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Volumn 57, Issue 4, 2004, Pages 218-232

A Subclass of Myosin XI Is Associated with Mitochondria, Plastids, and the Molecular Chaperone Subunit TCP-1α in Maize

Author keywords

Cytoskeleton; Molecular chaperone; Myosin; Plant; Zea mays

Indexed keywords

CHAPERONE; CYTOSKELETON PROTEIN; ISOPROTEIN; MYOSIN; MYOSIN XI; POLYPEPTIDE; SERINE PROTEINASE; TAILESS COMPLEX POLYPEPTIDE 1ALPHA; UNCLASSIFIED DRUG;

EID: 1842531907     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/cm.10168     Document Type: Article
Times cited : (68)

References (73)
  • 1
    • 8944236176 scopus 로고    scopus 로고
    • Myosins on the move to signal transduction
    • Bähler M. 1996. Myosins on the move to signal transduction. Curr Opin Cell Biol 8:18-22.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 18-22
    • Bähler, M.1
  • 2
    • 0033928321 scopus 로고    scopus 로고
    • Tissue-specific subcellular immunolocalization of a myosin-like protein in maize root apices
    • Baluska F, Polsakiewicz M, Peters M, Volkmann D. 2000. Tissue-specific subcellular immunolocalization of a myosin-like protein in maize root apices. Protoplasma 212:137-145.
    • (2000) Protoplasma , vol.212 , pp. 137-145
    • Baluska, F.1    Polsakiewicz, M.2    Peters, M.3    Volkmann, D.4
  • 4
    • 0034193779 scopus 로고    scopus 로고
    • A subtilisin-like serine protease involved in the regulation of stomatal density and distribution in Arabidopsis thaliana
    • Berger D, Altmann T. 2000. A subtilisin-like serine protease involved in the regulation of stomatal density and distribution in Arabidopsis thaliana. Genes Dev 14:1119-1131.
    • (2000) Genes Dev , vol.14 , pp. 1119-1131
    • Berger, D.1    Altmann, T.2
  • 6
    • 0030025137 scopus 로고    scopus 로고
    • Molecular chaperones and the centrosome: A role for TCP-1 in microtubule nucleation
    • Brown CR, Doxsey SJ, Hongbrown LQ, Martin RL, Welch WJ. 1996. Molecular chaperones and the centrosome: a role for TCP-1 in microtubule nucleation. J Biol Chem 271:824-832.
    • (1996) J Biol Chem , vol.271 , pp. 824-832
    • Brown, C.R.1    Doxsey, S.J.2    Hongbrown, L.Q.3    Martin, R.L.4    Welch, W.J.5
  • 7
    • 0029441250 scopus 로고
    • Methods in plant immunolight microscopy
    • Brown RC, Lemmon BE. 1995. Methods in plant immunolight microscopy. Methods Cell Biol 49:85-107.
    • (1995) Methods Cell Biol , vol.49 , pp. 85-107
    • Brown, R.C.1    Lemmon, B.E.2
  • 8
    • 0034193443 scopus 로고    scopus 로고
    • A homologue of the bacterial cell division site-determining factor MinD mediates placement of the chloroplast division apparatus
    • Colletti KS, Tattersall EA, Pyke KA, Froelich JE, Stokes KD, Osteryoung KW. 2000. A homologue of the bacterial cell division site-determining factor MinD mediates placement of the chloroplast division apparatus. Curr Biol 10:507-516.
    • (2000) Curr Biol , vol.10 , pp. 507-516
    • Colletti, K.S.1    Tattersall, E.A.2    Pyke, K.A.3    Froelich, J.E.4    Stokes, K.D.5    Osteryoung, K.W.6
  • 9
    • 15144351296 scopus 로고    scopus 로고
    • Conservation within the myosin motor domain: Implications for structure and function
    • Cope MJTV, Whisstock J, Rayment I, Kendrick-Jones J. 1996. Conservation within the myosin motor domain: implications for structure and function. Structure 4:969-987.
    • (1996) Structure , vol.4 , pp. 969-987
    • Cope, M.J.T.V.1    Whisstock, J.2    Rayment, I.3    Kendrick-Jones, J.4
  • 10
    • 0034953860 scopus 로고    scopus 로고
    • Fatty acid synthesis in pea root plastids is inhibited by the action of long-chain acyl-coenzyme as on metabolite transporters
    • Fox SR, Rawsthorne S, Hills MJ. 2001. Fatty acid synthesis in pea root plastids is inhibited by the action of long-chain acyl-coenzyme as on metabolite transporters. Plant Physiol 126:1259-1265.
    • (2001) Plant Physiol , vol.126 , pp. 1259-1265
    • Fox, S.R.1    Rawsthorne, S.2    Hills, M.J.3
  • 11
    • 0027077442 scopus 로고
    • Function in protein folding of TRIC, a cytosolic ring complex containing TCP-1 and structurally related subunits
    • Frydman J, Nimmesgern E, Erdjument-Bromage H, Wall JS, Tempst P, Hartl FU. 1992. Function in protein folding of TRIC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J 11:4767-4778.
    • (1992) EMBO J , vol.11 , pp. 4767-4778
    • Frydman, J.1    Nimmesgern, E.2    Erdjument-Bromage, H.3    Wall, J.S.4    Tempst, P.5    Hartl, F.U.6
  • 12
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes beta-actin folding
    • Gao Y, Thomas JO, Chow RL, Lee GH, Cowan NJ. 1992. A cytoplasmic chaperonin that catalyzes beta-actin folding. Cell 69:1043-1050.
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 13
    • 0029163054 scopus 로고
    • Molecular motors, membrane movements and physiology: Emerging roles for myosins
    • Hasson T, Mooseker MS. 1995. Molecular motors, membrane movements and physiology: emerging roles for myosins. Curr Opin Cell Biol 7:587-594.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 587-594
    • Hasson, T.1    Mooseker, M.S.2
  • 15
    • 0001013271 scopus 로고
    • Myosin associated with the surfaces of organelles, vegetative nuclei and generative cells in angiosperm pollen grains and tubes
    • Heslop-Harrison J, Heslop-Harrison Y. 1989. Myosin associated with the surfaces of organelles, vegetative nuclei and generative cells in angiosperm pollen grains and tubes. J Cell Sci 94:319-325.
    • (1989) J Cell Sci , vol.94 , pp. 319-325
    • Heslop-Harrison, J.1    Heslop-Harrison, Y.2
  • 16
    • 0031464179 scopus 로고    scopus 로고
    • Developmental and light-dependent changes of the cytosolic chaperonin containing TCP-1 (CCT) subunits in maize seedlings, and the localization in coleoptiles
    • Himmelspach R, Nick P, Shafer E, Ehmann B. 1997. Developmental and light-dependent changes of the cytosolic chaperonin containing TCP-1 (CCT) subunits in maize seedlings, and the localization in coleoptiles. Plant J 12:1299-1310.
    • (1997) Plant J , vol.12 , pp. 1299-1310
    • Himmelspach, R.1    Nick, P.2    Shafer, E.3    Ehmann, B.4
  • 18
    • 0029823194 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a vacuolar serine endopeptidase induced by glucose starvation in maize roots
    • James F, Brouquisse R, Suire C, Pradet A, Raymond P. 1996. Purification and biochemical characterization of a vacuolar serine endopeptidase induced by glucose starvation in maize roots. Biochem J 320:283-292.
    • (1996) Biochem J , vol.320 , pp. 283-292
    • James, F.1    Brouquisse, R.2    Suire, C.3    Pradet, A.4    Raymond, P.5
  • 20
    • 0040557481 scopus 로고    scopus 로고
    • Evidence for the presence of the ascorbate glutathione cycle in mitochondria and peroxisomes of pea leaves
    • Jimenes A, Hernandez JA, del Rio LA, Sevilla F. 1997. Evidence for the presence of the ascorbate glutathione cycle in mitochondria and peroxisomes of pea leaves. Plant Physiol 114:275-284.
    • (1997) Plant Physiol , vol.114 , pp. 275-284
    • Jimenes, A.1    Hernandez, J.A.2    Del Rio, L.A.3    Sevilla, F.4
  • 21
    • 0032885421 scopus 로고    scopus 로고
    • Actin-organelle interaction: Association with chloroplast in Arabidopsis leaf mesophyll cells
    • Kandasamy M, Meagher R. 1999. Actin-organelle interaction: association with chloroplast in Arabidopsis leaf mesophyll cells. Cell Motil Cytoskeleton 44:110-118.
    • (1999) Cell Motil Cytoskeleton , vol.44 , pp. 110-118
    • Kandasamy, M.1    Meagher, R.2
  • 22
    • 0033935268 scopus 로고    scopus 로고
    • Cloning and characterization of a myosin from characean alga, the fastest motor protein in the world
    • Kashiyama T, Kimura N, Mimura T, Yamamoto K. 2000. Cloning and characterization of a myosin from characean alga, the fastest motor protein in the world. J Biochem 127:1065-1070.
    • (2000) J Biochem , vol.127 , pp. 1065-1070
    • Kashiyama, T.1    Kimura, N.2    Mimura, T.3    Yamamoto, K.4
  • 24
    • 0028343414 scopus 로고
    • A myosin from a higher plant has structural similarities to class V myosins
    • Kinkema M, Schiefelbein J. 1994. A myosin from a higher plant has structural similarities to class V myosins. J Mol Biol 239:591-597.
    • (1994) J Mol Biol , vol.239 , pp. 591-597
    • Kinkema, M.1    Schiefelbein, J.2
  • 25
    • 0028535275 scopus 로고
    • Molecular analysis of the myosin gene family in Arabidopsis thaliana
    • Kinkema M, Wang H, Schiefelbein J. 1994. Molecular analysis of the myosin gene family in Arabidopsis thaliana. Plant Mol Biol 26:1139-1153.
    • (1994) Plant Mol Biol , vol.26 , pp. 1139-1153
    • Kinkema, M.1    Wang, H.2    Schiefelbein, J.3
  • 26
    • 0027278759 scopus 로고
    • A myosin-like protein from a higher plant
    • Knight AE, Kendrick-Jones J. 1993. A myosin-like protein from a higher plant. J Mol Biol 231:148-154.
    • (1993) J Mol Biol , vol.231 , pp. 148-154
    • Knight, A.E.1    Kendrick-Jones, J.2
  • 27
    • 0024006146 scopus 로고
    • Accelerated sliding of pollen tube organelles along Characeae actin bundles regulated by Ca++
    • Kohno T, Shimmen T. 1988a. Accelerated sliding of pollen tube organelles along Characeae actin bundles regulated by Ca++. J Cell Biol 106:1539-1543.
    • (1988) J Cell Biol , vol.106 , pp. 1539-1543
    • Kohno, T.1    Shimmen, T.2
  • 28
    • 0001231453 scopus 로고
    • Mechanism of Ca++ inhibition of cytoplasmic streaming in lily pollen tubes
    • Kohno T, Shimmen T. 1988b. Mechanism of Ca++ inhibition of cytoplasmic streaming in lily pollen tubes. J Cell Biol 91:501-509.
    • (1988) J Cell Biol , vol.91 , pp. 501-509
    • Kohno, T.1    Shimmen, T.2
  • 29
    • 0028119106 scopus 로고
    • Myosin in onion (Allium cepa) bulb scale epidermal cells: Involvement in dynamics of organelles and endoplasmic reticulum
    • Liebe S, Quader H. 1994. Myosin in onion (Allium cepa) bulb scale epidermal cells: involvement in dynamics of organelles and endoplasmic reticulum. Physiol Plantarum 90:114-124.
    • (1994) Physiol Plantarum , vol.90 , pp. 114-124
    • Liebe, S.1    Quader, H.2
  • 30
    • 0035042072 scopus 로고    scopus 로고
    • Evidence for non-ciradian light/dark-regulated expression of hsp70s in spinach leaves
    • Li QS, Guy CL. 2001. Evidence for non-ciradian light/dark-regulated expression of hsp70s in spinach leaves. Plant Physiol 125:1633-1642.
    • (2001) Plant Physiol , vol.125 , pp. 1633-1642
    • Li, Q.S.1    Guy, C.L.2
  • 31
    • 38249026313 scopus 로고
    • Myosin heavy chains: Detection by immunoblotting in higher plants and localization by immunofluorescence in alga Chara
    • Lin Q, Grolig F, Jablonsky PP, Williamson RE. 1989 Myosin heavy chains: detection by immunoblotting in higher plants and localization by immunofluorescence in alga Chara. Cell Biol Int Rep 13:107-117.
    • (1989) Cell Biol Int Rep , vol.13 , pp. 107-117
    • Lin, Q.1    Grolig, F.2    Jablonsky, P.P.3    Williamson, R.E.4
  • 36
    • 0026730943 scopus 로고
    • The ins and outs of mitochondrial-membrane channels
    • Mannella CA. 1992. The ins and outs of mitochondrial-membrane channels. Trends Biochem Sci 17:315-320.
    • (1992) Trends Biochem Sci , vol.17 , pp. 315-320
    • Mannella, C.A.1
  • 37
    • 0027293897 scopus 로고
    • Chaperonin-mediated folding of vertebrate actin-related protein and gamma-tubulin
    • Melki R, Vainberg IE, Chow, RL, Cowan NJ. 1993. Chaperonin-mediated folding of vertebrate actin-related protein and gamma-tubulin. J Cell Biol 122:13001-1310.
    • (1993) J Cell Biol , vol.122 , pp. 13001-11310
    • Melki, R.1    Vainberg, I.E.2    Chow, R.L.3    Cowan, N.J.4
  • 38
    • 0029166933 scopus 로고
    • Identification and localization of three classes of myosins in pollen tubes of Lilium longiflorum and Nicotiana alata
    • Miller DD, Scordilis SP, Helper PK. 1995. Identification and localization of three classes of myosins in pollen tubes of Lilium longiflorum and Nicotiana alata. J Cell Sci 108:2549-2653.
    • (1995) J Cell Sci , vol.108 , pp. 2549-2653
    • Miller, D.D.1    Scordilis, S.P.2    Helper, P.K.3
  • 41
    • 0036733734 scopus 로고    scopus 로고
    • Protein phosphorylation regulates actomyosin-driven vesicle movement in cell extracts isolated from the green algae, Chara corallina
    • Morimatsu M, Hasegawa S, Higashi-Fujime S. 2002. Protein phosphorylation regulates actomyosin-driven vesicle movement in cell extracts isolated from the green algae, Chara corallina. Cell Motil Cytoskeleton 53:66-76.
    • (2002) Cell Motil Cytoskeleton , vol.53 , pp. 66-76
    • Morimatsu, M.1    Hasegawa, S.2    Higashi-Fujime, S.3
  • 43
    • 0034099447 scopus 로고    scopus 로고
    • Plant chaperonins: A role in microtubule-dependent wall formation
    • Nick P, Heuing A, Ehmann B. 2000. Plant chaperonins: a role in microtubule-dependent wall formation. Protoplasma 211:234-244.
    • (2000) Protoplasma , vol.211 , pp. 234-244
    • Nick, P.1    Heuing, A.2    Ehmann, B.3
  • 44
    • 0003092302 scopus 로고
    • Higher plant myosin heavy chain identified using a monoclonal antibody
    • Parke J, Miller C. Anderton BH. 1986. Higher plant myosin heavy chain identified using a monoclonal antibody. Eur J Cell Biol 41:9-13.
    • (1986) Eur J Cell Biol , vol.41 , pp. 9-13
    • Parke, J.1    Miller, C.2    Anderton, B.H.3
  • 46
    • 0032102674 scopus 로고    scopus 로고
    • Localization of a myosin-like protein to plasmodesmata
    • Radford JE, White RG. 1998. Localization of a myosin-like protein to plasmodesmata. Plant J 14:743-750.
    • (1998) Plant J , vol.14 , pp. 743-750
    • Radford, J.E.1    White, R.G.2
  • 47
    • 0035947774 scopus 로고    scopus 로고
    • The yeast class V myosins, Myo2p and Myo4p, are nonprocessive actin-based motors
    • Reck-Peterson SL, Tyska MJ, Novick PJ, Mooseker MS. 2001. The yeast class V myosins, Myo2p and Myo4p, are nonprocessive actin-based motors. J Cell Biol 153:1121-1126.
    • (2001) J Cell Biol , vol.153 , pp. 1121-1126
    • Reck-Peterson, S.L.1    Tyska, M.J.2    Novick, P.J.3    Mooseker, M.S.4
  • 48
    • 0035224265 scopus 로고    scopus 로고
    • Analysis of the myosins encoded in the recently completed Arabidopsis thaliana genome sequence
    • Reddy ASN, Day IS. 2001. Analysis of the myosins encoded in the recently completed Arabidopsis thaliana genome sequence. Genome Biol 2:1-17.
    • (2001) Genome Biol , vol.2 , pp. 1-17
    • Reddy, A.S.N.1    Day, I.S.2
  • 49
    • 0033198432 scopus 로고    scopus 로고
    • Characterization of the unconventional myosin VIII in plant cells and its localization at the post-cytokinetic cell wall
    • Reichelt S, Knight AE, Hodge TP, Baluska F, Samaj J, Vokmann D, Kendrick-Jones J. 1999. Characterization of the unconventional myosin VIII in plant cells and its localization at the post-cytokinetic cell wall. Plant J 19:555-567.
    • (1999) Plant J , vol.19 , pp. 555-567
    • Reichelt, S.1    Knight, A.E.2    Hodge, T.P.3    Baluska, F.4    Samaj, J.5    Vokmann, D.6    Kendrick-Jones, J.7
  • 50
    • 0001812897 scopus 로고    scopus 로고
    • Golgi-membrane dynamics are cytoskeleton dependent: A study on Golgi stack movement induced by brefeldin A
    • SatiatJeunemaitre B, Steele C, Hawes C. 1996. Golgi-membrane dynamics are cytoskeleton dependent: A study on Golgi stack movement induced by brefeldin A. Protoplasma 191:21-33.
    • (1996) Protoplasma , vol.191 , pp. 21-33
    • Satiat Jeunemaitre, B.1    Steele, C.2    Hawes, C.3
  • 51
    • 0027987123 scopus 로고
    • Identification of a 50-kDa systemin-binding protein in tomato plasma membranes having Kex2p-like properties
    • Schaller A, Ryan CA. 1994. Identification of a 50-kDa systemin-binding protein in tomato plasma membranes having Kex2p-like properties. Proc Natl Acad Sci USA 91:11802-11806.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11802-11806
    • Schaller, A.1    Ryan, C.A.2
  • 52
    • 0026474824 scopus 로고
    • Identification of 2 general diffusion channels in the outer membrane of pea mitochondria
    • Schmid A, Kromer S, Heldt HW, Benz R. 1992. Identification of 2 general diffusion channels in the outer membrane of pea mitochondria. Biochim Biophys Acta 1112:174-180.
    • (1992) Biochim Biophys Acta , vol.1112 , pp. 174-180
    • Schmid, A.1    Kromer, S.2    Heldt, H.W.3    Benz, R.4
  • 53
    • 0030998145 scopus 로고    scopus 로고
    • Antigen retrieval immunohistochemistry: Past, present, and future
    • Shi SR, Cote RJ, Taylor CR. 1997. Antigen retrieval immunohistochemistry: past, present, and future. J Histochem Cytochem 45:327-343.
    • (1997) J Histochem Cytochem , vol.45 , pp. 327-343
    • Shi, S.R.1    Cote, R.J.2    Taylor, C.R.3
  • 55
    • 0033617146 scopus 로고    scopus 로고
    • A temperature dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess C, Beil A, Ehrmann M. 1999. A temperature dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97:339-347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 56
    • 0033578722 scopus 로고    scopus 로고
    • Myosin II folding is mediated by a molecular chaperonin
    • Srikakulam R, Winkelmann DA. 1999. Myosin II folding is mediated by a molecular chaperonin. J Biol Chem 274:27265-27273.
    • (1999) J Biol Chem , vol.274 , pp. 27265-27273
    • Srikakulam, R.1    Winkelmann, D.A.2
  • 59
    • 0034525998 scopus 로고    scopus 로고
    • Chloroplast division and morphology are differentially affected by over expression of FtsZ1 and FtsZ2 genes in Arabidopsis
    • Stokes KD, McAndrew RS, Figueroa R, Vitha S, Osteryoung KW. 2000. Chloroplast division and morphology are differentially affected by over expression of FtsZ1 and FtsZ2 genes in Arabidopsis. Plant Physiol 124:1668-1677.
    • (2000) Plant Physiol , vol.124 , pp. 1668-1677
    • Stokes, K.D.1    McAndrew, R.S.2    Figueroa, R.3    Vitha, S.4    Osteryoung, K.W.5
  • 60
    • 0032516067 scopus 로고    scopus 로고
    • Plant nuclear gene knockout reveals a role in plastid division for the homolog of the bacterial cell division protein FtsZ, an ancestral tubulin
    • Strepp R, Scholz S, Kruse S, Speth V, Reski R. 1998. Plant nuclear gene knockout reveals a role in plastid division for the homolog of the bacterial cell division protein FtsZ, an ancestral tubulin. Proc Natl Acad Sci USA 95:4368-4373.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4368-4373
    • Strepp, R.1    Scholz, S.2    Kruse, S.3    Speth, V.4    Reski, R.5
  • 61
    • 0033987381 scopus 로고    scopus 로고
    • Mitochondrial movement and morphology depend on an intact actin cytoskeleton in Aspergillus nidulans
    • Suelmann R, Fischer R. 2000. Mitochondrial movement and morphology depend on an intact actin cytoskeleton in Aspergillus nidulans. Cell Motil Cytoskeleton 45:42-50.
    • (2000) Cell Motil Cytoskeleton , vol.45 , pp. 42-50
    • Suelmann, R.1    Fischer, R.2
  • 62
    • 0038037717 scopus 로고    scopus 로고
    • Force-velocity relationships in actin-myosin interactions causing cytoplasmic streaming in algal cells
    • Sugi H, Chaen S. 2003. Force-velocity relationships in actin-myosin interactions causing cytoplasmic streaming in algal cells. J Exp Biol 206:1971-1976.
    • (2003) J Exp Biol , vol.206 , pp. 1971-1976
    • Sugi, H.1    Chaen, S.2
  • 63
    • 0024643957 scopus 로고
    • Immunochemical and immunocytochemical identification of a myosin heavy chain polypeptide in Nicotiana pollen tubes
    • Tang X, Hepler PK, Scordilis SP. 1989. Immunochemical and immunocytochemical identification of a myosin heavy chain polypeptide in Nicotiana pollen tubes. J Cell Sci 92:569-574.
    • (1989) J Cell Sci , vol.92 , pp. 569-574
    • Tang, X.1    Hepler, P.K.2    Scordilis, S.P.3
  • 64
    • 0036830196 scopus 로고    scopus 로고
    • Myosin superfamily evolutionary history
    • Thompson RF, Langford GM. 2002. Myosin superfamily evolutionary history. Anatomical Record 268:276-289.
    • (2002) Anatomical Record , vol.268 , pp. 276-289
    • Thompson, R.F.1    Langford, G.M.2
  • 65
    • 0030210490 scopus 로고    scopus 로고
    • Characterisation of LRP, a leucine-rich repeat (LRR) protein from tomato plants that is processed during pathogenesis
    • Tornero P, Mayda E, Gomez MD, Canas L, Conejero V, Vera P. 1996. Characterisation of LRP, a leucine-rich repeat (LRR) protein from tomato plants that is processed during pathogenesis. Plant J 10:315-330.
    • (1996) Plant J , vol.10 , pp. 315-330
    • Tornero, P.1    Mayda, E.2    Gomez, M.D.3    Canas, L.4    Conejero, V.5    Vera, P.6
  • 66
    • 85005136500 scopus 로고
    • Tomato actin and myosin: Contractile proteins from a higher land plant
    • Vahey M, Titus M, Trautwein R, Scordilis S. 1982. Tomato actin and myosin: contractile proteins from a higher land plant. Cell Motil 2:131-147.
    • (1982) Cell Motil , vol.2 , pp. 131-147
    • Vahey, M.1    Titus, M.2    Trautwein, R.3    Scordilis, S.4
  • 67
    • 0042429100 scopus 로고    scopus 로고
    • Class XIII myosins from the green alga Acetabularia: Driving force in organelle transport and tip growth
    • Vugrek O, Sawitzky H, Menzel D. 2003. Class XIII myosins from the green alga Acetabularia: driving force in organelle transport and tip growth. J Muscle Res Cell Motil 24:87-97.
    • (2003) J Muscle Res Cell Motil , vol.24 , pp. 87-97
    • Vugrek, O.1    Sawitzky, H.2    Menzel, D.3
  • 68
    • 0034278137 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cDNA and a gene for subtilisin-like serine proteases from rice (Oryza sativa L.) and Arobidopsis thaliana
    • Yamagata H, Uesugi M, Saka K, Iwasaki T, Aizono Y. 2000. Molecular cloning and characterization of a cDNA and a gene for subtilisin-like serine proteases from rice (Oryza sativa L.) and Arobidopsis thaliana. Biosci Biotechnol Biochem 64:1947-1957.
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 1947-1957
    • Yamagata, H.1    Uesugi, M.2    Saka, K.3    Iwasaki, T.4    Aizono, Y.5
  • 70
    • 0034349216 scopus 로고    scopus 로고
    • Identification and characterization of higher plant myosins responsible for cytoplasmic streaming
    • Yokota E. 2000. Identification and characterization of higher plant myosins responsible for cytoplasmic streaming. J Plant Res 113:511-519.
    • (2000) J Plant Res , vol.113 , pp. 511-519
    • Yokota, E.1
  • 71
    • 0036090849 scopus 로고    scopus 로고
    • Purification and characterization of myosin from wheat mitochondria
    • Zhao H, Liu A, Liu G, Yen L. 2002. Purification and characterization of myosin from wheat mitochondria. Chinese Science Bulletin 47:315-318.
    • (2002) Chinese Science Bulletin , vol.47 , pp. 315-318
    • Zhao, H.1    Liu, A.2    Liu, G.3    Yen, L.4
  • 72
    • 0036328582 scopus 로고    scopus 로고
    • A higher plant myosin in Luffa cylindrical: Electron microscopic visualization
    • Zhao, FQ, Yan LF. 2002. A higher plant myosin in Luffa cylindrical: electron microscopic visualization. Acta Bot Sin 44:22-28.
    • (2002) Acta Bot Sin , vol.44 , pp. 22-28
    • Zhao, F.Q.1    Yan, L.F.2
  • 73
    • 0031923127 scopus 로고    scopus 로고
    • The role of molecular chaperones in protein transport into the mammalian endoplasmic reticulum
    • Zimmermann R. 1998. The role of molecular chaperones in protein transport into the mammalian endoplasmic reticulum. Biol Chem 379:275-282.
    • (1998) Biol Chem , vol.379 , pp. 275-282
    • Zimmermann, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.