메뉴 건너뛰기




Volumn 288, Issue 5, 1999, Pages 1027-1036

High-resolution AFM-imaging and mechanistic analysis of the 20 S proteasome

Author keywords

Antigen processing; Enzyme; Interface; Membrane; Multicatalytic proteinase

Indexed keywords

HISTIDINE; PROTEASOME; PROTEIN SUBUNIT;

EID: 0033591349     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2714     Document Type: Article
Times cited : (58)

References (40)
  • 1
    • 0031030057 scopus 로고    scopus 로고
    • Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum
    • Akopian T., Kisselev A., Goldberg A. Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J. Biol. Chem. 272:1997;1791-1798.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1791-1798
    • Akopian, T.1    Kisselev, A.2    Goldberg, A.3
  • 4
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister W., Walz J., Zühl F., Seemüller E. The proteasome: paradigm of a self-compartmentalizing protease. Cell. 92:1998;367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 5
    • 0031886683 scopus 로고    scopus 로고
    • Specific interaction and two-dimensional crystallization of histidine-tagged yeast RNA polymerase I on nickel-chelating lipids
    • Bischler N., Balavoine F., Milkereit P., Tschochner H., Mioskowski C., Schultz P. Specific interaction and two-dimensional crystallization of histidine-tagged yeast RNA polymerase I on nickel-chelating lipids. Biophys. J. 74:1998;1522-1532.
    • (1998) Biophys. J. , vol.74 , pp. 1522-1532
    • Bischler, N.1    Balavoine, F.2    Milkereit, P.3    Tschochner, H.4    Mioskowski, C.5    Schultz, P.6
  • 6
    • 0028972449 scopus 로고
    • A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
    • Brannigan J., Dodson G., Duggleby H., Moody P., Smith J., Tomchick D., Murzin A. A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature. 378:1995;416-419.
    • (1995) Nature , vol.378 , pp. 416-419
    • Brannigan, J.1    Dodson, G.2    Duggleby, H.3    Moody, P.4    Smith, J.5    Tomchick, D.6    Murzin, A.7
  • 7
    • 0029025914 scopus 로고
    • Molecular organization of histidine-tagged biomolecules at self-assembled lipid interfaces using a novel class of chelator lipids
    • Dietrich C., Schmitt L., Tampé R. Molecular organization of histidine-tagged biomolecules at self-assembled lipid interfaces using a novel class of chelator lipids. Proc. Natl Acad. Sci. USA. 92:1995;9014-9018.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9014-9018
    • Dietrich, C.1    Schmitt, L.2    Tampé, R.3
  • 8
    • 0030069974 scopus 로고    scopus 로고
    • Functional immobilization of a DNA-binding protein at a membrane interface via histidine tag and synthetic chelator lipids
    • Dietrich C., Boscheinen O., Scharf K. D., Schmitt L., Tampé R. Functional immobilization of a DNA-binding protein at a membrane interface via histidine tag and synthetic chelator lipids. Biochemistry. 35:1996;1100-1105.
    • (1996) Biochemistry , vol.35 , pp. 1100-1105
    • Dietrich, C.1    Boscheinen, O.2    Scharf, K.D.3    Schmitt, L.4    Tampé, R.5
  • 9
    • 0032139588 scopus 로고    scopus 로고
    • Diacetylene chelator lipids as supports for immobilization and imaging of proteins by atomic force microscopy
    • Dorn I. T., Hofmann U. G., Peltonen J., Tampé R. Diacetylene chelator lipids as supports for immobilization and imaging of proteins by atomic force microscopy. Langmuir. 14:1998a;4836-4842.
    • (1998) Langmuir , vol.14 , pp. 4836-4842
    • Dorn, I.T.1    Hofmann, U.G.2    Peltonen, J.3    Tampé, R.4
  • 10
    • 0032053630 scopus 로고    scopus 로고
    • Molecular recognition of histidine-tagged molecules by metal-chelating lipids monitored by fluorescence energy transfer and correlation spectroscopy
    • Dorn I. T., Neumaier K. R., Tampé R. Molecular recognition of histidine-tagged molecules by metal-chelating lipids monitored by fluorescence energy transfer and correlation spectroscopy. J. Am. Chem. Soc. 121:1998b;2753-2763.
    • (1998) J. Am. Chem. Soc. , vol.121 , pp. 2753-2763
    • Dorn, I.T.1    Neumaier, K.R.2    Tampé, R.3
  • 11
    • 0031696253 scopus 로고    scopus 로고
    • Orientation and two-dimensional organization of proteins at chelator lipid interfaces
    • Dorn I. T., Pawlitschko K., Pettinger S. C., Tampé R. Orientation and two-dimensional organization of proteins at chelator lipid interfaces. Biol. Chem. 379:1998c;1151-1159.
    • (1998) Biol. Chem. , vol.379 , pp. 1151-1159
    • Dorn, I.T.1    Pawlitschko, K.2    Pettinger, S.C.3    Tampé, R.4
  • 12
    • 0030061052 scopus 로고    scopus 로고
    • Effects of major-histocompatibility-complex-encoded subunits on the peptidase and proteolytic activities of human 20 S proteasomes
    • Ehring B., Meyer T. H., Eckerskorn C., Lottspeich F., Tampé R. Effects of major-histocompatibility-complex-encoded subunits on the peptidase and proteolytic activities of human 20 S proteasomes. Eur. J. Biochem. 235:1996;404-415.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 404-415
    • Ehring, B.1    Meyer, T.H.2    Eckerskorn, C.3    Lottspeich, F.4    Tampé, R.5
  • 13
    • 0030951962 scopus 로고    scopus 로고
    • High-resolution imaging of native biological sample surfaces with scanning probe microscopy
    • Engel A., Schoenenberger C.-A., Müller D. J. High-resolution imaging of native biological sample surfaces with scanning probe microscopy. Curr. Opin. Struct. Biol. 7:1997;279-284.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 279-284
    • Engel, A.1    Schoenenberger, C.-A.2    Müller, D.J.3
  • 14
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin E.-L., Moy V., Gaub H. Adhesion forces between individual ligand-receptor pairs. Science. 264:1994;415-417.
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.-L.1    Moy, V.2    Gaub, H.3
  • 15
    • 0031352110 scopus 로고    scopus 로고
    • In situ surface plasmon resonance analysis of dextran monolayer degradation by dextranase
    • Frazier R., Davies M., Matthijs G., Roberts C., Schacht E., Tendler S., Williams P. In situ surface plasmon resonance analysis of dextran monolayer degradation by dextranase. Langmuir. 13:1997;7115-7120.
    • (1997) Langmuir , vol.13 , pp. 7115-7120
    • Frazier, R.1    Davies, M.2    Matthijs, G.3    Roberts, C.4    Schacht, E.5    Tendler, S.6    Williams, P.7
  • 17
    • 0028850498 scopus 로고
    • Engineered fusion molecules at chelator lipid interfaces imaged by reflection interference contrast microscopy (RICM)
    • Gritsch S., Neumaier K., Schmitt L., Tampé R. Engineered fusion molecules at chelator lipid interfaces imaged by reflection interference contrast microscopy (RICM). Biosens. Bioelect. 10:1995;805-812.
    • (1995) Biosens. Bioelect. , vol.10 , pp. 805-812
    • Gritsch, S.1    Neumaier, K.2    Schmitt, L.3    Tampé, R.4
  • 18
    • 0030773048 scopus 로고    scopus 로고
    • Kinetic and stochiometric analysis for the binding of Escherichia coli ribonuclease HI to RNA-DNA hybrids using surface plasmon resonance
    • Haruki M., Noguchi E., Kanaya S., Crouch R. Kinetic and stochiometric analysis for the binding of Escherichia coli ribonuclease HI to RNA-DNA hybrids using surface plasmon resonance. J. Biol. Chem. 272:1997;22015-22022.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22015-22022
    • Haruki, M.1    Noguchi, E.2    Kanaya, S.3    Crouch, R.4
  • 20
    • 0031892541 scopus 로고    scopus 로고
    • Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes
    • Kisselev A. F., Akopian T. N., Goldberg A. L. Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes. J. Biol. Chem. 273:1998;1982-1989.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1982-1989
    • Kisselev, A.F.1    Akopian, T.N.2    Goldberg, A.L.3
  • 21
    • 0028590161 scopus 로고
    • Two-dimensional crystallization of histidine-tagged HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid
    • Kubalek E. W., Le Grice F. J., Brown P. O. Two-dimensional crystallization of histidine-tagged HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid. J. Struct. Biol. 113:1994;117-123.
    • (1994) J. Struct. Biol. , vol.113 , pp. 117-123
    • Kubalek, E.W.1    Le, G.F.J.2    Brown, P.O.3
  • 22
    • 0030775380 scopus 로고    scopus 로고
    • Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1
    • Levitskaya J., Sharipo A., Leonchiks A., Ciechanover A., Masucci M. G. Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1. Proc. Natl Acad. Sci. USA. 94:1997;12616-12621.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12616-12621
    • Levitskaya, J.1    Sharipo, A.2    Leonchiks, A.3    Ciechanover, A.4    Masucci, M.G.5
  • 23
    • 0029042511 scopus 로고
    • Crystal structure of the 20 S proteasome from the archaeon Thermoplasma acidophilum at 3.4 Å resolution
    • Löwe J., Stock D., Jap B., Zwickl P., Baumeister W., Huber R. Crystal structure of the 20 S proteasome from the archaeon Thermoplasma acidophilum at 3.4 Å resolution. Science. 268:1995;533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 24
    • 0030058166 scopus 로고    scopus 로고
    • Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans monitored by atomic force microscopy
    • Müller D., Baumeister W., Engel A. Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans monitored by atomic force microscopy. J. Bacteriol. 178:1996;3025-3030.
    • (1996) J. Bacteriol. , vol.178 , pp. 3025-3030
    • Müller, D.1    Baumeister, W.2    Engel, A.3
  • 25
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • Müller D., Amrein M., Engel A. Adsorption of biological molecules to a solid support for scanning probe microscopy. J. Struct. Biol. 119:1997;172-188.
    • (1997) J. Struct. Biol. , vol.119 , pp. 172-188
    • Müller, D.1    Amrein, M.2    Engel, A.3
  • 26
    • 0030600394 scopus 로고    scopus 로고
    • Quantitative analysis of the transcription factor AP2 binding to DNA by atomic force microscopy
    • Nettikadan S., Tokumasu F., Takeyasu K. Quantitative analysis of the transcription factor AP2 binding to DNA by atomic force microscopy. Biochem. Biophys. Res. Commun. 226:1996;645-649.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 645-649
    • Nettikadan, S.1    Tokumasu, F.2    Takeyasu, K.3
  • 27
    • 0027293351 scopus 로고
    • Determination of rate and equilibrium binding constants for macromolecular interaction using surface plasmon resonance: Use of nonlinear least squares analysis methods
    • O'Shannessy D. J., Brigham-Burke M., Soneson K. K., Hensley P., Brooks I. Determination of rate and equilibrium binding constants for macromolecular interaction using surface plasmon resonance: use of nonlinear least squares analysis methods. Anal. Biochem. 212:1993;457-468.
    • (1993) Anal. Biochem. , vol.212 , pp. 457-468
    • O'Shannessy, D.J.1    Brigham-Burke, M.2    Soneson, K.K.3    Hensley, P.4    Brooks, I.5
  • 28
    • 0030397047 scopus 로고    scopus 로고
    • Imaging two-dimensional crystals of catalase by atomic force microscopy
    • Ohnishi S., Hara M., Furuno T., Sasabe H. Imaging two-dimensional crystals of catalase by atomic force microscopy. Jpn. J. Appl. Phys. 35:1996;6233-6238.
    • (1996) Jpn. J. Appl. Phys. , vol.35 , pp. 6233-6238
    • Ohnishi, S.1    Hara, M.2    Furuno, T.3    Sasabe, H.4
  • 29
    • 0028031337 scopus 로고
    • Direct observation of enzyme activity with the atomic force microscope
    • Radmacher M., Fritz M., Hansma H., Hansma P. Direct observation of enzyme activity with the atomic force microscope. Science. 265:1994;1577-1579.
    • (1994) Science , vol.265 , pp. 1577-1579
    • Radmacher, M.1    Fritz, M.2    Hansma, H.3    Hansma, P.4
  • 30
    • 0031880366 scopus 로고    scopus 로고
    • Growth of protein 2-D crystals on supported planar lipid bilayers imaged in situ by AFM
    • Reviakine I., Bergsma-Schutter W., Brisson A. Growth of protein 2-D crystals on supported planar lipid bilayers imaged in situ by AFM. J. Struct. Biol. 121:1998;356-361.
    • (1998) J. Struct. Biol. , vol.121 , pp. 356-361
    • Reviakine, I.1    Bergsma-Schutter, W.2    Brisson, A.3
  • 31
    • 0032055436 scopus 로고    scopus 로고
    • Screening ligands for membrane-protein receptors by total internal-reflection fluorescence - The 5HT3 serotonin receptor
    • Schmid E. L., Tairi A. P., Hovius R., Vogel H. Screening ligands for membrane-protein receptors by total internal-reflection fluorescence - the 5HT3 serotonin receptor. Anal. Chem. 70:1998;1331-1338.
    • (1998) Anal. Chem. , vol.70 , pp. 1331-1338
    • Schmid, E.L.1    Tairi, A.P.2    Hovius, R.3    Vogel, H.4
  • 32
    • 0028150044 scopus 로고
    • Synthesis and characterization of chelator lipids for reversible immobilization of engineered proteins at self-assembled lipid interfaces
    • Schmitt L., Dietrich C., Tampé R. Synthesis and characterization of chelator lipids for reversible immobilization of engineered proteins at self-assembled lipid interfaces. J. Am. Chem. Soc. 116:1994;8485-8491.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8485-8491
    • Schmitt, L.1    Dietrich, C.2    Tampé, R.3
  • 34
    • 0029734665 scopus 로고    scopus 로고
    • Biological atomic force microscopy - What is achieved and what is needed
    • Shao Z., Mou J., Czajkowsky D., Yang J., Yuan J. Biological atomic force microscopy - What is achieved and what is needed. Advan. Phys. 45:1996;1-86.
    • (1996) Advan. Phys. , vol.45 , pp. 1-86
    • Shao, Z.1    Mou, J.2    Czajkowsky, D.3    Yang, J.4    Yuan, J.5
  • 35
    • 0028463817 scopus 로고
    • Specific protein attachment to artificial membranes via coordination to lipid-bound copper(II)
    • Shnek D. R., Pack D. W., Sasaki D. Y., Arnold F. H. Specific protein attachment to artificial membranes via coordination to lipid-bound copper(II). Langmuir. 10:1994;2382-2388.
    • (1994) Langmuir , vol.10 , pp. 2382-2388
    • Shnek, D.R.1    Pack, D.W.2    Sasaki, D.Y.3    Arnold, F.H.4
  • 37
    • 0029927807 scopus 로고    scopus 로고
    • Covalent immobilization of native biomolecules onto Au(111) via N-hydroxysuccinimide ester functionalized self-assembled monolayers for scanning probe microscopy
    • Wagner P., Hegner M., Kernen P., Zaugg F., Semenza G. Covalent immobilization of native biomolecules onto Au(111) via N-hydroxysuccinimide ester functionalized self-assembled monolayers for scanning probe microscopy. Biophys. J. 70:1996;2052-2066.
    • (1996) Biophys. J. , vol.70 , pp. 2052-2066
    • Wagner, P.1    Hegner, M.2    Kernen, P.3    Zaugg, F.4    Semenza, G.5
  • 39
    • 0028070376 scopus 로고
    • Existence of a molecular ruler in proteasomes suggested by analysis of degradation products
    • Wenzel T., Eckerskorn C., Lottspeich F., Baumeister B. Existence of a molecular ruler in proteasomes suggested by analysis of degradation products. FEBS Letters. 349:1994;205-209.
    • (1994) FEBS Letters , vol.349 , pp. 205-209
    • Wenzel, T.1    Eckerskorn, C.2    Lottspeich, F.3    Baumeister, B.4
  • 40
    • 0029920469 scopus 로고    scopus 로고
    • Antigen processing and presentation by the class I major histocompatibility complex
    • York I., Rock K. Antigen processing and presentation by the class I major histocompatibility complex. Annu. Rev. Immunol. 14:1996;369-396.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 369-396
    • York, I.1    Rock, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.