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Volumn 7, Issue 4, 2012, Pages

The intracellular transport and secretion of calumenin-1/2 in living cells

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; CALUMENIN 1; CALUMENIN 2; CHROMOSOME PROTEIN; CYTOPLASMIC DYNEIN; ENHANCED GREEN FLUORESCENT PROTEIN; MOLECULAR MOTOR; PROTEIN KIF5B; UNCLASSIFIED DRUG; CALCIUM BINDING PROTEIN; CALU PROTEIN, HUMAN; DYNEIN ADENOSINE TRIPHOSPHATASE; GREEN FLUORESCENT PROTEIN; ISOPROTEIN; KIF5B PROTEIN, HUMAN; KINESIN;

EID: 84859698675     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0035344     Document Type: Article
Times cited : (16)

References (57)
  • 1
    • 0033978227 scopus 로고    scopus 로고
    • The CREC family, a novel family of multiple EF-hand, low-affinity Ca(2+)-binding proteins localised to the secretory pathway of mammalian cells
    • Honore B, Vorum H, (2000) The CREC family, a novel family of multiple EF-hand, low-affinity Ca(2+)-binding proteins localised to the secretory pathway of mammalian cells. FEBS Lett 466: 11-18.
    • (2000) FEBS Lett , vol.466 , pp. 11-18
    • Honore, B.1    Vorum, H.2
  • 2
    • 58049176372 scopus 로고    scopus 로고
    • Calumenin but not reticulocalbin forms a Ca2+-dependent complex with thrombospondin-1. A potential role in haemostasis and thrombosis
    • Hansen GA, Vorum H, Jacobsen C, Honore B, (2009) Calumenin but not reticulocalbin forms a Ca2+-dependent complex with thrombospondin-1. A potential role in haemostasis and thrombosis. Mol Cell Biochem 320: 25-33.
    • (2009) Mol Cell Biochem , vol.320 , pp. 25-33
    • Hansen, G.A.1    Vorum, H.2    Jacobsen, C.3    Honore, B.4
  • 3
    • 19244369899 scopus 로고    scopus 로고
    • Human calumenin gene (CALU): cDNA isolation and chromosomal mapping to 7q32
    • Yabe D, Taniwaki M, Nakamura T, Kanazawa N, Tashiro K, et al. (1998) Human calumenin gene (CALU): cDNA isolation and chromosomal mapping to 7q32. Genomics 49: 331-333.
    • (1998) Genomics , vol.49 , pp. 331-333
    • Yabe, D.1    Taniwaki, M.2    Nakamura, T.3    Kanazawa, N.4    Tashiro, K.5
  • 4
    • 0032979150 scopus 로고    scopus 로고
    • Crocalbin: a new calcium-binding protein that is also a binding protein for crotoxin, a neurotoxic phospholipase A2
    • Hseu MJ, Yen CH, Tzeng MC, (1999) Crocalbin: a new calcium-binding protein that is also a binding protein for crotoxin, a neurotoxic phospholipase A2. FEBS Lett 445: 440-444.
    • (1999) FEBS Lett , vol.445 , pp. 440-444
    • Hseu, M.J.1    Yen, C.H.2    Tzeng, M.C.3
  • 5
    • 33645108259 scopus 로고    scopus 로고
    • Calumenin, a multiple EF-hands Ca2+-binding protein, interacts with ryanodine receptor-1 in rabbit skeletal sarcoplasmic reticulum
    • Jung DH, Mo SH, Kim DH, (2006) Calumenin, a multiple EF-hands Ca2+-binding protein, interacts with ryanodine receptor-1 in rabbit skeletal sarcoplasmic reticulum. Biochem Biophys Res Commun 343: 34-42.
    • (2006) Biochem Biophys Res Commun , vol.343 , pp. 34-42
    • Jung, D.H.1    Mo, S.H.2    Kim, D.H.3
  • 6
    • 0032575258 scopus 로고    scopus 로고
    • Molecular cloning of a cDNA encoding human calumenin, expression in Escherichia coli and analysis of its Ca2+-binding activity
    • Vorum H, Liu X, Madsen P, Rasmussen HH, Honore B, (1998) Molecular cloning of a cDNA encoding human calumenin, expression in Escherichia coli and analysis of its Ca2+-binding activity. Biochim Biophys Acta 1386: 121-131.
    • (1998) Biochim Biophys Acta , vol.1386 , pp. 121-131
    • Vorum, H.1    Liu, X.2    Madsen, P.3    Rasmussen, H.H.4    Honore, B.5
  • 7
    • 65249104606 scopus 로고    scopus 로고
    • The rapidly expanding CREC protein family: members, localization, function, and role in disease
    • Honore B, (2009) The rapidly expanding CREC protein family: members, localization, function, and role in disease. Bioessays 31: 262-277.
    • (2009) Bioessays , vol.31 , pp. 262-277
    • Honore, B.1
  • 8
    • 0033134009 scopus 로고    scopus 로고
    • Human calumenin localizes to the secretory pathway and is secreted to the medium
    • Vorum H, Hager H, Christensen BM, Nielsen S, Honore B, (1999) Human calumenin localizes to the secretory pathway and is secreted to the medium. Exp Cell Res 248: 473-481.
    • (1999) Exp Cell Res , vol.248 , pp. 473-481
    • Vorum, H.1    Hager, H.2    Christensen, B.M.3    Nielsen, S.4    Honore, B.5
  • 9
    • 0033985775 scopus 로고    scopus 로고
    • Calumenin interacts with serum amyloid P component
    • Vorum H, Jacobsen C, Honore B, (2000) Calumenin interacts with serum amyloid P component. Febs Letters 465: 129-134.
    • (2000) Febs Letters , vol.465 , pp. 129-134
    • Vorum, H.1    Jacobsen, C.2    Honore, B.3
  • 10
    • 58049176372 scopus 로고    scopus 로고
    • Calumenin but not reticulocalbin forms a Ca(2+)-dependent complex with thrombospondin-1. A potential role in haemostasis and thrombosis
    • Honore B, Hansen GAW, Vorum H, Jacobsen C, (2009) Calumenin but not reticulocalbin forms a Ca(2+)-dependent complex with thrombospondin-1. A potential role in haemostasis and thrombosis. Molecular and Cellular Biochemistry 320: 25-33.
    • (2009) Molecular and Cellular Biochemistry , vol.320 , pp. 25-33
    • Honore, B.1    Hansen, G.A.W.2    Vorum, H.3    Jacobsen, C.4
  • 11
    • 0030610583 scopus 로고    scopus 로고
    • Calumenin, a Ca2+-binding protein retained in the endoplasmic reticulum with a novel carboxyl-terminal sequence, HDEF
    • Yabe D, Nakamura T, Kanazawa N, Tashiro K, Honjo T, (1997) Calumenin, a Ca2+-binding protein retained in the endoplasmic reticulum with a novel carboxyl-terminal sequence, HDEF. J Biol Chem 272: 18232-18239.
    • (1997) J Biol Chem , vol.272 , pp. 18232-18239
    • Yabe, D.1    Nakamura, T.2    Kanazawa, N.3    Tashiro, K.4    Honjo, T.5
  • 12
    • 2942627237 scopus 로고    scopus 로고
    • The inhibitory effect of calumenin on the vitamin K-dependent gamma-carboxylation system - Characterization of the system in normal and warfarin-resistant rats
    • Wajih N, Sane DC, Hutson SM, Wallin R, (2004) The inhibitory effect of calumenin on the vitamin K-dependent gamma-carboxylation system- Characterization of the system in normal and warfarin-resistant rats. Journal of Biological Chemistry 279: 25276-25283.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 25276-25283
    • Wajih, N.1    Sane, D.C.2    Hutson, S.M.3    Wallin, R.4
  • 13
    • 55249113945 scopus 로고    scopus 로고
    • Calumenin interacts with SERCA2 in rat cardiac sarcoplasmic reticulum
    • Kim DH, Sahoo SK, (2008) Calumenin interacts with SERCA2 in rat cardiac sarcoplasmic reticulum. Molecules and Cells 26: 265-269.
    • (2008) Molecules and Cells , vol.26 , pp. 265-269
    • Kim, D.H.1    Sahoo, S.K.2
  • 14
    • 70350446986 scopus 로고    scopus 로고
    • A novel endoplasmic reticulum export signal: proline at the +2-position from the signal peptide cleavage site
    • Tsukumo Y, Tsukahara S, Saito S, Tsuruo T, Tomida A, (2009) A novel endoplasmic reticulum export signal: proline at the +2-position from the signal peptide cleavage site. J Biol Chem 284: 27500-27510.
    • (2009) J Biol Chem , vol.284 , pp. 27500-27510
    • Tsukumo, Y.1    Tsukahara, S.2    Saito, S.3    Tsuruo, T.4    Tomida, A.5
  • 15
    • 0033985775 scopus 로고    scopus 로고
    • Calumenin interacts with serum amyloid P component
    • Vorum H, Jacobsen C, Honore B, (2000) Calumenin interacts with serum amyloid P component. FEBS Lett 465: 129-134.
    • (2000) FEBS Lett , vol.465 , pp. 129-134
    • Vorum, H.1    Jacobsen, C.2    Honore, B.3
  • 16
    • 33745697841 scopus 로고    scopus 로고
    • Proteomic profiling of fibroblasts reveals a modulating effect of extracellular calumenin on the organization of the actin cytoskeleton
    • Ostergaard M, Hansen GA, Vorum H, Honore B, (2006) Proteomic profiling of fibroblasts reveals a modulating effect of extracellular calumenin on the organization of the actin cytoskeleton. Proteomics 6: 3509-3519.
    • (2006) Proteomics , vol.6 , pp. 3509-3519
    • Ostergaard, M.1    Hansen, G.A.2    Vorum, H.3    Honore, B.4
  • 17
    • 61449242669 scopus 로고    scopus 로고
    • TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites
    • Saito K, Chen M, Bard F, Chen S, Zhou H, et al. (2009) TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites. Cell 136: 891-902.
    • (2009) Cell , vol.136 , pp. 891-902
    • Saito, K.1    Chen, M.2    Bard, F.3    Chen, S.4    Zhou, H.5
  • 19
    • 0023427610 scopus 로고
    • Effects of Cytochalasin and Phalloidin on Actin
    • Cooper JA, (1987) Effects of Cytochalasin and Phalloidin on Actin. Journal of Cell Biology 105: 1473-1478.
    • (1987) Journal of Cell Biology , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 20
    • 70349437416 scopus 로고    scopus 로고
    • Kinesin superfamily motor proteins and intracellular transport
    • Hirokawa N, Noda Y, Tanaka Y, Niwa S, (2009) Kinesin superfamily motor proteins and intracellular transport. Nat Rev Mol Cell Biol 10: 682-696.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 682-696
    • Hirokawa, N.1    Noda, Y.2    Tanaka, Y.3    Niwa, S.4
  • 21
    • 70450228589 scopus 로고    scopus 로고
    • Regulators of the cytoplasmic dynein motor
    • Kardon JR, Vale RD, (2009) Regulators of the cytoplasmic dynein motor. Nat Rev Mol Cell Biol 10: 854-865.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 854-865
    • Kardon, J.R.1    Vale, R.D.2
  • 22
    • 0032517767 scopus 로고    scopus 로고
    • Kinetic analysis of secretory protein traffic and characterization of golgi to plasma membrane transport intermediates in living cells
    • Hirschberg K, Miller CM, Ellenberg J, Presley JF, Siggia ED, et al. (1998) Kinetic analysis of secretory protein traffic and characterization of golgi to plasma membrane transport intermediates in living cells. J Cell Biol 143: 1485-1503.
    • (1998) J Cell Biol , vol.143 , pp. 1485-1503
    • Hirschberg, K.1    Miller, C.M.2    Ellenberg, J.3    Presley, J.F.4    Siggia, E.D.5
  • 23
    • 33947607769 scopus 로고    scopus 로고
    • The novel cargo Alcadein induces vesicle association of kinesin-1 motor components and activates axonal transport
    • Araki Y, Kawano T, Taru H, Saito Y, Wada S, et al. (2007) The novel cargo Alcadein induces vesicle association of kinesin-1 motor components and activates axonal transport. Embo J 26: 1475-1486.
    • (2007) Embo J , vol.26 , pp. 1475-1486
    • Araki, Y.1    Kawano, T.2    Taru, H.3    Saito, Y.4    Wada, S.5
  • 24
    • 34848926858 scopus 로고    scopus 로고
    • Polarization-dependent selective transport to the apical membrane by KIF5B in MDCK cells
    • Jaulin F, Xue X, Rodriguez-Boulan E, Kreitzer G, (2007) Polarization-dependent selective transport to the apical membrane by KIF5B in MDCK cells. Dev Cell 13: 511-522.
    • (2007) Dev Cell , vol.13 , pp. 511-522
    • Jaulin, F.1    Xue, X.2    Rodriguez-Boulan, E.3    Kreitzer, G.4
  • 27
    • 61849114654 scopus 로고    scopus 로고
    • NuMA-related LIN-5, ASPM-1, calmodulin and dynein promote meiotic spindle rotation independently of cortical LIN-5/GPR/Galpha
    • van der Voet M, Berends CW, Perreault A, Nguyen-Ngoc T, Gonczy P, et al. (2009) NuMA-related LIN-5, ASPM-1, calmodulin and dynein promote meiotic spindle rotation independently of cortical LIN-5/GPR/Galpha. Nat Cell Biol 11: 269-277.
    • (2009) Nat Cell Biol , vol.11 , pp. 269-277
    • van der Voet, M.1    Berends, C.W.2    Perreault, A.3    Nguyen-Ngoc, T.4    Gonczy, P.5
  • 28
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • Burkhardt JK, Echeverri CJ, Nilsson T, Vallee RB, (1997) Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution. J Cell Biol 139: 469-484.
    • (1997) J Cell Biol , vol.139 , pp. 469-484
    • Burkhardt, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 29
    • 14844331501 scopus 로고    scopus 로고
    • Molecular motors and mechanisms of directional transport in neurons
    • Hirokawa N, Takemura R, (2005) Molecular motors and mechanisms of directional transport in neurons. Nat Rev Neurosci 6: 201-214.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 201-214
    • Hirokawa, N.1    Takemura, R.2
  • 30
    • 77953290357 scopus 로고    scopus 로고
    • Characterization of kinesin-like proteins in silkworm posterior silkgland cells
    • Wang Q, Teng J, Shen B, Zhang W, Guo Y, et al. (2010) Characterization of kinesin-like proteins in silkworm posterior silkgland cells. Cell Res 20: 713-727.
    • (2010) Cell Res , vol.20 , pp. 713-727
    • Wang, Q.1    Teng, J.2    Shen, B.3    Zhang, W.4    Guo, Y.5
  • 31
    • 33751572018 scopus 로고    scopus 로고
    • Cargo selection by specific kinesin light chain 1 isoforms
    • Wozniak MJ, Allan VJ, (2006) Cargo selection by specific kinesin light chain 1 isoforms. Embo Journal 25: 5457-5468.
    • (2006) Embo Journal , vol.25 , pp. 5457-5468
    • Wozniak, M.J.1    Allan, V.J.2
  • 32
    • 0035900480 scopus 로고    scopus 로고
    • Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles
    • Belden WJ, Barlowe C, (2001) Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles. Science 294: 1528-1531.
    • (2001) Science , vol.294 , pp. 1528-1531
    • Belden, W.J.1    Barlowe, C.2
  • 33
    • 0032495477 scopus 로고    scopus 로고
    • COPII-cargo interactions direct protein sorting into ER-derived transport vesicles
    • Kuehn MJ, Herrmann JM, Schekman R, (1998) COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature 391: 187-190.
    • (1998) Nature , vol.391 , pp. 187-190
    • Kuehn, M.J.1    Herrmann, J.M.2    Schekman, R.3
  • 34
    • 0023658351 scopus 로고
    • The rate of bulk flow from the endoplasmic reticulum to the cell surface
    • Wieland FT, Gleason ML, Serafini TA, Rothman JE, (1987) The rate of bulk flow from the endoplasmic reticulum to the cell surface. Cell 50: 289-300.
    • (1987) Cell , vol.50 , pp. 289-300
    • Wieland, F.T.1    Gleason, M.L.2    Serafini, T.A.3    Rothman, J.E.4
  • 35
    • 0033538549 scopus 로고    scopus 로고
    • Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles
    • Martinez-Menarguez JA, Geuze HJ, Slot JW, Klumperman J, (1999) Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles. Cell 98: 81-90.
    • (1999) Cell , vol.98 , pp. 81-90
    • Martinez-Menarguez, J.A.1    Geuze, H.J.2    Slot, J.W.3    Klumperman, J.4
  • 36
    • 0037164807 scopus 로고    scopus 로고
    • Concentrative sorting of secretory cargo proteins into COPII-coated vesicles
    • Malkus P, Jiang F, Schekman R, (2002) Concentrative sorting of secretory cargo proteins into COPII-coated vesicles. J Cell Biol 159: 915-921.
    • (2002) J Cell Biol , vol.159 , pp. 915-921
    • Malkus, P.1    Jiang, F.2    Schekman, R.3
  • 37
    • 0345687308 scopus 로고    scopus 로고
    • Mechanism of constitutive export from the golgi: bulk flow via the formation, protrusion, and en bloc cleavage of large trans-golgi network tubular domains
    • Polishchuk EV, Di Pentima A, Luini A, Polishchuk RS, (2003) Mechanism of constitutive export from the golgi: bulk flow via the formation, protrusion, and en bloc cleavage of large trans-golgi network tubular domains. Mol Biol Cell 14: 4470-4485.
    • (2003) Mol Biol Cell , vol.14 , pp. 4470-4485
    • Polishchuk, E.V.1    Di Pentima, A.2    Luini, A.3    Polishchuk, R.S.4
  • 38
    • 0022402201 scopus 로고
    • Pathways of protein secretion in eukaryotes
    • Kelly RB, (1985) Pathways of protein secretion in eukaryotes. Science 230: 25-32.
    • (1985) Science , vol.230 , pp. 25-32
    • Kelly, R.B.1
  • 39
    • 12344277564 scopus 로고    scopus 로고
    • Coupling of ER exit to microtubules through direct interaction of COPII with dynactin
    • Watson P, Forster R, Palmer KJ, Pepperkok R, Stephens DJ, (2005) Coupling of ER exit to microtubules through direct interaction of COPII with dynactin. Nat Cell Biol 7: 48-55.
    • (2005) Nat Cell Biol , vol.7 , pp. 48-55
    • Watson, P.1    Forster, R.2    Palmer, K.J.3    Pepperkok, R.4    Stephens, D.J.5
  • 41
    • 4143088149 scopus 로고    scopus 로고
    • Kinesin transports RNA: isolation and characterization of an RNA-transporting granule
    • Kanai Y, Dohmae N, Hirokawa N, (2004) Kinesin transports RNA: isolation and characterization of an RNA-transporting granule. Neuron 43: 513-525.
    • (2004) Neuron , vol.43 , pp. 513-525
    • Kanai, Y.1    Dohmae, N.2    Hirokawa, N.3
  • 42
    • 34547414652 scopus 로고    scopus 로고
    • Rab6 regulates transport and targeting of exocytotic carriers
    • Grigoriev I, Splinter D, Keijzer N, Wulf PS, Demmers J, et al. (2007) Rab6 regulates transport and targeting of exocytotic carriers. Dev Cell 13: 305-314.
    • (2007) Dev Cell , vol.13 , pp. 305-314
    • Grigoriev, I.1    Splinter, D.2    Keijzer, N.3    Wulf, P.S.4    Demmers, J.5
  • 44
    • 68949167657 scopus 로고    scopus 로고
    • Role of kinesin-1 and cytoplasmic dynein in endoplasmic reticulum movement in VERO cells
    • Wozniak MJ, Bola B, Brownhill K, Yang YC, Levakova V, et al. (2009) Role of kinesin-1 and cytoplasmic dynein in endoplasmic reticulum movement in VERO cells. J Cell Sci 122: 1979-1989.
    • (2009) J Cell Sci , vol.122 , pp. 1979-1989
    • Wozniak, M.J.1    Bola, B.2    Brownhill, K.3    Yang, Y.C.4    Levakova, V.5
  • 45
    • 20344382542 scopus 로고    scopus 로고
    • Kinesin and dynein move a peroxisome in vivo: a tug-of-war or coordinated movement?
    • Kural C, Kim H, Syed S, Goshima G, Gelfand VI, et al. (2005) Kinesin and dynein move a peroxisome in vivo: a tug-of-war or coordinated movement? Science 308: 1469-1472.
    • (2005) Science , vol.308 , pp. 1469-1472
    • Kural, C.1    Kim, H.2    Syed, S.3    Goshima, G.4    Gelfand, V.I.5
  • 47
    • 0018399531 scopus 로고
    • The chromaffin granule surface: the presence of actin and the nature of its interaction with the membrane
    • Meyer DI, Burger MM, (1979) The chromaffin granule surface: the presence of actin and the nature of its interaction with the membrane. FEBS Lett 101: 129-133.
    • (1979) FEBS Lett , vol.101 , pp. 129-133
    • Meyer, D.I.1    Burger, M.M.2
  • 48
    • 0023321856 scopus 로고
    • Reorganisation of peripheral actin filaments as a prelude to exocytosis
    • Burgoyne RD, Cheek TR, (1987) Reorganisation of peripheral actin filaments as a prelude to exocytosis. Biosci Rep 7: 281-288.
    • (1987) Biosci Rep , vol.7 , pp. 281-288
    • Burgoyne, R.D.1    Cheek, T.R.2
  • 49
    • 43049100759 scopus 로고    scopus 로고
    • Genome-wide screen reveals APC-associated RNAs enriched in cell protrusions
    • Mili S, Moissoglu K, Macara IG, (2008) Genome-wide screen reveals APC-associated RNAs enriched in cell protrusions. Nature 453: 115-119.
    • (2008) Nature , vol.453 , pp. 115-119
    • Mili, S.1    Moissoglu, K.2    Macara, I.G.3
  • 50
    • 33745506389 scopus 로고    scopus 로고
    • CLASPs attach microtubule plus ends to the cell cortex through a complex with LL5beta
    • Lansbergen G, Grigoriev I, Mimori-Kiyosue Y, Ohtsuka T, Higa S, et al. (2006) CLASPs attach microtubule plus ends to the cell cortex through a complex with LL5beta. Dev Cell 11: 21-32.
    • (2006) Dev Cell , vol.11 , pp. 21-32
    • Lansbergen, G.1    Grigoriev, I.2    Mimori-Kiyosue, Y.3    Ohtsuka, T.4    Higa, S.5
  • 51
    • 78149297473 scopus 로고    scopus 로고
    • Clathrin recruits phosphorylated TACC3 to spindle poles for bipolar spindle assembly and chromosome alignment
    • Fu W, Tao W, Zheng P, Fu J, Bian M, et al. Clathrin recruits phosphorylated TACC3 to spindle poles for bipolar spindle assembly and chromosome alignment. J Cell Sci 123: 3645-3651.
    • J Cell Sci , vol.123 , pp. 3645-3651
    • Fu, W.1    Tao, W.2    Zheng, P.3    Fu, J.4    Bian, M.5
  • 52
    • 75849139266 scopus 로고    scopus 로고
    • The regulatory mechanism of Hsp90alpha secretion and its function in tumor malignancy
    • Wang X, Song X, Zhuo W, Fu Y, Shi H, et al. (2009) The regulatory mechanism of Hsp90alpha secretion and its function in tumor malignancy. Proc Natl Acad Sci U S A 106: 21288-21293.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 21288-21293
    • Wang, X.1    Song, X.2    Zhuo, W.3    Fu, Y.4    Shi, H.5
  • 53
    • 33751509047 scopus 로고    scopus 로고
    • 14-3-3 gamma affects dynamics and integrity of glial filaments by binding to phosphorylated GFAP
    • Li HH, Guo Y, Teng JL, Ding MX, Yu ACH, et al. (2006) 14-3-3 gamma affects dynamics and integrity of glial filaments by binding to phosphorylated GFAP. Journal of Cell Science 119: 4452-4461.
    • (2006) Journal of Cell Science , vol.119 , pp. 4452-4461
    • Li, H.H.1    Guo, Y.2    Teng, J.L.3    Ding, M.X.4    Yu, A.C.H.5
  • 54
    • 77953290357 scopus 로고    scopus 로고
    • Characterization of Kinesin-like Proteins in Silkworm Posterior Silkgland Cells
    • Wang Q, Teng J, Shen B, Zhang W, Guo Y, et al. (2010) Characterization of Kinesin-like Proteins in Silkworm Posterior Silkgland Cells. Cell Res.
    • (2010) Cell Res
    • Wang, Q.1    Teng, J.2    Shen, B.3    Zhang, W.4    Guo, Y.5
  • 55
    • 0037007668 scopus 로고    scopus 로고
    • Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites
    • Setou M, Seog DH, Tanaka Y, Kanai Y, Takei Y, et al. (2002) Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites. Nature 417: 83-87.
    • (2002) Nature , vol.417 , pp. 83-87
    • Setou, M.1    Seog, D.H.2    Tanaka, Y.3    Kanai, Y.4    Takei, Y.5
  • 56
    • 70350007286 scopus 로고    scopus 로고
    • Opposing effects of Ndel1 and alpha1 or alpha2 on cytoplasmic dynein through competitive binding to Lis1
    • Ding C, Liang X, Ma L, Yuan X, Zhu X, (2009) Opposing effects of Ndel1 and alpha1 or alpha2 on cytoplasmic dynein through competitive binding to Lis1. J Cell Sci 122: 2820-2827.
    • (2009) J Cell Sci , vol.122 , pp. 2820-2827
    • Ding, C.1    Liang, X.2    Ma, L.3    Yuan, X.4    Zhu, X.5
  • 57
    • 78149472115 scopus 로고    scopus 로고
    • Silkworm coatomers and their role in tube expansion of posterior silkgland
    • Wang Q, Shen B, Zheng P, Feng H, Chen L, et al. (2010) Silkworm coatomers and their role in tube expansion of posterior silkgland. PLoS ONE 5: e13252.
    • (2010) PLoS ONE , vol.5
    • Wang, Q.1    Shen, B.2    Zheng, P.3    Feng, H.4    Chen, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.