메뉴 건너뛰기




Volumn 74, Issue 6, 1998, Pages 2840-2849

Direct visualization of dynamic protein-DNA interactions with a dedicated atomic force microscope

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBODIPYRIMIDINE PHOTOLYASE; DNA;

EID: 0031836232     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77991-3     Document Type: Article
Times cited : (93)

References (29)
  • 1
    • 0019887628 scopus 로고
    • Diffusion-driven mechanism of protein translocation on nucleic acids. 1. Models and theory
    • Berg, O., R. B. Winter, and P. H. von Hippel. 1981. Diffusion-driven mechanism of protein translocation on nucleic acids. 1. Models and theory. Biochemistry. 20:6929-6948.
    • (1981) Biochemistry , vol.20 , pp. 6929-6948
    • Berg, O.1    Winter, R.B.2    Von Hippel, P.H.3
  • 2
    • 34347209835 scopus 로고
    • Calculation of thermal noise in atomic force microscopy
    • Butt, H.-J., and M. Jaschke. 1995. Calculation of thermal noise in atomic force microscopy. Nanotechnology. 6:1-7.
    • (1995) Nanotechnology , vol.6 , pp. 1-7
    • Butt, H.-J.1    Jaschke, M.2
  • 3
    • 0025257431 scopus 로고
    • Biological significance of facilitated diffusion in protein-DNA interactions
    • Dowd, D. R., and R. S. Lloyd. 1990. Biological significance of facilitated diffusion in protein-DNA interactions. J. Biol. Chem. 265:3424-3431.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3424-3431
    • Dowd, D.R.1    Lloyd, R.S.2
  • 4
    • 0025272139 scopus 로고
    • DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans
    • Eker, A. P. M., P. Kooiman, J. K. C. Hessels, and A. Yasui. 1990. DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans. J. Biol. Chem. 265:8009-815.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8009-8815
    • Eker, A.P.M.1    Kooiman, P.2    Hessels, J.K.C.3    Yasui, A.4
  • 5
    • 0028631162 scopus 로고
    • DNA bending by Cro protein in specific and nonspecific complexes: Implications for protein site recognition and specifity
    • Erie, D. A., G. Yang, H. C. Schultz, and C. Bustamante. 1994. DNA bending by Cro protein in specific and nonspecific complexes: implications for protein site recognition and specifity. Science. 266:1562-1566.
    • (1994) Science , vol.266 , pp. 1562-1566
    • Erie, D.A.1    Yang, G.2    Schultz, H.C.3    Bustamante, C.4
  • 6
    • 0028140707 scopus 로고
    • Intermolecular forces and energies between ligands and receptors
    • Florin, E.-L., V. T. Moy, and H. E. Gaub. 1994. Intermolecular forces and energies between ligands and receptors. Science. 266:257-259.
    • (1994) Science , vol.266 , pp. 257-259
    • Florin, E.-L.1    Moy, V.T.2    Gaub, H.E.3
  • 7
    • 0028559915 scopus 로고
    • Following the assembly of RNA polymerase-DNA complexes in aqueous solutions with the scanning force microscope
    • Guthold, M., M. Bezanilla, D. A. Erie, B. Jenkins, H. G. Hansma, and C. Bustamante. 1994. Following the assembly of RNA polymerase-DNA complexes in aqueous solutions with the scanning force microscope. Proc. Natl. Acad. Sci. USA. 91:12927-12931.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12927-12931
    • Guthold, M.1    Bezanilla, M.2    Erie, D.A.3    Jenkins, B.4    Hansma, H.G.5    Bustamante, C.6
  • 8
    • 0001116334 scopus 로고    scopus 로고
    • A magnetically driven oscillating probe microscope for operations in liquids
    • Han, W., and S. M. Lindsay. 1996. A magnetically driven oscillating probe microscope for operations in liquids. Appl. Phys. Lett. 69:4111-4113.
    • (1996) Appl. Phys. Lett. , vol.69 , pp. 4111-4113
    • Han, W.1    Lindsay, S.M.2
  • 9
    • 0031562553 scopus 로고    scopus 로고
    • Kinked DNA
    • Han, W., and S. M. Lindsay. 1997. Kinked DNA. Nature. 386:563.
    • (1997) Nature , vol.386 , pp. 563
    • Han, W.1    Lindsay, S.M.2
  • 10
    • 5544228349 scopus 로고
    • Atomic force microscopy of biomolecules
    • Hansma, H. G. 1995. Atomic force microscopy of biomolecules. J. Vac. Sci. Technol. B. 14:1390-1395.
    • (1995) J. Vac. Sci. Technol. B , vol.14 , pp. 1390-1395
    • Hansma, H.G.1
  • 11
    • 0029863919 scopus 로고    scopus 로고
    • DNA binding correlates with cationic radius: Assay by atomic force microscopy
    • Hansma, H. G., and D. E. Laney. 1996. DNA binding correlates with cationic radius: assay by atomic force microscopy. Biophys. J. 70: 1933-1939.
    • (1996) Biophys. J. , vol.70 , pp. 1933-1939
    • Hansma, H.G.1    Laney, D.E.2
  • 13
    • 0029866788 scopus 로고    scopus 로고
    • Atomic force microscopy of long and short double-stranded, single-stranded and triple-stranded nucleic acids
    • Hansma, H. G., I. Revenko, K. Kim, and D. E. Laney. 1996. Atomic force microscopy of long and short double-stranded, single-stranded and triple-stranded nucleic acids. Nucleic Acids Res. 24:713-720.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 713-720
    • Hansma, H.G.1    Revenko, I.2    Kim, K.3    Laney, D.E.4
  • 14
    • 0029054227 scopus 로고
    • The structure of photolyase: Using photon energy for DNA repair
    • Hearst, J. E. 1995. The structure of photolyase: using photon energy for DNA repair. Science. 268:1858-1868.
    • (1995) Science , vol.268 , pp. 1858-1868
    • Hearst, J.E.1
  • 16
    • 0028157680 scopus 로고
    • Biological applications of atomic force microscopy
    • Lal, R., and S. A. John, 1994. Biological applications of atomic force microscopy. Am. J. Physiol. 266:1-21.
    • (1994) Am. J. Physiol. , vol.266 , pp. 1-21
    • Lal, R.1    John, S.A.2
  • 17
    • 0028812143 scopus 로고
    • Crystal structure of DNA photolyase from Escherichia coli
    • Park, H.-W., S.-T. Kim, A. Sancar, and J. Deisenhofer. 1995. Crystal structure of DNA photolyase from Escherichia coli. Science. 268: 1866-1872.
    • (1995) Science , vol.268 , pp. 1866-1872
    • Park, H.-W.1    Kim, S.-T.2    Sancar, A.3    Deisenhofer, J.4
  • 19
    • 0028031337 scopus 로고
    • Direct observation of enzyme activity with the atomic force microscope
    • Radmacher, M., M. Fritz, H. G. Hansma, and P. K. Hansma. 1994. Direct observation of enzyme activity with the atomic force microscope. Science. 265:1577-1579.
    • (1994) Science , vol.265 , pp. 1577-1579
    • Radmacher, M.1    Fritz, M.2    Hansma, H.G.3    Hansma, P.K.4
  • 21
    • 0028117141 scopus 로고
    • Structure and function of DNA photolyase
    • Sancar, A. 1994. Structure and function of DNA photolyase. Biochemistry. 33:2-9.
    • (1994) Biochemistry , vol.33 , pp. 2-9
    • Sancar, A.1
  • 28
    • 0028831314 scopus 로고
    • Determination of heat-shock transcription factor 2 stoichiometry at looped DNA complexes using scanning force microscopy
    • Wyman, C., E. Grottkopp, C. Bustamante, and H. C. M. Nelson. 1995. Determination of heat-shock transcription factor 2 stoichiometry at looped DNA complexes using scanning force microscopy. EMBO J. 14:117-123.
    • (1995) EMBO J. , vol.14 , pp. 117-123
    • Wyman, C.1    Grottkopp, E.2    Bustamante, C.3    Nelson, H.C.M.4
  • 29
    • 0030894489 scopus 로고    scopus 로고
    • Unusual oligomerisation required for activity of NtrC, a bacterial enhancer-binding protein
    • Wyman, C., I. Rombel, A. K. North, C. Bustamante, and S. Kustu. 1997. Unusual oligomerisation required for activity of NtrC, a bacterial enhancer-binding protein. Science. 275:1658-1661.
    • (1997) Science , vol.275 , pp. 1658-1661
    • Wyman, C.1    Rombel, I.2    North, A.K.3    Bustamante, C.4    Kustu, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.