메뉴 건너뛰기




Volumn 398, Issue , 2005, Pages 414-425

Atomic force microscopy of the proteasome

Author keywords

[No Author keywords available]

Indexed keywords

BUFFER; MICA; PROTEASOME; PROTEIN; RESIN; SODIUM CHLORIDE;

EID: 27644467332     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(05)98034-8     Document Type: Review
Times cited : (9)

References (27)
  • 2
    • 0000006242 scopus 로고
    • Scanning tunneling microscopy
    • Binnig G., and Rohrer H. Scanning tunneling microscopy Helv. Phys. Acta 55 1982 726 735
    • (1982) Helv. Phys. Acta , vol.55 , pp. 726-735
    • Binnig, G.1    Rohrer, H.2
  • 4
    • 0033854391 scopus 로고    scopus 로고
    • Atomic force microscopy in structural biology: From the subcellular to the submolecular
    • Czajkowsky D.M., Iwamoto H., and Shao Z. Atomic force microscopy in structural biology: From the subcellular to the submolecular J. Electr. Micr. 49 2000 395 406
    • (2000) J. Electr. Micr. , vol.49 , pp. 395-406
    • Czajkowsky, D.M.1    Iwamoto, H.2    Shao, Z.3
  • 5
    • 0033591349 scopus 로고    scopus 로고
    • High-resolution AFM-imaging and mechanistic analysis of the 20 S proteasome
    • Dorn I.T., Eschrich R., Seemuller E., Guckenberger R., and Tampe R. High-resolution AFM-imaging and mechanistic analysis of the 20 S proteasome J. Mol. Biol. 288 1999 1027 1036
    • (1999) J. Mol. Biol. , vol.288 , pp. 1027-1036
    • Dorn, I.T.1    Eschrich, R.2    Seemuller, E.3    Guckenberger, R.4    Tampe, R.5
  • 6
    • 0035804929 scopus 로고    scopus 로고
    • Conformational spread in a ring of proteins: A stochastic approach to allostery
    • Duke T.A., Novere N.L., and Bray D. Conformational spread in a ring of proteins: A stochastic approach to allostery J. Mol. Biol. 308 2001 541 553
    • (2001) J. Mol. Biol. , vol.308 , pp. 541-553
    • Duke, T.A.1    Novere, N.L.2    Bray, D.3
  • 7
    • 0031274463 scopus 로고    scopus 로고
    • The atomic force microscope detects ATP-sensitive protein clusters in the plasma membrane of transformed MDCK cells
    • Ehrenhofer U., Rakowska A., Schneider S.W., Schwab A., and Oberleithner H. The atomic force microscope detects ATP-sensitive protein clusters in the plasma membrane of transformed MDCK cells Cell Biol. Int. 21 1997 737 746
    • (1997) Cell Biol. Int. , vol.21 , pp. 737-746
    • Ehrenhofer, U.1    Rakowska, A.2    Schneider, S.W.3    Schwab, A.4    Oberleithner, H.5
  • 8
    • 0043192299 scopus 로고    scopus 로고
    • The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation
    • Forster A., Whitby F.G., and Hill C.P. The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation EMBO J. 22 2003 4356 4364
    • (2003) EMBO J. , vol.22 , pp. 4356-4364
    • Forster, A.1    Whitby, F.G.2    Hill, C.P.3
  • 9
    • 0036005859 scopus 로고    scopus 로고
    • Imaging and manipulation of biological structures with the AFM
    • Fotiadis D., Scheuring S., Muller S.A., Engel A., and Muller D.J. Imaging and manipulation of biological structures with the AFM Micron 33 2002 385 397
    • (2002) Micron , vol.33 , pp. 385-397
    • Fotiadis, D.1    Scheuring, S.2    Muller, S.A.3    Engel, A.4    Muller, D.J.5
  • 10
    • 0042510141 scopus 로고    scopus 로고
    • Atomic force microscopy studies of interaction of the 20S proteasome with supported lipid bilayers
    • Furuike S., Hirokawa J., Yamada S., and Yamazaki M. Atomic force microscopy studies of interaction of the 20S proteasome with supported lipid bilayers Biochim. Biophys. Acta 1615 2003 1 6
    • (2003) Biochim. Biophys. Acta , vol.1615 , pp. 1-6
    • Furuike, S.1    Hirokawa, J.2    Yamada, S.3    Yamazaki, M.4
  • 11
    • 27644500950 scopus 로고    scopus 로고
    • Characterization of noncompetitive regulators of proteasome activity
    • Gaczynska M., and Osmulski P.A. Characterization of noncompetitive regulators of proteasome activity Methods Enzymol. 398 35 2005 2005 (this volume).
    • (2005) Methods Enzymol. , vol.398 , Issue.35
    • Gaczynska, M.1    Osmulski, P.A.2
  • 12
    • 0042848726 scopus 로고    scopus 로고
    • Proline- and arginine-rich peptides constitute a novel class of allosteric inhibitors of proteasome activity
    • Gaczynska M., Osmulski P.A., Gao Y., Post M.J., and Simons M. Proline- and arginine-rich peptides constitute a novel class of allosteric inhibitors of proteasome activity Biochemistry 42 2003 8663 8670
    • (2003) Biochemistry , vol.42 , pp. 8663-8670
    • Gaczynska, M.1    Osmulski, P.A.2    Gao, Y.3    Post, M.J.4    Simons, M.5
  • 13
    • 0037401695 scopus 로고    scopus 로고
    • Substrate access and processing by the 20S proteasome core particle
    • Groll M., and Huber R. Substrate access and processing by the 20S proteasome core particle Int. J. Bioch. Cell Biol. 35 2003 606 616
    • (2003) Int. J. Bioch. Cell Biol. , vol.35 , pp. 606-616
    • Groll, M.1    Huber, R.2
  • 17
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 a resolution
    • Lowe J., Stock D., Jap B., Zwickl P., Baumeister W., and Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution Science 268 1995 533 539
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 18
    • 0034607871 scopus 로고    scopus 로고
    • Atomic force microscopy reveals two conformations of the 20S proteasome from fission yeast
    • Osmulski P.A., and Gaczynska M. Atomic force microscopy reveals two conformations of the 20S proteasome from fission yeast J. Biol. Chem. 275 2000 13171 13174
    • (2000) J. Biol. Chem. , vol.275 , pp. 13171-13174
    • Osmulski, P.A.1    Gaczynska, M.2
  • 19
    • 0037018938 scopus 로고    scopus 로고
    • Nanoenzymology of the 20S proteasome: Proteasomal actions are controlled by the allosteric transition
    • Osmulski P.A., and Gaczynska M. Nanoenzymology of the 20S proteasome: Proteasomal actions are controlled by the allosteric transition Biochemistry 41 2002 7047 7053
    • (2002) Biochemistry , vol.41 , pp. 7047-7053
    • Osmulski, P.A.1    Gaczynska, M.2
  • 20
    • 1242271244 scopus 로고    scopus 로고
    • An overview of the biophysical applications of atomic force microscopy
    • Santos N.C., and Castanho M.A. An overview of the biophysical applications of atomic force microscopy Biophys. Chem. 107 2004 133 149
    • (2004) Biophys. Chem. , vol.107 , pp. 133-149
    • Santos, N.C.1    Castanho, M.A.2
  • 21
    • 0037184061 scopus 로고    scopus 로고
    • Specific orientation and two-dimensional crystallization of the proteasome at metal-chelating lipid interfaces
    • Thess A., Hutschenreiter S., Hofmann M., Tampe R., Baumeister W., and Guckenberger R. Specific orientation and two-dimensional crystallization of the proteasome at metal-chelating lipid interfaces J. Biol. Chem. 277 2002 36321 36328
    • (2002) J. Biol. Chem. , vol.277 , pp. 36321-36328
    • Thess, A.1    Hutschenreiter, S.2    Hofmann, M.3    Tampe, R.4    Baumeister, W.5    Guckenberger, R.6
  • 22
    • 0036191586 scopus 로고    scopus 로고
    • Structure determination of the constitutive 20S proteasome from bovine liver at 2.75 a resolution
    • Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N., and Tsukihara T. Structure determination of the constitutive 20S proteasome from bovine liver at 2.75 A resolution J. Biochem. 131 2002 171 173
    • (2002) J. Biochem. , vol.131 , pp. 171-173
    • Unno, M.1    Mizushima, T.2    Morimoto, Y.3    Tomisugi, Y.4    Tanaka, K.5    Yasuoka, N.6    Tsukihara, T.7
  • 26
    • 0037328523 scopus 로고    scopus 로고
    • Quantitative characterization of biomolecular assemblies and interactions using atomic force microscopy
    • Yang Y., Wang H., and Erie D.A. Quantitative characterization of biomolecular assemblies and interactions using atomic force microscopy Methods 29 2003 175 187
    • (2003) Methods , vol.29 , pp. 175-187
    • Yang, Y.1    Wang, H.2    Erie, D.A.3
  • 27
    • 0035716877 scopus 로고    scopus 로고
    • The proteasome: A supramolecular assembly designed for controlled proteolysis
    • Zwickl P., Seemuller E., Kapelari B., and Baumeister W. The proteasome: A supramolecular assembly designed for controlled proteolysis Adv. Prot. Chem. 59 2001 187 222
    • (2001) Adv. Prot. Chem. , vol.59 , pp. 187-222
    • Zwickl, P.1    Seemuller, E.2    Kapelari, B.3    Baumeister, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.