FEBS Lett. 557 2004 109 114 (Pubitemid 38115878)
    • (2004) FEBS Letters , vol.557 , Issue.1-3 , pp. 109-114
    • Chew, O.1    Lister, R.2    Qbadou, S.3    Heazlewood, J.L.4    Soll, J.5    Schleiff, E.6    Millar, A.H.7    Whelan, J.8
  • 16
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • DOI 10.1016/S0092-8674(00)80830-2
    • C. Scheufler, and A. Brinker I. Moarefi Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine Cell. 101 2000 199 210 (Pubitemid 32004747)
    • (2000) Cell , vol.101 , Issue.2 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl F.Ulrich7    Moarefi, I.8
  • 17
    • 0035887167 scopus 로고    scopus 로고
    • Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins
    • DOI 10.1042/0264-6021:3590419
    • S.J. Wu, and F.H. Liu C. Wang Different combinations of the heat-shock cognate protein 70 (Hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins Biochem. J. 359 2001 419 426 (Pubitemid 32999788)
    • (2001) Biochemical Journal , vol.359 , Issue.2 , pp. 419-426
    • Wu, S.-J.1    Liu, F.-H.2    Hu, S.-M.3    Wang, C.4
  • 18
    • 0037470073 scopus 로고    scopus 로고
    • Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity
    • DOI 10.1074/jbc.M206867200
    • O.O. Odunuga, and J.A. Hornby G.L. Blatch Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity J. Biol. Chem. 278 2003 6896 6904 (Pubitemid 36800681)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 6896-6904
    • Odunuga, O.O.1    Hornby, J.A.2    Bies, C.3    Zimmermann, R.4    Pugh, D.J.5    Blatch, G.L.6
  • 19
    • 37549040609 scopus 로고    scopus 로고
    • The tetratricopeptide repeats of receptors involved in protein translocation across membranes
    • T. Schlegel, and O. Mirus E. Schleiff The tetratricopeptide repeats of receptors involved in protein translocation across membranes Mol. Biol. Evol. 24 2007 2763 2774
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 2763-2774
    • Schlegel, T.1    Mirus, O.2    Schleiff, E.3
  • 20
    • 84855303092 scopus 로고    scopus 로고
    • Chaperone receptors: Guiding proteins to intracellular compartments
    • in press
    • V. Kriechbaumer, O. von Löffelholz, and B.M. Abell Chaperone receptors: guiding proteins to intracellular compartments Protoplasma. 2011 in press
    • (2011) Protoplasma.
    • Kriechbaumer, V.1    Von Löffelholz, O.2    Abell, B.M.3
  • 21
    • 34250183921 scopus 로고    scopus 로고
    • Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones
    • B.M. Abell, and C. Rabu S. High Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones J. Cell Sci. 120 2007 1743
    • (2007) J. Cell Sci. , vol.120 , pp. 1743
    • Abell, B.M.1    Rabu, C.2    High, S.3
  • 22
    • 0037067724 scopus 로고    scopus 로고
    • Binding to chaperones allows import of a purified mitochondrial precursor into mitochondria
    • DOI 10.1074/jbc.M203474200
    • A. Artigues, A. Iriarte, and M. Martinez-Carrion Binding to chaperones allows import of a purified mitochondrial precursor into mitochondria J. Biol. Chem. 277 2002 25047 25055 (Pubitemid 34951809)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25047-25055
    • Artigues, A.1    Iriarte, A.2    Martinez-Carrion, M.3
  • 24
    • 0000560328 scopus 로고
    • Characterization of an HSP70 cognate gene family in Arabidopsis
    • C.H. Wu, and T. Caspar C. Somerville Characterization of an HSP70 cognate gene family in Arabidopsis Plant Physiol. 88 1988 731 740
    • (1988) Plant Physiol. , vol.88 , pp. 731-740
    • Wu, C.H.1    Caspar, T.2    Somerville, C.3
  • 25
    • 0028445992 scopus 로고
    • Isolation of a cDNA encoding a 70 kDa heat-shock cognate protein expressed in vegetative tissues of Arabidopsis thaliana
    • S.H. Wu, and C. Wang B.L. Lin Isolation of a cDNA encoding a 70 kDa heat-shock cognate protein expressed in vegetative tissues of Arabidopsis thaliana Plant Mol. Biol. 25 1994 577 583 (Pubitemid 2117213)
    • (1994) Plant Molecular Biology , vol.25 , Issue.3 , pp. 577-583
    • Wu Shiuh Hwan1    Wang Chung2    Chen Jychian3    Lin Bai Ling4
  • 26
    • 11844277123 scopus 로고    scopus 로고
    • The HSP90 chaperone complex, an emerging force in plant development and phenotypic plasticity
    • DOI 10.1016/j.pbi.2004.11.012, PII S1369526604001645
    • T.A. Sangster, and C. Queitsch The HSP90 chaperone complex, an emerging force in plant development and phenotypic plasticity Curr. Opin. Plant Biol. 8 2005 86 92 (Pubitemid 40084751)
    • (2005) Current Opinion in Plant Biology , vol.8 , Issue.1 , pp. 86-92
    • Sangster, T.A.1    Queitsch, C.2
  • 27
    • 79960814461 scopus 로고    scopus 로고
    • OEP61 is a chaperone receptor at the plastid outer envelope
    • 10.1042/BJ20110448 Epub ahead of print
    • O. v. Loeffelholz, and V. Kriechbaumer B.M. Abell OEP61 is a chaperone receptor at the plastid outer envelope Biochem. J. 2011 10.1042/BJ20110448 Epub ahead of print
    • (2011) Biochem. J.
    • Loeffelholz, O.V.1    Kriechbaumer, V.2    Abell, B.M.3
  • 28
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • DOI 10.1016/S0092-8674(02)01250-3
    • J.C. Young, N.J. Hoogenraad, and F.U. Hartl Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70 Cell. 112 2003 41 50 (Pubitemid 36106417)
    • (2003) Cell , vol.112 , Issue.1 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 30
    • 61449126034 scopus 로고    scopus 로고
    • Optical waveguide lightmode spectroscopy immunosensors for environmental monitoring
    • A. Székács, and N. Adányi I. Szendr Optical waveguide lightmode spectroscopy immunosensors for environmental monitoring Appl. Opt. 48 2009 151 158
    • (2009) Appl. Opt. , vol.48 , pp. 151-158
    • Székács, A.1    Adányi, N.2    Szendr, I.3
  • 31
    • 0032567434 scopus 로고    scopus 로고
    • Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery
    • DOI 10.1074/jbc.273.52.35194
    • S. Chen, and D.F. Smith Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery J. Biol. Chem. 273 1998 35194 35200 (Pubitemid 29028224)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.52 , pp. 35194-35200
    • Chen, S.1    Smith, D.F.2
  • 32
    • 12244301558 scopus 로고    scopus 로고
    • Determination of affinities and antigenic epitopes of bovine cardiac troponin I (cTnI) with monoclonal antibodies by surface plasmon resonance biosensor
    • DOI 10.1016/S0003-2697(02)00696-6
    • X. Liu, and J. Wei G. Luo Determination of affinities and antigenic epitopes of bovine cardiac troponin I (cTnI) with monoclonal antibodies by surface plasmon resonance biosensor Anal. Biochem. 314 2003 301 309 (Pubitemid 36315912)
    • (2003) Analytical Biochemistry , vol.314 , Issue.2 , pp. 301-309
    • Liu, X.1    Wei, J.2    Song, D.3    Zhang, Z.4    Zhang, H.5    Luo, G.6
  • 33
    • 0034978496 scopus 로고    scopus 로고
    • Comprehensive expression profile analysis of the Arabidopsis hsp70 gene family
    • DOI 10.1104/pp.126.2.789
    • D.Y. Sung, E. Vierling, and C.L. Guy Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family Plant Physiol. 126 2001 789 800 (Pubitemid 32568814)
    • (2001) Plant Physiology , vol.126 , Issue.2 , pp. 789-800
    • Dong Yul Sung1    Vierling, E.2    Guy, C.L.3
  • 34
    • 70349227588 scopus 로고    scopus 로고
    • WPP-domain proteins mimic the activity of the HSC70-1 chaperone in preventing mistargeting of RanGAP1-anchoring protein WIT1
    • J. Brkljacic, Q. Zhao, and I. Meier WPP-domain proteins mimic the activity of the HSC70-1 chaperone in preventing mistargeting of RanGAP1-anchoring protein WIT1 Plant Physiol. 151 2009 142 154
    • (2009) Plant Physiol. , vol.151 , pp. 142-154
    • Brkljacic, J.1    Zhao, Q.2    Meier, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.