메뉴 건너뛰기




Volumn 28, Issue 8, 2000, Pages 611-620

Imaging microtubules and kinesin decorated microtubules using tapping mode atomic force microscopy in fluids

Author keywords

Atomic force microscopy; Kinesin; Microtubules

Indexed keywords

ADENOSINE TRIPHOSPHATE DERIVATIVE; ADENYLYLIMIDODIPHOSPHATE; GLASS; KINESIN; PALMITIC ACID DERIVATIVE; SILANE DERIVATIVE;

EID: 0033964571     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490050001     Document Type: Article
Times cited : (35)

References (41)
  • 2
    • 0029252016 scopus 로고
    • Adsorption of DNA to mica, silylated mica and minerals: Characterization by atomic force microscopy
    • Bezanilla M, Manne S, Laney DE, Lyubchenko YL, Hansma HG (1995) Adsorption of DNA to mica, silylated mica and minerals: characterization by atomic force microscopy. Langmuir 11: 655-659
    • (1995) Langmuir , vol.11 , pp. 655-659
    • Bezanilla, M.1    Manne, S.2    Laney, D.E.3    Lyubchenko, Y.L.4    Hansma, H.G.5
  • 4
    • 0030948539 scopus 로고    scopus 로고
    • Real engines of creation
    • Block SM (1997) Real engines of creation. Nature 386: 217-219
    • (1997) Nature , vol.386 , pp. 217-219
    • Block, S.M.1
  • 5
    • 0028678828 scopus 로고
    • Motor proteins 1: Kinesins
    • Bloom GS, Endow SA (1994) Motor proteins 1: kinesins. Protein Profile 1: 1059-1106
    • (1994) Protein Profile , vol.1 , pp. 1059-1106
    • Bloom, G.S.1    Endow, S.A.2
  • 6
    • 0023944514 scopus 로고
    • Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptide
    • Bloom GS, Wagner MC, Pfister KK, Brady ST (1988) Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptide. Biochemistry 27: 3409-3416
    • (1988) Biochemistry , vol.27 , pp. 3409-3416
    • Bloom, G.S.1    Wagner, M.C.2    Pfister, K.K.3    Brady, S.T.4
  • 7
    • 0030930491 scopus 로고    scopus 로고
    • Microtubules: A brief historical perspective
    • Brinkley WBR (1997) Microtubules: a brief historical perspective. J Struct Biol 118: 84-86
    • (1997) J Struct Biol , vol.118 , pp. 84-86
    • Brinkley, W.B.R.1
  • 8
    • 0028215348 scopus 로고
    • Granula motion and membrane spreading during activation of human platelets imaged by atomic force microscopy
    • Fritz M, Radmacher M, Gaub HE (1994) Granula motion and membrane spreading during activation of human platelets imaged by atomic force microscopy. Biophys J 66: 1328-1334
    • (1994) Biophys J , vol.66 , pp. 1328-1334
    • Fritz, M.1    Radmacher, M.2    Gaub, H.E.3
  • 12
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa N (1998) Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279: 519-5265
    • (1998) Science , vol.279 , pp. 519-5265
    • Hirokawa, N.1
  • 13
    • 0028979598 scopus 로고
    • Nucleotide-dependent angular change in kinesin motor domain bound to tubulin
    • Hirose K, Lockhart A, Cross RA, Amos LA (1995) Nucleotide-dependent angular change in kinesin motor domain bound to tubulin. Nature 376: 277-279
    • (1995) Nature , vol.376 , pp. 277-279
    • Hirose, K.1    Lockhart, A.2    Cross, R.A.3    Amos, L.A.4
  • 14
    • 0032550175 scopus 로고    scopus 로고
    • Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: Comparison with X-ray structure and implications for motility
    • Hoenger A, Sack S, Thormählen M, Marx A, Müller J, Gross H, Mandelkow E (1998) Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: comparison with X-ray structure and implications for motility. J Cell Biol 141: 419-430
    • (1998) J Cell Biol , vol.141 , pp. 419-430
    • Hoenger, A.1    Sack, S.2    Thormählen, M.3    Marx, A.4    Müller, J.5    Gross, H.6    Mandelkow, E.7
  • 15
    • 0028276694 scopus 로고
    • Surface morphology and mechanical properties of MDCK monolayers by atomic force microscopy
    • Hoh JH, Schoenenberger C-A (1994) Surface morphology and mechanical properties of MDCK monolayers by atomic force microscopy. Biophys J 107: 1105-1114
    • (1994) Biophys J , vol.107 , pp. 1105-1114
    • Hoh, J.H.1    Schoenenberger, C.-A.2
  • 16
    • 0027163746 scopus 로고
    • Structure of the extracellular surface of the gap junction by atomic force microscopy
    • Hoh J, Sosinsky GE, Revel J-P, Hansma PK (1993) Structure of the extracellular surface of the gap junction by atomic force microscopy. Biophys J 65: 149-163
    • (1993) Biophys J , vol.65 , pp. 149-163
    • Hoh, J.1    Sosinsky, G.E.2    Revel, J.-P.3    Hansma, P.K.4
  • 18
    • 0027138210 scopus 로고
    • Covalent binding of biological samples to solid supports for scanning probe microscopy in buffer solution
    • Karrasch S, Dolder M, Schabert F, Ramsden J, Engel A (1993) Covalent binding of biological samples to solid supports for scanning probe microscopy in buffer solution. Biophys J 65: 2437-2446
    • (1993) Biophys J , vol.65 , pp. 2437-2446
    • Karrasch, S.1    Dolder, M.2    Schabert, F.3    Ramsden, J.4    Engel, A.5
  • 19
    • 0028087275 scopus 로고
    • Atomic force microscopy produces faithful high-resolution images of protein surfaces in an aqueous environment
    • Karrasch S, Hegerl R, Hoh JH, Baumeister W, Engel A (1994) Atomic force microscopy produces faithful high-resolution images of protein surfaces in an aqueous environment. Proc Natl Acad Sci USA 91: 836-838
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 836-838
    • Karrasch, S.1    Hegerl, R.2    Hoh, J.H.3    Baumeister, W.4    Engel, A.5
  • 20
    • 0026899346 scopus 로고
    • Sharp, vertical-walled tips for SFM imaging of steep or soft samples
    • 1481-1489
    • Keller D, Deputy D, Alduino A, Luo K (1992) Sharp, vertical-walled tips for SFM imaging of steep or soft samples. Ultramicroscopy 42-44: 1481-1489
    • (1992) Ultramicroscopy , pp. 42-44
    • Keller, D.1    Deputy, D.2    Alduino, A.3    Luo, K.4
  • 21
    • 0028979606 scopus 로고
    • Three-dimensional structure of the kinesin head-microtubule complex
    • Kikkawa M, Ishikawa T, Wakabayashi T, Hirokawa N (1995) Three-dimensional structure of the kinesin head-microtubule complex. Nature 376: 274-276
    • (1995) Nature , vol.376 , pp. 274-276
    • Kikkawa, M.1    Ishikawa, T.2    Wakabayashi, T.3    Hirokawa, N.4
  • 22
    • 0022483059 scopus 로고
    • On the surface lattice of microtubules: Helix starts, protofilament number, seam, and handedness
    • Mandelkow E-M, Schultheiss R, Rapp R, Müller M, Mandelkow E (1986) On the surface lattice of microtubules: helix starts, protofilament number, seam, and handedness. J Cell Biol 102: 1067-1073
    • (1986) J Cell Biol , vol.102 , pp. 1067-1073
    • Mandelkow, E.-M.1    Schultheiss, R.2    Rapp, R.3    Müller, M.4    Mandelkow, E.5
  • 23
    • 0030962705 scopus 로고    scopus 로고
    • Diffraction by helical structures with seams: Microtubules
    • Metoz F, Wade RH (1997) Diffraction by helical structures with seams: microtubules. J Struct Biol 118: 128-139
    • (1997) J Struct Biol , vol.118 , pp. 128-139
    • Metoz, F.1    Wade, R.H.2
  • 24
    • 0028998339 scopus 로고
    • Force-induced conformational change of bacteriohodopsin
    • Müller DJ, Büldt G, Engel A (1995a) Force-induced conformational change of bacteriohodopsin. J Mol Biol 249: 239-243
    • (1995) J Mol Biol , vol.249 , pp. 239-243
    • Müller, D.J.1    Büldt, G.2    Engel, A.3
  • 25
    • 0028957621 scopus 로고
    • Imaging purple membranes in aqueous solutions at sub-nanometer resolution by atomic force microscopy
    • Müller DJ, Schabert FA, Büldt G, Engel A (1995b) Imaging purple membranes in aqueous solutions at sub-nanometer resolution by atomic force microscopy. Biophys J 68: 1681-1686
    • (1995) Biophys J , vol.68 , pp. 1681-1686
    • Müller, D.J.1    Schabert, F.A.2    Büldt, G.3    Engel, A.4
  • 26
    • 0029063397 scopus 로고
    • Structure of tubulin at 6.5 Å and location of the taxol-binding site
    • Nogales E, Wolf SG, Khan I, Luduena RF, Downig KH (1995) Structure of tubulin at 6.5 Å and location of the taxol-binding site. Nature 375: 424-427
    • (1995) Nature , vol.375 , pp. 424-427
    • Nogales, E.1    Wolf, S.G.2    Khan, I.3    Luduena, R.F.4    Downig, K.H.5
  • 27
    • 0031010399 scopus 로고    scopus 로고
    • Visualizing the secondary structure of tubulin: Three-dimensional map at 4 Å
    • Nogales E, Wolf SG, Downing KH (1997) Visualizing the secondary structure of tubulin: three-dimensional map at 4 Å. J Struct Biol 118: 119-127
    • (1997) J Struct Biol , vol.118 , pp. 119-127
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 28
    • 0026917533 scopus 로고
    • From molecules to cells - Imaging soft samples with the AFM
    • Radmacher M, Tillmann RW, Fritz M, Gaub HE (1992) From molecules to cells - imaging soft samples with the AFM. Science 257: 1900-1905
    • (1992) Science , vol.257 , pp. 1900-1905
    • Radmacher, M.1    Tillmann, R.W.2    Fritz, M.3    Gaub, H.E.4
  • 29
    • 0028031337 scopus 로고
    • Direct observation of enzyme activity with the atomic force microscope
    • Radmacher M, Fritz M, Hansma HG, Hansma PK (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
  • 30
    • 0030053843 scopus 로고    scopus 로고
    • Measuring viscoelastic properties of human platelets with the atomic force microscope
    • Radmacher M, Fritz M, Kacher CM, Cleveland JP, Hansma PK (1996) Measuring viscoelastic properties of human platelets with the atomic force microscope. Biophys J 70: 556-567
    • (1996) Biophys J , vol.70 , pp. 556-567
    • Radmacher, M.1    Fritz, M.2    Kacher, C.M.3    Cleveland, J.P.4    Hansma, P.K.5
  • 31
    • 0030033874 scopus 로고    scopus 로고
    • Vertical dimension of hydrated biological samples in tapping mode scanning force microscopy
    • Schabert FA, Rabe JP (1996) Vertical dimension of hydrated biological samples in tapping mode scanning force microscopy. Biophys J 70: 1514-1520
    • (1996) Biophys J , vol.70 , pp. 1514-1520
    • Schabert, F.A.1    Rabe, J.P.2
  • 32
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • Svoboda K, Schmidt CF, Schnapp BJ, Block SM (1993) Direct observation of kinesin stepping by optical trapping interferometry. Nature 365: 721-727
    • (1993) Nature , vol.365 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 34
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
    • Vale RD, Reese TS, Sheetz MP (1985) Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell 42: 39-50
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 36
    • 0031055639 scopus 로고    scopus 로고
    • Microtubule structure and dynamics
    • Wade RH, Hyman AA (1997) Microtubule structure and dynamics. Curr Opin Cell Biol 9: 12-17
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 12-17
    • Wade, R.H.1    Hyman, A.A.2
  • 37
    • 36449000481 scopus 로고
    • Sharpened electron beam deposited tips for high resolution atomic force microscope lithography and imaging
    • Wendel M, Lorenz H, Kotthaus JP (1995) Sharpened electron beam deposited tips for high resolution atomic force microscope lithography and imaging. Appl Phys Lett 67: 3732-3734
    • (1995) Appl Phys Lett , vol.67 , pp. 3732-3734
    • Wendel, M.1    Lorenz, H.2    Kotthaus, J.P.3
  • 38
    • 0020009818 scopus 로고
    • Preparation of tubulin from brain
    • Williams RCJ, Lee JC (1982) Preparation of tubulin from brain. Methods Enzymol 85: 376-385
    • (1982) Methods Enzymol , vol.85 , pp. 376-385
    • Williams, R.C.J.1    Lee, J.C.2
  • 39
    • 0025362646 scopus 로고
    • Evidence that the head of kinesin is sufficient for force generation and motility in vitro
    • Yang JT, Saxton WM, Stewart RJ, Raff E, Goldstein LSB (1990) Evidence that the head of kinesin is sufficient for force generation and motility in vitro. Science 249: 42-47
    • (1990) Science , vol.249 , pp. 42-47
    • Yang, J.T.1    Saxton, W.M.2    Stewart, R.J.3    Raff, E.4    Goldstein, L.S.B.5
  • 40
    • 0027406608 scopus 로고
    • New approach for atomic force microscopy of membrane proteins - The imaging of cholera toxin
    • Yang J, Tamm LK, Tillack TW, Shao Z (1993) New approach for atomic force microscopy of membrane proteins - the imaging of cholera toxin. J Mol Biol 229: 286-290
    • (1993) J Mol Biol , vol.229 , pp. 286-290
    • Yang, J.1    Tamm, L.K.2    Tillack, T.W.3    Shao, Z.4
  • 41
    • 0032590170 scopus 로고    scopus 로고
    • Thermotropic structural changes of saturated-cationic-lipid-DNA complexes
    • Zantl R, Artzner F, Rapp G, Rädler JO (1999) Thermotropic structural changes of saturated-cationic-lipid-DNA complexes. Europhys Lett 45: 90-96
    • (1999) Europhys Lett , vol.45 , pp. 90-96
    • Zantl, R.1    Artzner, F.2    Rapp, G.3    Rädler, J.O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.