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Volumn 9, Issue 5, 2009, Pages 1326-1343

Biospecific irreversible fishing coupled with atomic force microscopy for detection of extremely low-abundant proteins

Author keywords

Atomic force microscopy; Biospecific fishing; Detection limit; Molecular detectors; Optical biosensor

Indexed keywords

BIOMATERIAL;

EID: 63049093298     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800598     Document Type: Article
Times cited : (72)

References (47)
  • 1
    • 0023850178 scopus 로고
    • Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase
    • Saiki, R. K., Gelfand, D. H., Stoffel, S., Scharf, S. J. et al., Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science 1988, 239, 487-491.
    • (1988) Science , vol.239 , pp. 487-491
    • Saiki, R.K.1    Gelfand, D.H.2    Stoffel, S.3    Scharf, S.J.4
  • 2
    • 0037253089 scopus 로고    scopus 로고
    • Protein arrays: The current state-of-the-art
    • Cutler, P., Protein arrays: The current state-of-the-art. Proteomics 2003, 3, 3-18.
    • (2003) Proteomics , vol.3 , pp. 3-18
    • Cutler, P.1
  • 4
    • 0037464428 scopus 로고    scopus 로고
    • Single-molecule PCR using water-in-oil emulsion
    • Nakano, M., Komatsu, J., Matsuura, S., Takashima, K. et al., Single-molecule PCR using water-in-oil emulsion. J. Biotechnol. 2003, 102, 117-124.
    • (2003) J. Biotechnol , vol.102 , pp. 117-124
    • Nakano, M.1    Komatsu, J.2    Matsuura, S.3    Takashima, K.4
  • 5
    • 10744228049 scopus 로고    scopus 로고
    • New real-time reverse transcriptase-initiated PCR assay with single-copy sensitivity for human immunodeficiency virus type 1 RNA in plasma
    • Palmer, S., Wiegand, A. P., Maldarelli, F., Bazmi, H. et al., New real-time reverse transcriptase-initiated PCR assay with single-copy sensitivity for human immunodeficiency virus type 1 RNA in plasma. J. Clin. Microbiol. 2003, 41, 4531-4546.
    • (2003) J. Clin. Microbiol , vol.41 , pp. 4531-4546
    • Palmer, S.1    Wiegand, A.P.2    Maldarelli, F.3    Bazmi, H.4
  • 6
    • 0025297178 scopus 로고
    • Direct electrophoretic detection of the allelic state of single DNA molecules in human sperm by using the polymerase chain reaction
    • Li, H., Cui, X., Arnheim, N., Direct electrophoretic detection of the allelic state of single DNA molecules in human sperm by using the polymerase chain reaction. Proc. Natl. Acad. Sci. USA 1990, 87, 4580-4584.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4580-4584
    • Li, H.1    Cui, X.2    Arnheim, N.3
  • 7
    • 19944408971 scopus 로고    scopus 로고
    • Limitations of current proteomics technologies
    • Garbis, S., Lubec, G., Fountoulakis, M., Limitations of current proteomics technologies. J. Chromatogr. A 2005, 1077, 1-18.
    • (2005) J. Chromatogr. A , vol.1077 , pp. 1-18
    • Garbis, S.1    Lubec, G.2    Fountoulakis, M.3
  • 9
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson, N. L., Anderson, N. G., The human plasma proteome: History, character, and diagnostic prospects. Mol. Cell. Proteomics 2002, 1, 845-867.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 10
    • 0034056940 scopus 로고    scopus 로고
    • The dynamic range of protein expression: A challenge for proteomic research
    • Corthals, G. L., Wasinger, V. C., Hochstrasser, D. F., Sanchez, J. C., The dynamic range of protein expression: A challenge for proteomic research. Electrophoresis 2000, 21, 1104-1115.
    • (2000) Electrophoresis , vol.21 , pp. 1104-1115
    • Corthals, G.L.1    Wasinger, V.C.2    Hochstrasser, D.F.3    Sanchez, J.C.4
  • 11
    • 0034662907 scopus 로고    scopus 로고
    • Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology
    • Gygi, S. P., Corthals, G. L., Zhang, Y., Rochon, Y., Aebersold, R., Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology. Proc. Natl. Acad. Sci. USA 2000, 97, 9390-9395.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9390-9395
    • Gygi, S.P.1    Corthals, G.L.2    Zhang, Y.3    Rochon, Y.4    Aebersold, R.5
  • 12
    • 33846010726 scopus 로고    scopus 로고
    • Extent of modifications in human proteome samples and their effect on dynamic range of analysis in shotgun proteomics
    • Nielsen, M. L., Savitski, M. M., Zubarev, R. A., Extent of modifications in human proteome samples and their effect on dynamic range of analysis in shotgun proteomics. Mol. Cell. Proteomics 2006, 5, 2384-2391.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2384-2391
    • Nielsen, M.L.1    Savitski, M.M.2    Zubarev, R.A.3
  • 13
    • 33846622299 scopus 로고    scopus 로고
    • AFM fishing nanotechnology is the way to reverse the Avogadro number in proteomics
    • Archakov, A. I., Ivanov, Y. D., Lisitsa, A. V., Zgoda, V. G., AFM fishing nanotechnology is the way to reverse the Avogadro number in proteomics. Proteomics 2007, 7, 4-9.
    • (2007) Proteomics , vol.7 , pp. 4-9
    • Archakov, A.I.1    Ivanov, Y.D.2    Lisitsa, A.V.3    Zgoda, V.G.4
  • 14
    • 40549133187 scopus 로고    scopus 로고
    • Proteomics, nanotechnology and molecular diagnostics
    • Johnson, C. J., Zhukovsky, N., Cass, A. E. G., Nagy, J. M., Proteomics, nanotechnology and molecular diagnostics. Proteomics 2008, 8, 715-730.
    • (2008) Proteomics , vol.8 , pp. 715-730
    • Johnson, C.J.1    Zhukovsky, N.2    Cass, A.E.G.3    Nagy, J.M.4
  • 15
    • 33750575732 scopus 로고    scopus 로고
    • Protein stains for proteomic applications: Which, when, why?
    • Miller, I., Crawford, J., Gianazza, E., Protein stains for proteomic applications: Which, when, why? Proteomics 2006, 6, 5385-5408.
    • (2006) Proteomics , vol.6 , pp. 5385-5408
    • Miller, I.1    Crawford, J.2    Gianazza, E.3
  • 16
    • 0034665968 scopus 로고    scopus 로고
    • Martin, S. E., Shabanowitz, J., Hunt, D. F., Marto, J. A., Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 2000, 72, 4266-4274.
    • Martin, S. E., Shabanowitz, J., Hunt, D. F., Marto, J. A., Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 2000, 72, 4266-4274.
  • 17
    • 14844311934 scopus 로고    scopus 로고
    • Candidate-based proteomics in the search for biomarkers of cardiovascular disease
    • Anderson, L., Candidate-based proteomics in the search for biomarkers of cardiovascular disease. J. Physiol. 2005, 563, 23-60.
    • (2005) J. Physiol , vol.563 , pp. 23-60
    • Anderson, L.1
  • 18
    • 3142699803 scopus 로고    scopus 로고
    • A protein microarray ELISA for screening biological fluids
    • Varnum, S. M., Woodbury, R. L., Zangar, R. C., A protein microarray ELISA for screening biological fluids. Methods Mol. Biol. 2004, 264, 161-172.
    • (2004) Methods Mol. Biol , vol.264 , pp. 161-172
    • Varnum, S.M.1    Woodbury, R.L.2    Zangar, R.C.3
  • 19
    • 34249659127 scopus 로고    scopus 로고
    • Aptamers as perspective affine reagents for clinical proteomics
    • Rad'ko, S. P., Rakhmetova, S. I., Bodoev, N. V., Archakov, A. I., Aptamers as perspective affine reagents for clinical proteomics. Biomed. Khim. 2007, 53, 5-24.
    • (2007) Biomed. Khim , vol.53 , pp. 5-24
    • Rad'ko, S.P.1    Rakhmetova, S.I.2    Bodoev, N.V.3    Archakov, A.I.4
  • 20
    • 33750595486 scopus 로고    scopus 로고
    • Label-free detection methods for protein microarrays
    • Yu, X., Xu, D., Cheng, Q., Label-free detection methods for protein microarrays. Proteomics 2006, 6, 5493-5503.
    • (2006) Proteomics , vol.6 , pp. 5493-5503
    • Yu, X.1    Xu, D.2    Cheng, Q.3
  • 21
    • 35148869587 scopus 로고    scopus 로고
    • Progress in miniaturization of protein arrays - A step closer to high-density nanoarrays
    • Wingren, C., Borrebaeck, C. A. K., Progress in miniaturization of protein arrays - A step closer to high-density nanoarrays. Drug Discov. Today 2007, 12, 813-819.
    • (2007) Drug Discov. Today , vol.12 , pp. 813-819
    • Wingren, C.1    Borrebaeck, C.A.K.2
  • 23
    • 33847683875 scopus 로고    scopus 로고
    • Design of atto-vial based recombinant antibody arrays combined with a planar wave-guide detection system
    • Ghatnekar-Nilsson, S., Dexlin, L., Wingren, C., Montelius, L., Borrebaeck, C. A. K., Design of atto-vial based recombinant antibody arrays combined with a planar wave-guide detection system. Proteomics 2007, 7, 540-547.
    • (2007) Proteomics , vol.7 , pp. 540-547
    • Ghatnekar-Nilsson, S.1    Dexlin, L.2    Wingren, C.3    Montelius, L.4    Borrebaeck, C.A.K.5
  • 24
    • 34948833721 scopus 로고    scopus 로고
    • Label-free and high-resolution protein/DNA nanoarray analysis using Kelvin probe force microscopy
    • Sinensky, A., Belcher, A., Label-free and high-resolution protein/DNA nanoarray analysis using Kelvin probe force microscopy, Nat. Nanotech. 2007, 2, 653-659.
    • (2007) Nat. Nanotech , vol.2 , pp. 653-659
    • Sinensky, A.1    Belcher, A.2
  • 25
    • 23944492134 scopus 로고    scopus 로고
    • Results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database
    • Overview of the HUPO Plasma Proteome Project
    • Omenn, G. S., States, D. J., Adamski, M., Blackwell, T. W. et al., Overview of the HUPO Plasma Proteome Project: Results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database. Proteomics 2005, 5, 3226-3245.
    • (2005) Proteomics , vol.5 , pp. 3226-3245
    • Omenn, G.S.1    States, D.J.2    Adamski, M.3    Blackwell, T.W.4
  • 26
    • 3042731730 scopus 로고    scopus 로고
    • Industrial-scale proteomics: From liters of plasma to chemically synthesized proteins
    • Rose, K., Bougueleret, L., Baussant, T., Boehm, G. et al., Industrial-scale proteomics: From liters of plasma to chemically synthesized proteins. Proteomics 2004, 4, 2125-2150.
    • (2004) Proteomics , vol.4 , pp. 2125-2150
    • Rose, K.1    Bougueleret, L.2    Baussant, T.3    Boehm, G.4
  • 27
    • 33645073886 scopus 로고    scopus 로고
    • Is protein overlap in two-dimensional gels a serious practical problem?
    • Hunsucker, S. W., Duncan, M. W., Is protein overlap in two-dimensional gels a serious practical problem? Proteomics 2006, 6, 137-145.
    • (2006) Proteomics , vol.6 , pp. 137-145
    • Hunsucker, S.W.1    Duncan, M.W.2
  • 28
    • 34247639389 scopus 로고    scopus 로고
    • Analytical nanobiotechnology for medicine diagnostics
    • Archakov, A. I., Ivanov, Y. D., Analytical nanobiotechnology for medicine diagnostics. Mol. Biosyst. 2007, 3, 336-342.
    • (2007) Mol. Biosyst , vol.3 , pp. 336-342
    • Archakov, A.I.1    Ivanov, Y.D.2
  • 29
    • 0033230230 scopus 로고    scopus 로고
    • AFM study of membrane proteins, cytochrome P450 2B4, and NADPH-cytochrome P450 reductase and their complex formation
    • Kiselyova, O. I., Yaminsky, I. V., Ivanov, Y. D., Kanaeva, I. P. et al., AFM study of membrane proteins, cytochrome P450 2B4, and NADPH-cytochrome P450 reductase and their complex formation. Arch. Biochem. Biophys. 1999, 371, 1-7.
    • (1999) Arch. Biochem. Biophys , vol.371 , pp. 1-7
    • Kiselyova, O.I.1    Yaminsky, I.V.2    Ivanov, Y.D.3    Kanaeva, I.P.4
  • 30
    • 3543081091 scopus 로고    scopus 로고
    • Atomic force microscopy revelation of molecular complexes in the multiprotein cytochrome P450 2B4-containing system
    • Kuznetsov, V. Y., Ivanov, Y. D., Archakov, A. I., Atomic force microscopy revelation of molecular complexes in the multiprotein cytochrome P450 2B4-containing system. Proteomics 2004, 4, 2390-2396.
    • (2004) Proteomics , vol.4 , pp. 2390-2396
    • Kuznetsov, V.Y.1    Ivanov, Y.D.2    Archakov, A.I.3
  • 31
    • 33750485825 scopus 로고    scopus 로고
    • Applied physics. High-speed atomic forcemicroscopy
    • Hansma, P. K., Schitter, G., Fantner, G. E., Prater, C., Applied physics. High-speed atomic forcemicroscopy. Science 2006, 314, 601-602.
    • (2006) Science , vol.314 , pp. 601-602
    • Hansma, P.K.1    Schitter, G.2    Fantner, G.E.3    Prater, C.4
  • 32
    • 0033704649 scopus 로고    scopus 로고
    • The Millipede - More than one thousand tips for future AFM data storage
    • Vettiger, P., Despont, M., Drechsler, U., Duerig, U. et al., The Millipede - More than one thousand tips for future AFM data storage. IBM J. Res. Develop. 2000, 44, 323-339.
    • (2000) IBM J. Res. Develop , vol.44 , pp. 323-339
    • Vettiger, P.1    Despont, M.2    Drechsler, U.3    Duerig, U.4
  • 33
    • 0028969366 scopus 로고
    • Staining methods in gel electrophoresis, including the use of multiple detection methods
    • Wirth, P. J., Romano, A., Staining methods in gel electrophoresis, including the use of multiple detection methods. J. Chromatogr. A 1995, 698, 123-143.
    • (1995) J. Chromatogr. A , vol.698 , pp. 123-143
    • Wirth, P.J.1    Romano, A.2
  • 34
    • 0023931883 scopus 로고
    • Improved staining of proteins in PAGEs including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff, V., Arold, N., Taube, D., Ehrhardt, W., Improved staining of proteins in PAGEs including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 1988, 9, 255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 35
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., Mann, M., Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 1996, 68, 850-858.
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 36
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • Wray, W., Boulikas, T., Wray, V. P., Hancock, R., Silver staining of proteins in polyacrylamide gels. Anal. Biochem. 1981, 118, 197-203.
    • (1981) Anal. Biochem , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3    Hancock, R.4
  • 37
    • 0017089931 scopus 로고
    • Photoactivated cross-linking of proteins within the erythrocyte membrane core
    • Mikkelsen, R. B., Wallach, D. F., Photoactivated cross-linking of proteins within the erythrocyte membrane core. J. Biol. Chem. 1976, 251, 7413-7416.
    • (1976) J. Biol. Chem , vol.251 , pp. 7413-7416
    • Mikkelsen, R.B.1    Wallach, D.F.2
  • 39
    • 0042847104 scopus 로고    scopus 로고
    • The proteasome as a lipopolysaccharide-binding protein in macrophages: Differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events
    • Qureshi, N., Perera, P.-Y., Shen, J., Zhang, G. et al., The proteasome as a lipopolysaccharide-binding protein in macrophages: Differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events. J. Immunol. 2003, 1515-1525.
    • (2003) J. Immunol , pp. 1515-1525
    • Qureshi, N.1    Perera, P.-Y.2    Shen, J.3    Zhang, G.4
  • 40
    • 0033054935 scopus 로고    scopus 로고
    • Optical biosensor studies on the productive complex formation between the components of cytochrome P450scc dependent monooxygenase system
    • Ivanov, Y. D., Usanov, S. A., Archakov, A. I., Optical biosensor studies on the productive complex formation between the components of cytochrome P450scc dependent monooxygenase system. Biochem. Mol. Biol. 1999, 47, 327-336.
    • (1999) Biochem. Mol. Biol , vol.47 , pp. 327-336
    • Ivanov, Y.D.1    Usanov, S.A.2    Archakov, A.I.3
  • 41
  • 43
    • 0141955818 scopus 로고    scopus 로고
    • DNA molecules and configurations in a solid-state nanopore microscope
    • Li, J., Gershow, M., Stein, D., Brandin, E., Golovchenko, J. A., DNA molecules and configurations in a solid-state nanopore microscope. Nat. Mater. 2003, 2, 611-615.
    • (2003) Nat. Mater , vol.2 , pp. 611-615
    • Li, J.1    Gershow, M.2    Stein, D.3    Brandin, E.4    Golovchenko, J.A.5
  • 44
    • 0027318108 scopus 로고
    • Directed mutagenesis and barnase-barstar recognition
    • Hartley, R. W., Directed mutagenesis and barnase-barstar recognition. Biochemistry 1993, 32, 5978-5984.
    • (1993) Biochemistry , vol.32 , pp. 5978-5984
    • Hartley, R.W.1
  • 45
    • 0037388679 scopus 로고    scopus 로고
    • Protein-protein interactions as a target for drugs in proteomics
    • Archakov, A. I., Govorun, V. M., Dubanov, A. V., Ivanov, Y. D. et al., Protein-protein interactions as a target for drugs in proteomics. Proteomics 2003, 3, 380-391.
    • (2003) Proteomics , vol.3 , pp. 380-391
    • Archakov, A.I.1    Govorun, V.M.2    Dubanov, A.V.3    Ivanov, Y.D.4
  • 46
    • 33750454460 scopus 로고    scopus 로고
    • Biomarker discovery by proteomics: Challenges not only for the analytical chemist
    • Horvatovich, P., Govorukhina, N., Bischoff, R., Biomarker discovery by proteomics: Challenges not only for the analytical chemist. Analyst 2006, 131, 1193-1196.
    • (2006) Analyst , vol.131 , pp. 1193-1196
    • Horvatovich, P.1    Govorukhina, N.2    Bischoff, R.3
  • 47
    • 33750682085 scopus 로고    scopus 로고
    • Evaluation of multiprotein immunoaffinity subtraction for plasma proteomics and candidate biomarker discovery using mass spectrometry
    • Liu, T., Qian, W.-J., Mottaz, H. M., Gritsenko, M. A. et al., Evaluation of multiprotein immunoaffinity subtraction for plasma proteomics and candidate biomarker discovery using mass spectrometry. Mol. Cell. Proteomics 2006, 5, 2167-2174.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2167-2174
    • Liu, T.1    Qian, W.-J.2    Mottaz, H.M.3    Gritsenko, M.A.4


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