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Volumn 31, Issue 1, 1996, Pages 87-100

A novel kinesin-like protein with a calmodulin-binding domain

Author keywords

calcium; calmodulin; calmodulin binding protein; kinesin; microtubule; motor protein

Indexed keywords

ANIMALIA; ESCHERICHIA COLI; NICOTIANA TABACUM; TABACUM;

EID: 0030127222     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00020609     Document Type: Article
Times cited : (53)

References (63)
  • 1
    • 0027203970 scopus 로고
    • A plant glutamate decarboxylase containing a calmodulin binding domain, cloning, sequence and functional analysis
    • Baum G, Chen Y, Arazi T, Takatsuji H, Fromm H: A plant glutamate decarboxylase containing a calmodulin binding domain, cloning, sequence and functional analysis. J Biol Chem 268: 19610-19617 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 19610-19617
    • Baum, G.1    Chen, Y.2    Arazi, T.3    Takatsuji, H.4    Fromm, H.5
  • 2
    • 0023021577 scopus 로고
    • Identification of a 52-kD calmodulin-binding protein associated with the mitotic spindle apparatus in mammalian cells
    • Brady RC, Cabrai F, Dedman JR: Identification of a 52-kD calmodulin-binding protein associated with the mitotic spindle apparatus in mammalian cells. J Cell Biol 103: 1855-1861 (1986).
    • (1986) J Cell Biol , vol.103 , pp. 1855-1861
    • Brady, R.C.1    Cabrai, F.2    Dedman, J.R.3
  • 3
    • 0027712714 scopus 로고
    • Expression of microtubule proteins in bacteria for characterization in in vitro motility assays
    • Wilson L, Matsudaira P (eds) Academic Press, New York
    • Chandra R, Endow SA: Expression of microtubule proteins in bacteria for characterization in in vitro motility assays. In: Wilson L, Matsudaira P (eds) Methods in Cell Biology, pp. 115-128. Academic Press, New York (1993).
    • (1993) Methods in Cell Biology , pp. 115-128
    • Chandra, R.1    Endow, S.A.2
  • 4
    • 0025992588 scopus 로고
    • 2+/calmodulin affects microtubule stability in lysed protoplasts
    • 2+/calmodulin affects microtubule stability in lysed protoplasts. J Cell Sci 100: 311-317 (1991).
    • (1991) J Cell Sci , vol.100 , pp. 311-317
    • Cyr, R.J.1
  • 5
    • 0024276852 scopus 로고
    • Calcium and calmodulin-dependent phosphorylation of a 62 kD protein induces microtubule depolymerization in sea urchin mitotic apparatuses
    • Dinsmore JH, Sloboda RD: Calcium and calmodulin-dependent phosphorylation of a 62 kD protein induces microtubule depolymerization in sea urchin mitotic apparatuses. Cell 53: 769-780 (1988).
    • (1988) Cell , vol.53 , pp. 769-780
    • Dinsmore, J.H.1    Sloboda, R.D.2
  • 6
    • 0028445306 scopus 로고
    • A calmodulin-sensitive interaction between microtubules and a higher plant homolog of elongation factor-1α
    • Durso NA, Cyr RJ: A calmodulin-sensitive interaction between microtubules and a higher plant homolog of elongation factor-1α. Plant Cell 6: 893-905 (1994).
    • (1994) Plant Cell , vol.6 , pp. 893-905
    • Durso, N.A.1    Cyr, R.J.2
  • 7
    • 51249167396 scopus 로고
    • 35S-labeled recombinant as a probe
    • 35S-labeled recombinant as a probe. Plant Mol Biol Rep 10: 199-206 (1992).
    • (1992) Plant Mol Biol Rep , vol.10 , pp. 199-206
    • Fromm, H.1    Chua, N.H.2
  • 9
    • 0026577748 scopus 로고
    • Kinesin-like cut 7 protein associates with mitotic and meiotic spindles in fission yeast
    • Hagan Z, Yanagida M: Kinesin-like cut 7 protein associates with mitotic and meiotic spindles in fission yeast. Nature 356: 74-76 (1992).
    • (1992) Nature , vol.356 , pp. 74-76
    • Hagan, Z.1    Yanagida, M.2
  • 10
    • 23444436196 scopus 로고
    • Cellular roles of kinesin and related proteins
    • Hoyt MA: Cellular roles of kinesin and related proteins. Curr Opin Cell Biol 6: 63-68 (1994).
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 63-68
    • Hoyt, M.A.1
  • 11
    • 0028921581 scopus 로고
    • Calmodulin-binding domains: Just two-faced or multifaceted?
    • James P, Vorherr T, Carafoli E: Calmodulin-binding domains: just two-faced or multifaceted? Trends Biochem Sci 20: 38-42 (1995).
    • (1995) Trends Biochem Sci , vol.20 , pp. 38-42
    • James, P.1    Vorherr, T.2    Carafoli, E.3
  • 12
    • 0020473203 scopus 로고
    • Recycling of cold-stable microtubules: Evidence that cold-stability is due to substoichiometric polymer blocks
    • Job D, Rausch CT, Fisher EH, Margolis RL: Recycling of cold-stable microtubules: Evidence that cold-stability is due to substoichiometric polymer blocks. Biochemistry 21: 509-515 (1982).
    • (1982) Biochemistry , vol.21 , pp. 509-515
    • Job, D.1    Rausch, C.T.2    Fisher, E.H.3    Margolis, R.L.4
  • 13
    • 0001820378 scopus 로고
    • Control of the cytoskeleton by calmodulin and calmodulin-binding proteins
    • Kakiuchi S, Sobue K: Control of the cytoskeleton by calmodulin and calmodulin-binding proteins. Trends Biochem Sci 8: 59-62 (1983).
    • (1983) Trends Biochem Sci , vol.8 , pp. 59-62
    • Kakiuchi, S.1    Sobue, K.2
  • 14
    • 0028343414 scopus 로고
    • A myosin for a higher plant has structural similarities to class V myosins
    • Kinkema M, Schiefelbein J: A myosin for a higher plant has structural similarities to class V myosins. J Mol Biol 239: 591-597 (1994).
    • (1994) J Mol Biol , vol.239 , pp. 591-597
    • Kinkema, M.1    Schiefelbein, J.2
  • 15
    • 0027278759 scopus 로고
    • A myosin-like protein from a higher plant
    • Knight AE, Kendrick-Jones J: A myosin-like protein from a higher plant. J Mol Biol 231: 148-154 (1993).
    • (1993) J Mol Biol , vol.231 , pp. 148-154
    • Knight, A.E.1    Kendrick-Jones, J.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0344327388 scopus 로고
    • Calcium and calmodulin as regulators of chromosome movement during mitosis in higher plants
    • Trewavas AJ (ed) Plenum, New York
    • Lambert AM, Vantard M: Calcium and calmodulin as regulators of chromosome movement during mitosis in higher plants. In: Trewavas AJ (ed) Molecular and Cellular Aspects of Calcium in Plant Development, pp. 175-183. Plenum, New York (1986).
    • (1986) Molecular and Cellular Aspects of Calcium in Plant Development , pp. 175-183
    • Lambert, A.M.1    Vantard, M.2
  • 18
    • 0021357249 scopus 로고
    • Calmodulin binds to both microtubule-associated protein 2 and tau proteins
    • Lee YC, Wo1ff J: Calmodulin binds to both microtubule-associated protein 2 and tau proteins. J Biol Chem 259: 1226-1230 (1984).
    • (1984) J Biol Chem , vol.259 , pp. 1226-1230
    • Lee, Y.C.1    Woff, J.2
  • 19
    • 0027106458 scopus 로고
    • Cellular distribution of calmodulin and calmodulin-binding proteins in Vicia faba L
    • Ling V, Assman SM: Cellular distribution of calmodulin and calmodulin-binding proteins in Vicia faba L. Plant Physiol 100: 970-978 (1992).
    • (1992) Plant Physiol , vol.100 , pp. 970-978
    • Ling, V.1    Assman, S.M.2
  • 20
    • 0028486212 scopus 로고
    • Analysis of a soluble calmodulin binding protein from fava bean roots: Identification of glutamate decarboxylase as a calmodulin-activated enzyme
    • Ling V, Snedden WA, Shelp BJ, Assman SM: Analysis of a soluble calmodulin binding protein from fava bean roots: identification of glutamate decarboxylase as a calmodulin-activated enzyme. Plant Cell 6: 1135-1142 (1994).
    • (1994) Plant Cell , vol.6 , pp. 1135-1142
    • Ling, V.1    Snedden, W.A.2    Shelp, B.J.3    Assman, S.M.4
  • 21
    • 0028007935 scopus 로고
    • Isolation of tobacco cDNA clones encoding calmodulin-binding proteins and characterization of a known calmodulin-binding domain
    • Lu Y, Harrington HM: Isolation of tobacco cDNA clones encoding calmodulin-binding proteins and characterization of a known calmodulin-binding domain. Plant Physiol Biochem 32: 413-422 (1994).
    • (1994) Plant Physiol Biochem , vol.32 , pp. 413-422
    • Lu, Y.1    Harrington, H.M.2
  • 22
    • 0026356891 scopus 로고
    • Predicting coiled from protein sequences
    • Lupas A, Dyke MV, Stock J: Predicting coiled from protein sequences. Science 252: 1162-1164 (1991).
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Dyke, M.V.2    Stock, J.3
  • 23
    • 0027164170 scopus 로고
    • Calmodulin binding to and cAMP-dependent phosphorylation of kinesin light chains modulate kinesin ATPase activity
    • Matthies HJG, Miller RJ, Palfrey HC: Calmodulin binding to and cAMP-dependent phosphorylation of kinesin light chains modulate kinesin ATPase activity. J Biol Chem 268: 11176-11187 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 11176-11187
    • Matthies, H.J.G.1    Miller, R.J.2    Palfrey, H.C.3
  • 24
    • 0025364774 scopus 로고
    • Identification and characterization of a gene encoding a kinesin-like protein in Drosophila
    • McDonald HB, Goldstein LSB: Identification and characterization of a gene encoding a kinesin-like protein in Drosophila. Cell 61: 991-1000 (1990).
    • (1990) Cell , vol.61 , pp. 991-1000
    • McDonald, H.B.1    Goldstein, L.S.B.2
  • 25
    • 0027273614 scopus 로고
    • Identification of a gene family (kat) encoding kinesin-like proteins in Arabidopsis thaliana and the characterization of secondary structure of KatA
    • Mitsui H, Yamaguchi-Shinozaki K, Shinozaki K, Takahashi H: Identification of a gene family (kat) encoding kinesin-like proteins in Arabidopsis thaliana and the characterization of secondary structure of KatA. Mol Gen Genet 238: 326-368 (1993).
    • (1993) Mol Gen Genet , vol.238 , pp. 326-368
    • Mitsui, H.1    Yamaguchi-Shinozaki, K.2    Shinozaki, K.3    Takahashi, H.4
  • 26
    • 0028484520 scopus 로고
    • Sequencing and characterization of the kinesin-like gene KatB and KatC of Arabidopsis thaliana
    • Mitsui H, Nakatani K, Yamaguchi-Shinozaki K, Nishikawa K, Takahashi H; Sequencing and characterization of the kinesin-like gene KatB and KatC of Arabidopsis thaliana. Plant Mol Biol 25: 865-876 (1994).
    • (1994) Plant Mol Biol , vol.25 , pp. 865-876
    • Mitsui, H.1    Nakatani, K.2    Yamaguchi-Shinozaki, K.3    Nishikawa, K.4    Takahashi, H.5
  • 27
    • 0028493116 scopus 로고
    • Calcium/calmodulin-dependent protein kinases
    • Nairn AC, Picciotto MR: Calcium/calmodulin-dependent protein kinases. Sem Cancer Biol 5: 295-303 (1994).
    • (1994) Sem Cancer Biol , vol.5 , pp. 295-303
    • Nairn, A.C.1    Picciotto, M.R.2
  • 28
    • 0028363485 scopus 로고
    • Cloning and localization of a conventional kinesin motor expressed exclusively in neurons
    • Niclas J, Navone F, Hom-Booher N, Vale RD: Cloning and localization of a conventional kinesin motor expressed exclusively in neurons. Neuron 12: 1059-1072 (1994).
    • (1994) Neuron , vol.12 , pp. 1059-1072
    • Niclas, J.1    Navone, F.2    Hom-Booher, N.3    Vale, R.D.4
  • 29
    • 0028948491 scopus 로고
    • KIF2 is a new microtubule-based anterograde motor that transports membranous organelles distinct from those carried by kinesin heavy chain or KIF 3A/B
    • Noda Y, Sato-Yoshitake R, Kondo S, Nangaku M, Hirokawa N: KIF2 is a new microtubule-based anterograde motor that transports membranous organelles distinct from those carried by kinesin heavy chain or KIF 3A/B. J Cell Biol 129: 157-167 (1995).
    • (1995) J Cell Biol , vol.129 , pp. 157-167
    • Noda, Y.1    Sato-Yoshitake, R.2    Kondo, S.3    Nangaku, M.4    Hirokawa, N.5
  • 30
    • 0026657618 scopus 로고
    • Modulation of calmodulin levels, calmodulin methylation, and calmodulin binding proteins during carrot cell growth and embryogenesis
    • Oh SH, Steiner HY, Dougall DK, Roberts DM: Modulation of calmodulin levels, calmodulin methylation, and calmodulin binding proteins during carrot cell growth and embryogenesis. Arch Biochem Biophys 297: 28-34 (1992).
    • (1992) Arch Biochem Biophys , vol.297 , pp. 28-34
    • Oh, S.H.1    Steiner, H.Y.2    Dougall, D.K.3    Roberts, D.M.4
  • 31
    • 0029051298 scopus 로고
    • The neuron-specific kinesin superfamily protein KIF1A is a unique monomeric motor for anterograde axonal transport of synaptic vesicle percursors
    • Okada Y, Yamazaki H, Sekine-Aizawa Y, Hirokawa N: The neuron-specific kinesin superfamily protein KIF1A is a unique monomeric motor for anterograde axonal transport of synaptic vesicle percursors. Cell 81: 769-780 (1995).
    • (1995) Cell , vol.81 , pp. 769-780
    • Okada, Y.1    Yamazaki, H.2    Sekine-Aizawa, Y.3    Hirokawa, N.4
  • 32
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphiphilic α-helicals
    • O'Neil KT, DeGrado WF: How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helicals. Trends Biochem Sci 15: 59-64 (1990).
    • (1990) Trends Biochem Sci , vol.15 , pp. 59-64
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 33
    • 0029065702 scopus 로고
    • Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like clacium-binding domain
    • Patil S, Takezawa D, Poovaiah BW: Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like clacium-binding domain. Proc Natl Acad Sci USA 92: 4897-4901 (1995).
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4897-4901
    • Patil, S.1    Takezawa, D.2    Poovaiah, B.W.3
  • 34
    • 0001900087 scopus 로고
    • The kinesin superfamily in microtubules
    • Hyams JS, Lloyd CW (eds) Wiley-Liss, New York
    • Pereira A, Goldstein LSB: The kinesin superfamily in microtubules. In: Hyams JS, Lloyd CW (eds) Microtubules, pp. 269-284. Wiley-Liss, New York (1994).
    • (1994) Microtubules , pp. 269-284
    • Pereira, A.1    Goldstein, L.S.B.2
  • 36
    • 27044439436 scopus 로고
    • Isolation of a novel calmodulin-binding protein from Arabidopsis thaliana
    • Reddy ASN, Safadi F, Narasimhulu SB, Golovkin M, Hu X: Isolation of a novel calmodulin-binding protein from Arabidopsis thaliana. Plant Physiol 108 (Suppl): 41 (1995).
    • (1995) Plant Physiol , vol.108 , Issue.SUPPL. , pp. 41
    • Reddy, A.S.N.1    Safadi, F.2    Narasimhulu, S.B.3    Golovkin, M.4    Hu, X.5
  • 37
    • 0029966327 scopus 로고    scopus 로고
    • A novel calmodulin-binding protein with kinesin heavy-chain motor domain
    • Reddy ASN, Safadi F, Narasimhulu SB, Golovkin M, Hu X: A novel calmodulin-binding protein with kinesin heavy-chain motor domain. J Biol Chem 271: 7052-7060 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 7052-7060
    • Reddy, A.S.N.1    Safadi, F.2    Narasimhulu, S.B.3    Golovkin, M.4    Hu, X.5
  • 38
    • 0027145921 scopus 로고
    • Isolation and characterization of two cDNAs that encode for calmodulin-binding proteins from corn root tips
    • Reddy ASN, Takezawa D, Fromm H, Poovaiah BW: Isolation and characterization of two cDNAs that encode for calmodulin-binding proteins from corn root tips. Plant Sci 94: 107-117 (1993).
    • (1993) Plant Sci , vol.94 , pp. 107-117
    • Reddy, A.S.N.1    Takezawa, D.2    Fromm, H.3    Poovaiah, B.W.4
  • 39
    • 11944252555 scopus 로고
    • Calcium-modulated proteins: Targets of intracellular calcium signals in higher plants
    • Roberts DM, Harmon AC: Calcium-modulated proteins: targets of intracellular calcium signals in higher plants. Annu Rev Plant Mol Biol 43: 375-414 (1992).
    • (1992) Annu Rev Plant Mol Biol , vol.43 , pp. 375-414
    • Roberts, D.M.1    Harmon, A.C.2
  • 42
    • 0028101057 scopus 로고
    • Interaction with calmodulin is required for the function of spc 110p, an essential component of the yeast spindle pole body
    • Stirling DA, Welsh KA, Stark MJR: Interaction with calmodulin is required for the function of spc 110p, an essential component of the yeast spindle pole body. EMBO J 13: 4329-4342 (1994).
    • (1994) EMBO J , vol.13 , pp. 4329-4342
    • Stirling, D.A.1    Welsh, K.A.2    Stark, M.J.R.3
  • 43
    • 0029240357 scopus 로고
    • Calmodulin gene family in potato: Developmental and touch-induced expression of the mRNA encoding a novel isoform
    • Takezawa D, Liu ZH, An G, Poovaiah BW: Calmodulin gene family in potato: developmental and touch-induced expression of the mRNA encoding a novel isoform. Plant Mol Biol 27: 693-703 (1995).
    • (1995) Plant Mol Biol , vol.27 , pp. 693-703
    • Takezawa, D.1    Liu, Z.H.2    An, G.3    Poovaiah, B.W.4
  • 44
    • 0026665567 scopus 로고
    • An immunoreactive homolog of mammalian kinesin in Nicotiana tabacum pollen tubes
    • Tiezzi A, Moscatelli A, Cai G, Bartalesi A, Cresti M: An immunoreactive homolog of mammalian kinesin in Nicotiana tabacum pollen tubes. Cell Motil Cytoskel 21: 132-137 (1992).
    • (1992) Cell Motil Cytoskel , vol.21 , pp. 132-137
    • Tiezzi, A.1    Moscatelli, A.2    Cai, G.3    Bartalesi, A.4    Cresti, M.5
  • 46
    • 0009482260 scopus 로고
    • Electrophoritic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon T: Electrophoritic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 79: 4350-4354 (1979).
    • (1979) Proc Natl Acad Sci USA , vol.79 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, T.3
  • 47
    • 0025946856 scopus 로고
    • Signal transduction in plant cells
    • Trewavas AJ, Gilroy S: Signal transduction in plant cells. Trends Genet 7: 356-361 (1991).
    • (1991) Trends Genet , vol.7 , pp. 356-361
    • Trewavas, A.J.1    Gilroy, S.2
  • 48
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
    • Vale RD, Reese TS, Sheetz MP: Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell 42: 39-50 (1985).
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 49
    • 0027285087 scopus 로고
    • Multiple kinesin-like transcripts in Xenopus oocytes
    • Vernos I, Heasman J, Wylie C: Multiple kinesin-like transcripts in Xenopus oocytes. Devel Biol 157: 232-239 (1993).
    • (1993) Devel Biol , vol.157 , pp. 232-239
    • Vernos, I.1    Heasman, J.2    Wylie, C.3
  • 50
    • 0028988361 scopus 로고
    • Xklpl, a chromosomal xenopus kinesin-like protein essential for spindle organization and chromosome positioning
    • Vernos I, Raats J, Hirano T, Heasman J, Karsenti E, Wylie C: Xklpl, a chromosomal xenopus kinesin-like protein essential for spindle organization and chromosome positioning. Cell 81: 117-127 (1995).
    • (1995) Cell , vol.81 , pp. 117-127
    • Vernos, I.1    Raats, J.2    Hirano, T.3    Heasman, J.4    Karsenti, E.5    Wylie, C.6
  • 51
    • 0024978113 scopus 로고
    • A small-scale procedure for the rapid isolation of plant RNAs
    • Verwoerd TC, Dekker BMM, Hoekema A: A small-scale procedure for the rapid isolation of plant RNAs. Nucl Acids Res 17: 2362 (1989).
    • (1989) Nucl Acids Res , vol.17 , pp. 2362
    • Verwoerd, T.C.1    Dekker, B.M.M.2    Hoekema, A.3
  • 52
    • 0027176792 scopus 로고
    • Dimerization specificity of the leucine zipper containing bZIP motif on DNA binding: Prediction and rational design
    • Vinson CR, Hai TW, Boyd S: Dimerization specificity of the leucine zipper containing bZIP motif on DNA binding: prediction and rational design. Genes Devel 7: 1047-1058 (1993).
    • (1993) Genes Devel , vol.7 , pp. 1047-1058
    • Vinson, C.R.1    Hai, T.W.2    Boyd, S.3
  • 53
    • 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 binding fold
    • Walker JE, Saraste M, Runswick MJ, Gay NJ: Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1: 945-951 (1982).
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 54
    • 27044432569 scopus 로고
    • Isolation and characterization of cDNAs that encode calmodulin-binding proteins
    • Wang W, Takezawa D, Poovaiah BW: Isolation and characterization of cDNAs that encode calmodulin-binding proteins. Plant Physiol 108 (Suppl): 103 (1995).
    • (1995) Plant Physiol , vol.108 , Issue.SUPPL. , pp. 103
    • Wang, W.1    Takezawa, D.2    Poovaiah, B.W.3
  • 55
    • 27044433618 scopus 로고
    • Immunolocalization of tubulin and calmodulin in meristematic plant cells
    • Thompson MP (ed) CRC Press, Boca Raton
    • Wick SM: Immunolocalization of tubulin and calmodulin in meristematic plant cells. In: Thompson MP (ed) Calcium Binding Proteins, Biological Functions, vol 2, pp. 21-45. CRC Press, Boca Raton (1988).
    • (1988) Calcium Binding Proteins, Biological Functions , vol.2 , pp. 21-45
    • Wick, S.M.1
  • 56
    • 0024573497 scopus 로고
    • Cloning and deletion mutegenesis using direct protein-protein interaction on an expression vector, identification of the calmodulin binding domain of α-fodrin
    • Widada JS, Asselin J, Colote S, Marti J, Ferraz C, Trave G, Haiech J, Liautard JP: Cloning and deletion mutegenesis using direct protein-protein interaction on an expression vector, identification of the calmodulin binding domain of α-fodrin. J Mol Biol 205: 455-458 (1989).
    • (1989) J Mol Biol , vol.205 , pp. 455-458
    • Widada, J.S.1    Asselin, J.2    Colote, S.3    Marti, J.4    Ferraz, C.5    Trave, G.6    Haiech, J.7    Liautard, J.P.8
  • 57
    • 0020009818 scopus 로고
    • Preparation of tubulin from brain
    • Williams R, Lee JC: Preparation of tubulin from brain. Meth Enzymol 85: 376-385 (1982).
    • (1982) Meth Enzymol , vol.85 , pp. 376-385
    • Williams, R.1    Lee, J.C.2
  • 58
    • 84982757558 scopus 로고
    • Calcium and the plant cytoskeleton
    • Williamson RE: Calcium and the plant cytoskeleton. Plant Cell Environ 7: 431-440 (1984).
    • (1984) Plant Cell Environ , vol.7 , pp. 431-440
    • Williamson, R.E.1
  • 59
    • 0020642587 scopus 로고
    • 2+- and calmodulin-dependent phosphorylation of microtubule-associated protein 2 and tau factor, and inhibition of microtubule assembly
    • 2+- and calmodulin-dependent phosphorylation of microtubule-associated protein 2 and tau factor, and inhibition of microtubule assembly. J Neurochem 41: 1119-1125 (1983).
    • (1983) J Neurochem , vol.41 , pp. 1119-1125
    • Yamamoto, H.1    Fukunaga, K.2    Tanaka, E.3    Miyamoto, E.4
  • 61
    • 0024550571 scopus 로고
    • A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analysis
    • Yang JT, Laymon RA, Goldstein LSB: A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analysis. Cell 56: 879-889 (1989).
    • (1989) Cell , vol.56 , pp. 879-889
    • Yang, J.T.1    Laymon, R.A.2    Goldstein, L.S.B.3
  • 62
    • 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 EC, Goldstein LSB: Evidence that the head of kinesin is sufficient for force generation and motility in vitro. Science 249: 42-47 (1990).
    • (1990) Science , vol.249 , pp. 42-47
    • Yang, J.T.1    Saxton, W.M.2    Stewart, R.J.3    Raff, E.C.4    Goldstein, L.S.B.5
  • 63
    • 0025299114 scopus 로고
    • Regulation of anaphase chromosome motion in Tradescantia stamen hair cells by calcium and related signaling agents
    • Zhang DH, Callaham DA, Hepler PK: Regulation of anaphase chromosome motion in Tradescantia stamen hair cells by calcium and related signaling agents. J Cell Biol 111: 171-182 (1990).
    • (1990) J Cell Biol , vol.111 , pp. 171-182
    • Zhang, D.H.1    Callaham, D.A.2    Hepler, P.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.