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Volumn 93, Issue 2, 1998, Pages 277-287

Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; KATANIN; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 18344403503     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81578-0     Document Type: Article
Times cited : (283)

References (58)
  • 1
    • 0027488417 scopus 로고
    • Anchor-ligated cDNA libraries: A technique for generating acDNA library for the immediate cloning of the 5′ ends of mRNAs
    • Apte, A.N., and Siebert, P.D. (1993). Anchor-ligated cDNA libraries: a technique for generating acDNA library for the immediate cloning of the 5′ ends of mRNAs. Biotechniques 15, 890-893.
    • (1993) Biotechniques , vol.15 , pp. 890-893
    • Apte, A.N.1    Siebert, P.D.2
  • 2
    • 0030048731 scopus 로고    scopus 로고
    • Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules
    • Belmont, LD., and Mitchison, T.J. (1996). Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules. Cell 84, 623-631.
    • (1996) Cell , vol.84 , pp. 623-631
    • Belmont, L.D.1    Mitchison, T.J.2
  • 3
    • 0025109181 scopus 로고
    • Real-time visualization of cell cycle-dependent changes in microtubule dynamics in cytoplasmic extracts
    • Belmont, L.D., Hyman, A.A., Sawin, K.E., and Mitchison, T.J. (1990). Real-time visualization of cell cycle-dependent changes in microtubule dynamics in cytoplasmic extracts. Cell 62, 579-589.
    • (1990) Cell , vol.62 , pp. 579-589
    • Belmont, L.D.1    Hyman, A.A.2    Sawin, K.E.3    Mitchison, T.J.4
  • 4
    • 0026046950 scopus 로고
    • Tau protein binds to microtubules through a flexible array of distributed weak sites
    • Butner, K., and Kirschner, M. (1991). Tau protein binds to microtubules through a flexible array of distributed weak sites. J. Cell Biol. 115, 717-730.
    • (1991) J. Cell Biol. , vol.115 , pp. 717-730
    • Butner, K.1    Kirschner, M.2
  • 5
    • 0029989442 scopus 로고    scopus 로고
    • Evidence that a single monolayer tubulin-GTP cap is both necessary and sufficient to stabilize microtubules
    • Caplow, M., and Shanks, J. (1996). Evidence that a single monolayer tubulin-GTP cap is both necessary and sufficient to stabilize microtubules. Mol. Biol. Cell 7, 663-675.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 663-675
    • Caplow, M.1    Shanks, J.2
  • 6
    • 0028147310 scopus 로고
    • mei-1, a gene required for meiotic spindle formation in Caenorhabditis elegans, is a member of a family of ATPases
    • Clark-Maguire, S., and Mains, P.E. (1994a). mei-1, a gene required for meiotic spindle formation in Caenorhabditis elegans, is a member of a family of ATPases. Genetics 136, 533-546.
    • (1994) Genetics , vol.136 , pp. 533-546
    • Clark-Maguire, S.1    Mains, P.E.2
  • 7
    • 0028236624 scopus 로고
    • Localization of the mei-1 gene product of Caenorhabditis elegans, a meiotic-specific spindle component
    • Clark-Maguire, S., and Mains, P.E. (1994b). Localization of the mei-1 gene product of Caenorhabditis elegans, a meiotic-specific spindle component. J. Cell Biol. 126, 199-209.
    • (1994) J. Cell Biol. , vol.126 , pp. 199-209
    • Clark-Maguire, S.1    Mains, P.E.2
  • 8
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri, F., and Duguet, M. (1995). A 200-amino acid ATPase module in search of a basic function. BioEssays 17, 639-650.
    • (1995) Bioessays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 9
    • 0028833289 scopus 로고
    • A new role for motor proteins as couplers to depolymerizing microtubules
    • Desai, A., and Mitchison, T.J. (1995). A new role for motor proteins as couplers to depolymerizing microtubules. J. Cell Biol. 128, 1-4.
    • (1995) J. Cell Biol. , vol.128 , pp. 1-4
    • Desai, A.1    Mitchison, T.J.2
  • 11
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel, D.N., Hyman, A.A., Cobb, M.H., and Kirschner, M.W. (1992). Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell. 3, 1141-1154.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 12
    • 0030297912 scopus 로고    scopus 로고
    • Crystal structure at 2.4 Å resolution of the complex of transducin βγ and its regulator, phosducin
    • Gaudet, R., Bohm, A., and Sigler, P.B. (1996). Crystal structure at 2.4 Å resolution of the complex of transducin βγ and its regulator, phosducin. Cell 87, 577-588.
    • (1996) Cell , vol.87 , pp. 577-588
    • Gaudet, R.1    Bohm, A.2    Sigler, P.B.3
  • 13
    • 0027163090 scopus 로고
    • Expression, purification, and characterization of the Drosophila kinesin motor domain produced in Escherichia coli
    • Gilbert, S.P., and Johnson, K.A. (1993). Expression, purification, and characterization of the Drosophila kinesin motor domain produced in Escherichia coli. Biochemistry 32, 4677-4684.
    • (1993) Biochemistry , vol.32 , pp. 4677-4684
    • Gilbert, S.P.1    Johnson, K.A.2
  • 14
    • 1542353988 scopus 로고
    • Kinesin ATPase: Rate-limiting ADP release
    • Hackney, D.O. (1988). Kinesin ATPase: rate-limiting ADP release. Proc. Natl. Acad. Sci. USA 85, 6314-6318.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6314-6318
    • Hackney, D.O.1
  • 15
    • 0029075363 scopus 로고
    • The N-ethylmaleimide-sensitive fusion protein and α-SNAP induce a conformational change in syntaxin
    • Hanson, P.I., Otto,H., Barton, N.,and Jahn, R. (1995).The N-ethylmaleimide-sensitive fusion protein and α-SNAP induce a conformational change in syntaxin. J. Biol. Chem. 270, 16955-16961.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16955-16961
    • Hanson, P.I.1    Barton, N.2    Jahn, R.3
  • 16
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P.I., Roth, R., Morisake, H., Jahn, R., and Heuser, J.E. (1997). Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisake, H.3    Jahn, R.4    Heuser, J.E.5
  • 17
    • 0003448569 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Harlow, E., and Lane, D. (1988). Antibodies: A Laboratory Manual (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press).
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 18
    • 0029004741 scopus 로고
    • Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro
    • Hayashi, T., Yamasaki, S., Nauenburg, S., Binz, T., and Neimann, H. (1995). Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro. EMBO J. 14, 2317-2325.
    • (1995) EMBO J. , vol.14 , pp. 2317-2325
    • Hayashi, T.1    Yamasaki, S.2    Nauenburg, S.3    Binz, T.4    Neimann, H.5
  • 19
    • 0023185013 scopus 로고
    • Is microtubule assembly a biphasic process? A fluorimetric study using 4′,6-diamidino-2-phenylindole as a probe
    • Heusele, C., Bonne, D., and Carlier, M.F. (1987). Is microtubule assembly a biphasic process? A fluorimetric study using 4′,6-diamidino-2-phenylindole as a probe. Eur. J. Biochem. 165, 613-620.
    • (1987) Eur. J. Biochem. , vol.165 , pp. 613-620
    • Heusele, C.1    Bonne, D.2    Carlier, M.F.3
  • 20
    • 0021095633 scopus 로고
    • Procedure for freeze-drying molecules adsorbed to mica flakes
    • Heuser, J.E. (1983). Procedure for freeze-drying molecules adsorbed to mica flakes. J. Mol. Biol. 169, 155-195.
    • (1983) J. Mol. Biol. , vol.169 , pp. 155-195
    • Heuser, J.E.1
  • 21
    • 0024416678 scopus 로고
    • Procedure for 3-D visualization of molecules on mica via the quick-freeze, deep-etch technique
    • Heuser, J. (1989). Procedure for 3-D visualization of molecules on mica via the quick-freeze, deep-etch technique. J. Electron Microsc. Technique 13, 244-263.
    • (1989) J. Electron Microsc. Technique , vol.13 , pp. 244-263
    • Heuser, J.1
  • 22
    • 0022492523 scopus 로고
    • Visualization of the dynamic instability of individual microtubules by dark-field microscopy
    • Horio, T., and Hotani, H. (1986). Visualization of the dynamic instability of individual microtubules by dark-field microscopy. Nature 321, 605-607.
    • (1986) Nature , vol.321 , pp. 605-607
    • Horio, T.1    Hotani, H.2
  • 24
    • 0026559120 scopus 로고
    • S-carboxymethylation of proteins transferred onto polyvinylidene difluoride membranes followed by in situ protease digestion and amino acid microsequencing
    • Iwamatsu, A. (1992). S-carboxymethylation of proteins transferred onto polyvinylidene difluoride membranes followed by in situ protease digestion and amino acid microsequencing. Electrophoresis 13, 142-147.
    • (1992) Electrophoresis , vol.13 , pp. 142-147
    • Iwamatsu, A.1
  • 25
    • 0026538817 scopus 로고
    • Gamma-tubulin is a centrosomal protein required for cell cycle-dependent microtubule nucleation
    • Joshi, H.C., Palacios, M.J., McNamara, L., and Cleveland, D.W. (1992). Gamma-tubulin is a centrosomal protein required for cell cycle-dependent microtubule nucleation. Nature 356, 80-83.
    • (1992) Nature , vol.356 , pp. 80-83
    • Joshi, H.C.1    Palacios, M.J.2    McNamara, L.3    Cleveland, D.W.4
  • 27
    • 0002447019 scopus 로고
    • Reorganization of microtubules during mitosis in Dictyostelium: Dissociation from MTOC and selective assembly/disassembly in situ
    • Kitanishi-Yumura, T., and Fukui, Y. (1987). Reorganization of microtubules during mitosis in Dictyostelium: dissociation from MTOC and selective assembly/disassembly in situ. Cell Motil. Cytoskeleton 8, 106-117.
    • (1987) Cell Motil. Cytoskeleton , vol.8 , pp. 106-117
    • Kitanishi-Yumura, T.1    Fukui, Y.2
  • 28
    • 0022497304 scopus 로고
    • The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate
    • Kodama, T., Fukui, K., and Kometani, K. (1986). The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate. J. Biochem. 99, 1465-1472.
    • (1986) J. Biochem. , vol.99 , pp. 1465-1472
    • Kodama, T.1    Fukui, K.2    Kometani, K.3
  • 29
    • 0030825790 scopus 로고    scopus 로고
    • Residues in the WD repeats of Tup1 required for interaction with alpha-2
    • Komachi, K., and Johnson, A.D. (1997). Residues in the WD repeats of Tup1 required for interaction with alpha-2. Mol. Cell. Biol. 17, 6023-6028.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6023-6028
    • Komachi, K.1    Johnson, A.D.2
  • 30
    • 0028034201 scopus 로고
    • The WD repeats of Tup1 interact with the homeo domain protein alpha 2
    • Komachi, K., Redd, M.J., and Johnson, A.D. (1994). The WD repeats of Tup1 interact with the homeo domain protein alpha 2. Genes Dev. 8, 2857-2867.
    • (1994) Genes Dev. , vol.8 , pp. 2857-2867
    • Komachi, K.1    Redd, M.J.2    Johnson, A.D.3
  • 31
    • 0027285334 scopus 로고
    • Microtubule-associated protein 2 alters the dynamic properties of microtubule assembly and disassembly
    • Kowalski, R.J., and Williams, R.J. (1993). Microtubule-associated protein 2 alters the dynamic properties of microtubule assembly and disassembly. J. Biol. Chem. 268, 9847-9855.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9847-9855
    • Kowalski, R.J.1    Williams, R.J.2
  • 32
    • 0028862359 scopus 로고
    • Malignant transformation of human fibroblast strain MSU-1.1 by v-fes requires an additional genetic change
    • Lin, C., Maher, V., and McCormick, J. (1995). Malignant transformation of human fibroblast strain MSU-1.1 by v-fes requires an additional genetic change. Int. J. Cancer 63, 140-147.
    • (1995) Int. J. Cancer , vol.63 , pp. 140-147
    • Lin, C.1    Maher, V.2    McCormick, J.3
  • 33
    • 0027209690 scopus 로고
    • Efficient generation of infections recombinant baculoviruses by site-specific transposon-mediated insertion of foreign genes into a baculovirus genome propagated in Escherichia coli
    • Luckow, V.A., Lee, S.C., Barry, G.F., and Olins, P.O. (1993). Efficient generation of infections recombinant baculoviruses by site-specific transposon-mediated insertion of foreign genes into a baculovirus genome propagated in Escherichia coli. J. Virol. 67, 4566-4579.
    • (1993) J. Virol. , vol.67 , pp. 4566-4579
    • Luckow, V.A.1    Lee, S.C.2    Barry, G.F.3    Olins, P.O.4
  • 34
    • 0022993689 scopus 로고
    • ATPase activities and actin-binding properties of subfragments of acanthamoeba myosin IA
    • Lynch, T.J., Albanesi, J.P., Korn, E.D., Robinson, E.A., Bowers, B., and Fujisaki, H. (1986). ATPase activities and actin-binding properties of subfragments of acanthamoeba myosin IA. J. Biol. Chem. 261, 17156-17162.
    • (1986) J. Biol. Chem. , vol.261 , pp. 17156-17162
    • Lynch, T.J.1    Albanesi, J.P.2    Korn, E.D.3    Robinson, E.A.4    Bowers, B.5    Fujisaki, H.6
  • 35
    • 0027424297 scopus 로고
    • Identification of katanin, an ATPase that severs and disassembles stable microtubules
    • McNally, F.J., and Vale, R.D. (1993). Identification of katanin, an ATPase that severs and disassembles stable microtubules. Cell 75, 419-429.
    • (1993) Cell , vol.75 , pp. 419-429
    • McNally, F.J.1    Vale, R.D.2
  • 36
    • 0029978787 scopus 로고    scopus 로고
    • Katanin, the microtubule-severing ATPase, is concentrated at centrosomes
    • McNally, F., Okawa, K., Iwamatsu, A., and Vale, R. (1996). Katanin, the microtubule-severing ATPase, is concentrated at centrosomes. J. Cell Sci. 109, 561-567.
    • (1996) J. Cell Sci. , vol.109 , pp. 561-567
    • McNally, F.1    Okawa, K.2    Iwamatsu, A.3    Vale, R.4
  • 37
    • 0024369644 scopus 로고
    • Polewards microtubule flux in the mitotic spindle: Evidence from photoactivation of fluorescence
    • Mitchison, T.J. (1989). Polewards microtubule flux in the mitotic spindle: evidence from photoactivation of fluorescence. J. Cell Biol. 109, 637-652.
    • (1989) J. Cell Biol. , vol.109 , pp. 637-652
    • Mitchison, T.J.1
  • 38
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison, T., and Kirschner, M. (1984). Dynamic instability of microtubule growth. Nature 312, 237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 39
    • 0028149757 scopus 로고
    • The ATPase activity of N-ethylmaleimide-sensitive fusion protein (NSF) is regulated by soluble NSF attachment proteins
    • Morgan, A., Dimaline, R., and Burgoyne, R.D. (1994). The ATPase activity of N-ethylmaleimide-sensitive fusion protein (NSF) is regulated by soluble NSF attachment proteins. J. Biol. Chem. 269, 29347-29350.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29347-29350
    • Morgan, A.1    Dimaline, R.2    Burgoyne, R.D.3
  • 40
    • 0028973450 scopus 로고
    • Microtubule nucleation by gamma-tubulin-containing rings in the centrosome
    • Moritz, M., Braunfeld, M.B., Sedat, J.W., Alberts, B., and Agard, D.A. (1995). Microtubule nucleation by gamma-tubulin-containing rings in the centrosome. Nature 378, 638-640.
    • (1995) Nature , vol.378 , pp. 638-640
    • Moritz, M.1    Braunfeld, M.B.2    Sedat, J.W.3    Alberts, B.4    Agard, D.A.5
  • 41
    • 0024801639 scopus 로고
    • The microtubule binding domain of microtubule-associated protein MAP1B contains a repeated sequence motif unrelated to that of MAP2 and tau
    • Noble, M., Lewis, S., and Cowan, N. (1989). The microtubule binding domain of microtubule-associated protein MAP1B contains a repeated sequence motif unrelated to that of MAP2 and tau. J. Cell Biol. 109, 3367-3376.
    • (1989) J. Cell Biol. , vol.109 , pp. 3367-3376
    • Noble, M.1    Lewis, S.2    Cowan, N.3
  • 42
    • 0028800962 scopus 로고
    • The cell cycle-dependent localization of the CP190 centrosomal protein is determined by the coordinate action of two separable domains
    • Oegema, K., Whitfield, W.G.F., and Alberts, B. (1995). The cell cycle-dependent localization of the CP190 centrosomal protein is determined by the coordinate action of two separable domains. J. Cell Biol. 131, 1261-1273.
    • (1995) J. Cell Biol. , vol.131 , pp. 1261-1273
    • Oegema, K.1    Whitfield, W.G.F.2    Alberts, B.3
  • 44
    • 0027049935 scopus 로고
    • A novel homo-oligomeric protein responsible for an MPF-dependent microtubule-severing activity
    • Shiina, N., Gotoh, Y., and Nishida, E. (1992). A novel homo-oligomeric protein responsible for an MPF-dependent microtubule-severing activity. EMBO J. 11, 4723-4731.
    • (1992) EMBO J. , vol.11 , pp. 4723-4731
    • Shiina, N.1    Gotoh, Y.2    Nishida, E.3
  • 47
    • 0028036711 scopus 로고
    • Activation of dynamin GTPase is a result of positive cooperativity
    • Tuma, P.L., and Collins, C.A. (1994). Activation of dynamin GTPase is a result of positive cooperativity. J. Biol. Chem. 269, 30842-30847.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30842-30847
    • Tuma, P.L.1    Collins, C.A.2
  • 48
    • 0026016405 scopus 로고
    • Severing of stable microtubules by a mitotically activated protein in Xenopus egg extracts
    • Vale, R.D. (1991). Severing of stable microtubules by a mitotically activated protein in Xenopus egg extracts. Cell 64, 827-839.
    • (1991) Cell , vol.64 , pp. 827-839
    • Vale, R.D.1
  • 49
    • 0030031999 scopus 로고    scopus 로고
    • XKCM1 : A Xenopus kinesin-related protein that regulates microtubule dynamics during mitotic spindle assembly
    • Walczak, C.E., Mitchison, T.J., and Desai, A. (1996). XKCM1 : a Xenopus kinesin-related protein that regulates microtubule dynamics during mitotic spindle assembly. Cell 84, 37-47.
    • (1996) Cell , vol.84 , pp. 37-47
    • Walczak, C.E.1    Mitchison, T.J.2    Desai, A.3
  • 50
    • 0001607723 scopus 로고
    • Distantly related sequences in the α and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide fold
    • Walker, J.E., Saraste, M., Runswick, M.J., and Gay, N.J. (1982). Distantly related sequences in the α and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide fold. EMBO J. 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 52
    • 0029787352 scopus 로고    scopus 로고
    • Dynamin self-assembly stimulates its GTPase activity
    • Warnock, D.E., Hinshaw, J.E., and Schmid, S.L. (1996). Dynamin self-assembly stimulates its GTPase activity. J. Biol. Chem. 271, 22310-22314.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22310-22314
    • Warnock, D.E.1    Hinshaw, J.E.2    Schmid, S.L.3
  • 53
    • 0029836707 scopus 로고    scopus 로고
    • The kinetochore microtubule minus-end disassembly associated with flux produces a force that can do work
    • Waters, J.C., Mitchison, T.J., Rieder, C.L., and Salmon, E.D. (1996). The kinetochore microtubule minus-end disassembly associated with flux produces a force that can do work. Mol. Biol. Cell 7, 1547-1558.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1547-1558
    • Waters, J.C.1    Mitchison, T.J.2    Rieder, C.L.3    Salmon, E.D.4
  • 54
    • 0029188122 scopus 로고
    • Insect cell culture in serum-free media
    • C.D. Richardson, ed. (Totowa, NJ: Humana Press Inc.)
    • Weiss, S.A., Godwin, G.P., Gorfien, S.F., and Whitford, W.G. (1995). Insect cell culture in serum-free media. In Baculovirus Expression Protocols, C.D. Richardson, ed. (Totowa, NJ: Humana Press Inc.), pp. 79-95.
    • (1995) Baculovirus Expression Protocols , pp. 79-95
    • Weiss, S.A.1    Godwin, G.P.2    Gorfien, S.F.3    Whitford, W.G.4
  • 55
    • 0020009818 scopus 로고
    • Preparation of tubulin from brain
    • Williams, R.C.J., and Lee, J.C. (1982). Preparation of tubulin from brain. Meth. Enzymol. 85B, 376-385.
    • (1982) Meth. Enzymol. , vol.85 B , pp. 376-385
    • Williams, R.C.J.1    Lee, J.C.2
  • 56
    • 0025770088 scopus 로고
    • Subcellular localization and sequence of sea urchin kinesin heavy chain: Evidence for its association with membranes in mitotic apparatus and interphase cytoplasm
    • Wright, B.D., Henson, J.H.,Wedaman, K.P., Willy, P.J., Morand, J.N., and Scholey, J.M. (1991). Subcellular localization and sequence of sea urchin kinesin heavy chain: evidence for its association with membranes in mitotic apparatus and interphase cytoplasm. J. Cell Biol. 113, 817-833.
    • (1991) J. Cell Biol. , vol.113 , pp. 817-833
    • Wright, B.D.1    Henson, J.H.2    Wedaman, K.P.3    Willy, P.J.4    Morand, J.N.5    Scholey, J.M.6
  • 57
    • 0029662197 scopus 로고    scopus 로고
    • Microtubule dynamics at the G-2-M transition: Abrupt breakdown of cytoplasmic microtubules at nuclear envelope breakdown and implications for spindle morphogenesis
    • Zhai, Y., Kronebusch, P.J., Simon, P.M., and Borisy, G.G. (1996). Microtubule dynamics at the G-2-M transition: abrupt breakdown of cytoplasmic microtubules at nuclear envelope breakdown and implications for spindle morphogenesis. J. Cell Biol. 135, 201-214.
    • (1996) J. Cell Biol. , vol.135 , pp. 201-214
    • Zhai, Y.1    Kronebusch, P.J.2    Simon, P.M.3    Borisy, G.G.4
  • 58
    • 0028879986 scopus 로고
    • Nucleation of microtubule assembly by a gamma-tubulin-containing ring complex
    • Zheng, Y., Wong, M.L., Alberts, B., and Mitchison, T. (1995). Nucleation of microtubule assembly by a gamma-tubulin-containing ring complex. Nature 378, 578-583.
    • (1995) Nature , vol.378 , pp. 578-583
    • Zheng, Y.1    Wong, M.L.2    Alberts, B.3    Mitchison, T.4


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