메뉴 건너뛰기




Volumn 37, Issue 2, 2010, Pages 445-454

Characterisation of a multimeric protein complex associated with ERp57 within the nucleus in paclitaxel-sensitive and -resistant epithelial ovarian cancer cells: The involvement of specific conformational states of β-actin

Author keywords

Chemoresistance; ERp57; Mass spectrometry; Ovarian cancer; Paclitaxel

Indexed keywords

AURORA C KINASE; BETA ACTIN; NUCLEOLIN; NUCLEOPHOSMIN; PACLITAXEL; PROTEIN; PROTEIN ERP57; UNCLASSIFIED DRUG; VIMENTIN; ACTIN; ANTINEOPLASTIC AGENT; MULTIPROTEIN COMPLEX; PDIA3 PROTEIN, HUMAN; PROTEIN DISULFIDE ISOMERASE;

EID: 77954157573     PISSN: 10196439     EISSN: 17912423     Source Type: Journal    
DOI: 10.3892/ijo-0000693     Document Type: Article
Times cited : (27)

References (71)
  • 2
    • 38449097524 scopus 로고    scopus 로고
    • Mechanisms of multidrug resistance: The potential role of microtubule-stabilizing agents
    • Fojo T and Menefee M: Mechanisms of multidrug resistance: the potential role of microtubule-stabilizing agents. Ann Oncol 18 (Suppl. 5): V3-V8, 2007.
    • (2007) Ann Oncol , vol.18 , Issue.SUPPL. 5
    • Fojo, T.1    Menefee, M.2
  • 3
    • 65349153918 scopus 로고    scopus 로고
    • Comparative proteomic analysis of paclitaxel sensitive A2780 epithelial ovarian cancer cell line and its resistant counterpart A2780TC1 by 2D-DIGE: The role of ERp57
    • Cicchillitti L, Di Michele M, Urbani A, Ferlini C, Donati MB, Scambia G and Rotilio D: Comparative proteomic analysis of paclitaxel sensitive A2780 epithelial ovarian cancer cell line and its resistant counterpart A2780TC1 by 2D-DIGE: the role of ERp57. J Proteome Res 8: 1902-1912, 2009.
    • (2009) J Proteome Res , vol.8 , pp. 1902-1912
    • Cicchillitti, L.1    Di Michele, M.2    Urbani, A.3    Ferlini, C.4    Donati, M.B.5    Scambia, G.6    Rotilio, D.7
  • 6
    • 0029074071 scopus 로고
    • A possible role of ER-60 protease in the degradation of misfolded proteins in the endoplasmic reticulum
    • Otsu M, Urade R, Kito M, Omura F and Kikuchi M: A possible role of ER-60 protease in the degradation of misfolded proteins in the endoplasmic reticulum. J Biol Chem 270: 14958-14961, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 14958-14961
    • Otsu, M.1    Urade, R.2    Kito, M.3    Omura, F.4    Kikuchi, M.5
  • 7
    • 0028114733 scopus 로고
    • A stress-regulated protein, GRP58, a member of thioredoxin superfamily, is a carnitine palmitoyl-transferase isoenzyme
    • Murthy MS and Pande SV: A stress-regulated protein, GRP58, a member of thioredoxin superfamily, is a carnitine palmitoyl-transferase isoenzyme. Biochem J 304: 31-34, 1994.
    • (1994) Biochem J , vol.304 , pp. 31-34
    • Murthy, M.S.1    Pande, S.V.2
  • 8
    • 0032754311 scopus 로고    scopus 로고
    • Molecular dissection of nucleolin's role in growth and cell proliferation: New insights
    • Srivastava M and Pollard HB: Molecular dissection of nucleolin's role in growth and cell proliferation: new insights. FASEB J 13: 1911-1922, 1999.
    • (1999) FASEB J , vol.13 , pp. 1911-1922
    • Srivastava, M.1    Pollard, H.B.2
  • 9
    • 0028823248 scopus 로고
    • Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation
    • Hirano N, Shibasaki F, Sakai R, Tanaka T, Nishida J, Yazaki Y, Takenawa T and Hirai H: Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation. Eur J Biochem 234: 336-342, 1995.
    • (1995) Eur J Biochem , vol.234 , pp. 336-342
    • Hirano, N.1    Shibasaki, F.2    Sakai, R.3    Tanaka, T.4    Nishida, J.5    Yazaki, Y.6    Takenawa, T.7    Hirai, H.8
  • 10
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: Building bridges in protein folding
    • DOI 10.1016/0968-0004(94)90072-8
    • Freedman RB, Hirst TR and Tuite MF: Protein disulphide isomerase: building bridges in protein folding. Trends Biochem Sci 19: 331-336, 1994. (Pubitemid 24259985)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.8 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 12
    • 0036087077 scopus 로고    scopus 로고
    • Interaction with grp58 increases activity of the thiazide-sensitive Na-Cl cotransporter
    • Wyse B, Ali N and Ellison DH: Interaction with grp58 increases activity of the thiazide-sensitive Na-Cl cotransporter. Am J Physiol Renal Physiol 282: F424-F430, 2002. (Pubitemid 34654530)
    • (2002) American Journal of Physiology - Renal Physiology , vol.282 , Issue.3
    • Wyse, B.1    Ali, N.2    Ellison, D.H.3
  • 13
    • 0037228781 scopus 로고    scopus 로고
    • A nuclear protein complex containing high mobility group proteins B1 and B2, heat shock cognate protein 70, ERp60, and glyceraldehyde-3-phosphate dehydrogenase is involved in the cytotoxic response to DNA modified by incorporation of anticancer nucleoside analogues
    • Krynetski EY, Krynetskaia NF, Bianchi ME and Evans WE: A nuclear protein complex containing high mobility group proteins B1 and B2, heat shock cognate protein 70, ERp60, and glyceraldehyde-3-phosphate dehydrogenase is involved in the cytotoxic response to DNA modified by incorporation of anticancer nucleoside analogues. Cancer Res 63: 100-106, 2003.
    • (2003) Cancer Res , vol.63 , pp. 100-106
    • Krynetski, E.Y.1    Krynetskaia, N.F.2    Bianchi, M.E.3    Evans, W.E.4
  • 15
    • 66849140943 scopus 로고    scopus 로고
    • MicroRNA-200c mitigates invasiveness and restores sensitivity to microtubule-targeting chemotherapeutic agents
    • In press
    • Cochrane DR, Spoelstra NS, Howe EN, Nordeen SK and Richer JK: MicroRNA-200c mitigates invasiveness and restores sensitivity to microtubule-targeting chemotherapeutic agents. Mol Cancer Ther (In press).
    • Mol Cancer Ther
    • Cochrane, D.R.1    Spoelstra, N.S.2    Howe, E.N.3    Nordeen, S.K.4    Richer, J.K.5
  • 18
    • 0033597825 scopus 로고    scopus 로고
    • Signal-regulated activation of serum response factor is mediated by changes in actin dynamics
    • DOI 10.1016/S0092-8674(00)81011-9
    • Sotiropoulos A, Gineitis D, Copeland J and Treisman R: Signal-regulated activation of serum response factor is mediated by changes in actin dynamics. Cell 98: 159-169, 1999. (Pubitemid 29344904)
    • (1999) Cell , vol.98 , Issue.2 , pp. 159-169
    • Sotiropoulos, A.1    Gineitis, D.2    Copeland, J.3    Treisman, R.4
  • 19
    • 33644852058 scopus 로고    scopus 로고
    • Actin and myosin as transcription factors
    • Grummt I: Actin and myosin as transcription factors. Curr Opin Genet Dev 16: 191-196, 2006.
    • (2006) Curr Opin Genet Dev , vol.16 , pp. 191-196
    • Grummt, I.1
  • 20
    • 0014443113 scopus 로고
    • Intranuclear fibrillar bodies in actinomycin D-treated oocytes
    • Lane NJ: Intranuclear fibrillar bodies in actinomycin D-treated oocytes. J Cell Biol 40: 286-291, 1969.
    • (1969) J Cell Biol , vol.40 , pp. 286-291
    • Lane, N.J.1
  • 21
    • 0035997387 scopus 로고    scopus 로고
    • Nuclear actin and actin-related proteins in chromatin remodeling
    • DOI 10.1146/annurev.biochem.71.110601.135507
    • Olave IA, Reck-Peterson SL and Crabtree GR: Nuclear actin and actin-related proteins in chromatin remodeling. Annu Rev Biochem 71: 755-781, 2002. (Pubitemid 34800234)
    • (2002) Annual Review of Biochemistry , vol.71 , pp. 755-781
    • Olave, I.A.1    Reck-Peterson, S.L.2    Crabtree, G.R.3
  • 23
    • 27644506209 scopus 로고    scopus 로고
    • Nuclear actin extends, with no contraction in sight
    • DOI 10.1091/mbc.E05-07-0656
    • Pederson T and Aebi U: Nuclear actin extends, with no contraction in sight. Mol Biol Cell 16: 5055-5060, 2005. (Pubitemid 41566818)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.11 , pp. 5055-5060
    • Pederson, T.1    Aebi, U.2
  • 24
    • 33645285000 scopus 로고    scopus 로고
    • Molecular functions of nuclear actin in transcription
    • Percipalle P and Visa N: Molecular functions of nuclear actin in transcription. J Cell Biol 172: 967-971, 2006.
    • (2006) J Cell Biol , vol.172 , pp. 967-971
    • Percipalle, P.1    Visa, N.2
  • 25
    • 23944495664 scopus 로고    scopus 로고
    • The growing pre-mRNA recruits actin and chromatin-modifying factors to transcriptionally active genes
    • Sjolinder M, Bjork P, Soderberg E, Sabri N, Farrants AK and Visa N: The growing pre-mRNA recruits actin and chromatin-modifying factors to transcriptionally active genes. Genes Dev 19: 1871-1884, 2005.
    • (2005) Genes Dev , vol.19 , pp. 1871-1884
    • Sjolinder, M.1    Bjork, P.2    Soderberg, E.3    Sabri, N.4    Farrants, A.K.5    Visa, N.6
  • 27
    • 0032523820 scopus 로고    scopus 로고
    • A pancreas-specific glycosylated protein disulphide-isomerase binds to misfolded proteins and peptides with an interaction inhibited by oestrogens
    • Klappa P, Stromer T, Zimmermann R, Ruddock LW and Freedman RB: A pancreas-specific glycosylated protein disulphide-isomerase binds to misfolded proteins and peptides with an interaction inhibited by oestrogens. Eur J Biochem 254: 63-69, 1998.
    • (1998) Eur J Biochem , vol.254 , pp. 63-69
    • Klappa, P.1    Stromer, T.2    Zimmermann, R.3    Ruddock, L.W.4    Freedman, R.B.5
  • 28
    • 29344442591 scopus 로고    scopus 로고
    • Evidence for phosphorylation of rat liver glucose-regulated protein 58, GRP58/ERp57/ER-60, induced by fasting and leptin
    • Kita K, Okumura N, Takao T, Watanabe M, Matsubara T, Nishimura O and Nagai K: Evidence for phosphorylation of rat liver glucose-regulated protein 58, GRP58/ERp57/ER-60, induced by fasting and leptin. FEBS Lett 580: 199-205, 2006.
    • (2006) FEBS Lett , vol.580 , pp. 199-205
    • Kita, K.1    Okumura, N.2    Takao, T.3    Watanabe, M.4    Matsubara, T.5    Nishimura, O.6    Nagai, K.7
  • 29
    • 36048968942 scopus 로고    scopus 로고
    • Oxidation of Prx2 and phosphorylation of GRP58 by angiotensin II in human coronary smooth muscle cells identified by 2D-DIGE analysis
    • Tokutomi Y, Arak, N, Kataoka K, Yamamoto E and Kim-Mitsuyama S: Oxidation of Prx2 and phosphorylation of GRP58 by angiotensin II in human coronary smooth muscle cells identified by 2D-DIGE analysis. Biochem Biophys Res Commun 364: 822-830, 2007.
    • (2007) Biochem Biophys Res Commun , vol.364 , pp. 822-830
    • Tokutomi, Y.1    Arak, N.2    Kataoka, K.3    Yamamoto, E.4    Kim-Mitsuyama, S.5
  • 30
    • 34249777555 scopus 로고    scopus 로고
    • Functions of the histone chaperone nucleolin in diseases
    • Storck S, Shukla M, Dimitrov S and Bouvet P: Functions of the histone chaperone nucleolin in diseases. Subcell Biochem 41: 125-144, 2007.
    • (2007) Subcell Biochem , vol.41 , pp. 125-144
    • Storck, S.1    Shukla, M.2    Dimitrov, S.3    Bouvet, P.4
  • 31
    • 0037052950 scopus 로고    scopus 로고
    • Identification of nucleolin and nucleophosmin as genotoxic stress-responsive RNA-binding proteins
    • Yang C, Maiguel DA and Carrier F: Identification of nucleolin and nucleophosmin as genotoxic stress-responsive RNA-binding proteins. Nucleic Acids Res 30: 2251-2260, 2002. (Pubitemid 34567946)
    • (2002) Nucleic Acids Research , vol.30 , Issue.10 , pp. 2251-2260
    • Yang, C.1    Maiguel, D.A.2    Carrier, F.3
  • 32
    • 0033548619 scopus 로고    scopus 로고
    • Cell cycle-dependent expression and centrosome localization of a third human Aurora/Ipl1-related protein kinase, AIK3
    • Kimura M, Matsuda Y, Yoshioka T and Okano Y: Cell cycle-dependent expression and centrosome localization of a third human aurora/Ipl1-related protein kinase, AIK3. J Biol Chem 274: 7334-7340, 1999. (Pubitemid 129505026)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.2-11 , pp. 7334-7340
    • Kimura, M.1    Matsuda, Y.2    Yoshioka, T.3    Okano, Y.4
  • 34
    • 51649095569 scopus 로고    scopus 로고
    • The Aurora kinase family in cell division and cancer
    • Vader G and Lens SM: The Aurora kinase family in cell division and cancer. Biochim Biophys Acta 1786: 60-72, 2008.
    • (2008) Biochim Biophys Acta , vol.1786 , pp. 60-72
    • Vader, G.1    Lens, S.M.2
  • 37
    • 0031714080 scopus 로고    scopus 로고
    • Tumour amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation
    • DOI 10.1038/2496
    • Zhou H, Kuang J, Zhong L, Kuo WL, Gray JW, Sahin A, Brinkley BR and Sen S: Tumour amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation. Nat Genet 20: 189-193, 1998. (Pubitemid 28455454)
    • (1998) Nature Genetics , vol.20 , Issue.2 , pp. 189-193
    • Zhou, H.1    Kuang, J.2    Zhong, L.3    Kuo, W.-L.4    Gray, J.W.5    Sahin, A.6    Brinkley, B.R.7    Sen, S.8
  • 38
    • 33646004279 scopus 로고    scopus 로고
    • Regulatory mechanisms and functions of intermediate filaments: A study using site- And phosphorylation state-specific antibodies
    • Izawa I and Inagaki M: Regulatory mechanisms and functions of intermediate filaments: a study using site- and phosphorylation state-specific antibodies. Cancer Sci 97: 167-174, 2006.
    • (2006) Cancer Sci , vol.97 , pp. 167-174
    • Izawa, I.1    Inagaki, M.2
  • 41
    • 50349084887 scopus 로고    scopus 로고
    • Actin and microtubules: Working together to control spindle polarity
    • Xu FL and Saunders WS: Actin and microtubules: working together to control spindle polarity. Cancer Cell 14: 197-199, 2008.
    • (2008) Cancer Cell , vol.14 , pp. 197-199
    • Xu, F.L.1    Saunders, W.S.2
  • 43
    • 28944449940 scopus 로고    scopus 로고
    • Conformation-specific antibodies reveal distinct actin structures in the nucleus and the cytoplasm
    • DOI 10.1016/j.jsb.2005.09.003, PII S1047847705001930
    • Schoenenberger CA, Buchmeier S, Boerries M, Sutterlin R, Aebi U and Jockusch BM: Conformation-specific antibodies reveal distinct actin structures in the nucleus and the cytoplasm. J Struct Biol 152: 157-168, 2005. (Pubitemid 41785513)
    • (2005) Journal of Structural Biology , vol.152 , Issue.3 , pp. 157-168
    • Schoenenberger, C.-A.1    Buchmeier, S.2    Boerries, M.3    Sutterlin, R.4    Aebi, U.5    Jockusch, B.M.6
  • 44
    • 0032957520 scopus 로고    scopus 로고
    • Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody
    • Gonsior SM, Platz S, Buchmeier S, Scheer U, Jockusch BM and Hinssen H: Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody. J Cell Sci 112: 797-809, 1999. (Pubitemid 29179313)
    • (1999) Journal of Cell Science , vol.112 , Issue.6 , pp. 797-809
    • Gonsior, S.M.1    Platz, S.2    Buchmeier, S.3    Scheer, U.4    Jockusch, B.M.5    Hinssen, H.6
  • 45
    • 2342505236 scopus 로고    scopus 로고
    • Separate Roles and Different Routing of Calnexin and ERp57 in Endoplasmic Reticulum Quality Control Revealed by Interactions with Asialoglycoprotein Receptor Chains
    • DOI 10.1091/mbc.E03-12-0899
    • Frenkel Z, Shenkman M, Kondratyev M and Lederkremer GZ: Separate roles and different routing of calnexin and ERp57 in endoplasmic reticulum quality control revealed by interactions with asialoglycoprotein receptor chains. Mol Biol Cell 15: 2133-2142, 2004. (Pubitemid 38580633)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.5 , pp. 2133-2142
    • Frenkel, Z.1    Shenkman, M.2    Kondratyev, M.3    Lederkremer, G.Z.4
  • 46
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • DOI 10.1038/47062
    • Molinari M and Helenius A: Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature 402: 90-93, 1999. (Pubitemid 29533521)
    • (1999) Nature , vol.402 , Issue.6757 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 47
    • 34447558236 scopus 로고    scopus 로고
    • ER chaperones in mammalian development and human diseases
    • DOI 10.1016/j.febslet.2007.04.045, PII S0014579307004334, Cellular Stress
    • Ni M and Lee AS: ER chaperones in mammalian development and human diseases. FEBS Lett 581: 3641-3651, 2007. (Pubitemid 47082516)
    • (2007) FEBS Letters , vol.581 , Issue.19 , pp. 3641-3651
    • Ni, M.1    Lee, A.S.2
  • 50
    • 33748329644 scopus 로고    scopus 로고
    • Cooperative activity of Ref-1/APE and ERp57 in reductive activation of transcription factors
    • DOI 10.1016/j.freeradbiomed.2006.06.016, PII S0891584906004199
    • Grillo C, D'Ambrosio C, Scaloni A, Maceroni M, Merluzzi S, Turano C and Altieri F: Cooperative activity of Ref-1/APE and ERp57 in reductive activation of transcription factors. Free Radic Biol Med 41: 1113-1123, 2006. (Pubitemid 44331573)
    • (2006) Free Radical Biology and Medicine , vol.41 , Issue.7 , pp. 1113-1123
    • Grillo, C.1    D'Ambrosio, C.2    Scaloni, A.3    Maceroni, M.4    Merluzzi, S.5    Turano, C.6    Altieri, F.7
  • 51
    • 0141619285 scopus 로고    scopus 로고
    • Role of GRP58 in mitomycin C-induced DNA cross-linking
    • Celli CM and Jaiswal AK: Role of GRP58 in mitomycin C-induced DNA cross-linking. Cancer Res 63: 6016-6025, 2003.
    • (2003) Cancer Res , vol.63 , pp. 6016-6025
    • Celli, C.M.1    Jaiswal, A.K.2
  • 52
    • 55549130231 scopus 로고    scopus 로고
    • Overlapping signal sequences control nuclear localization and endoplasmic reticulum retention of GRP58
    • Adikesavan AK, Unni E and Jaiswal AK: Overlapping signal sequences control nuclear localization and endoplasmic reticulum retention of GRP58. Biochem Biophys Res Commun 377: 407-412, 2008.
    • (2008) Biochem Biophys Res Commun , vol.377 , pp. 407-412
    • Adikesavan, A.K.1    Unni, E.2    Jaiswal, A.K.3
  • 53
    • 56149087648 scopus 로고    scopus 로고
    • Nucleophosmin is required for chromosome congression, proper mitotic spindle formation, and kinetochore-microtubule attachment in HeLa cells
    • Amin MA, Matsunaga S, Uchiyama S and Fukui K: Nucleophosmin is required for chromosome congression, proper mitotic spindle formation, and kinetochore-microtubule attachment in HeLa cells. FEBS Lett 582: 3839-3844, 2008.
    • (2008) FEBS Lett , vol.582 , pp. 3839-3844
    • Amin, M.A.1    Matsunaga, S.2    Uchiyama, S.3    Fukui, K.4
  • 54
    • 4744348300 scopus 로고    scopus 로고
    • Hypoxia-induced nucleophosmin protects cell death through inhibition of p53
    • DOI 10.1074/jbc.C400297200
    • Li J, Zhang X, Sejas DP, Bagby GC and Pang Q: Hypoxia-induced nucleophosmin protects cell death through inhibition of p53. J Biol Chem 279: 41275-41279, 2004. (Pubitemid 39313565)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.40 , pp. 41275-41279
    • Li, J.1    Zhang, X.2    Sejas, D.P.3    Bagby, G.C.4    Pang, Q.5
  • 56
    • 66449133562 scopus 로고    scopus 로고
    • The Aurora kinase inhibitor SNS-314 shows broad therapeutic potential with chemo+- Therapeutics and synergy with microtubule-targeted agents in a colon carcinoma model
    • VanderPorten EC, Taverna P, Hogan JN, Ballinger MD, Flanagan WM and Fucini RV: The Aurora kinase inhibitor SNS-314 shows broad therapeutic potential with chemo+- therapeutics and synergy with microtubule-targeted agents in a colon carcinoma model. Mol Cancer Ther 8: 930-939, 2009.
    • (2009) Mol Cancer Ther , vol.8 , pp. 930-939
    • VanderPorten, E.C.1    Taverna, P.2    Hogan, J.N.3    Ballinger, M.D.4    Flanagan, W.M.5    Fucini, R.V.6
  • 57
    • 67649345473 scopus 로고    scopus 로고
    • Aurora B kinase inhibition in mitosis: Strategies for optimising the use of aurora kinase inhibitors such as AT9283
    • Curry J, Angove H, Fazal L, Lyons J, Reule M, Thompson N and Wallis N: Aurora B kinase inhibition in mitosis: strategies for optimising the use of aurora kinase inhibitors such as AT9283. Cell Cycle 8: 1921-1929, 2009.
    • (2009) Cell Cycle , vol.8 , pp. 1921-1929
    • Curry, J.1    Angove, H.2    Fazal, L.3    Lyons, J.4    Reule, M.5    Thompson, N.6    Wallis, N.7
  • 59
    • 34848822818 scopus 로고    scopus 로고
    • Chromosome protein framework from proteome analysis of isolated human metaphase chromosomes
    • Fukui K and Uchiyama S: Chromosome protein framework from proteome analysis of isolated human metaphase chromosomes. Chem Rec 7: 230-237, 2007.
    • (2007) Chem Rec , vol.7 , pp. 230-237
    • Fukui, K.1    Uchiyama, S.2
  • 60
    • 57349187712 scopus 로고    scopus 로고
    • A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin
    • Slawson C, Lakshmanan T, Knapp S and Hart GW: A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin. Mol Biol Cell 19: 4130-4140, 2008.
    • (2008) Mol Biol Cell , vol.19 , pp. 4130-4140
    • Slawson, C.1    Lakshmanan, T.2    Knapp, S.3    Hart, G.W.4
  • 62
    • 0036531790 scopus 로고    scopus 로고
    • Differential mitotic responses to microtubule-stabilizing and -destabilizing drugs
    • Chen JG and Horwitz SB: Differential mitotic responses to microtubule-stabilizing and -destabilizing drugs. Cancer Res 62: 1935-1938, 2002.
    • (2002) Cancer Res , vol.62 , pp. 1935-1938
    • Chen, J.G.1    Horwitz, S.B.2
  • 63
    • 0345275866 scopus 로고    scopus 로고
    • Gene Expression and Mitotic Exit Induced by Microtubule-Stabilizing Drugs
    • Chen JG, Yang CP, Cammer M and Horwitz SB: Gene expression and mitotic exit induced by microtubule-stabilizing drugs. Cancer Res 63: 7891-7899, 2003. (Pubitemid 37466724)
    • (2003) Cancer Research , vol.63 , Issue.22 , pp. 7891-7899
    • Chen, J.-G.1    Yang, C.-P.H.2    Cammer, M.3    Horwitz, S.B.4
  • 64
    • 41549114618 scopus 로고    scopus 로고
    • As functional nuclear actin comes into view, is it globular, filamentous
    • Pederson T: As functional nuclear actin comes into view, is it globular, filamentous, or both? J Cell Biol 180: 1061-1064, 2008.
    • (2008) Or Both? J Cell Biol , vol.180 , pp. 1061-1064
    • Pederson, T.1
  • 65
    • 44149092116 scopus 로고    scopus 로고
    • Actin: Its cumbersome pilgrimage through cellular compartments
    • Schleicher M and Jockusch BM: Actin: its cumbersome pilgrimage through cellular compartments. Histochem Cell Biol 129: 695-704, 2008.
    • (2008) Histochem Cell Biol , vol.129 , pp. 695-704
    • Schleicher, M.1    Jockusch, B.M.2
  • 67
    • 0038303229 scopus 로고    scopus 로고
    • Stable and controllable RNA interference: Investigating the physiological function of glutathionylated actin
    • Wang J, Tekle E, Oubrahim H, Mieyal JJ, Stadtman ER and Chock PB: Stable and controllable RNA interference: investigating the physiological function of glutathionylated actin. Proc Natl Acad Sci USA 100: 5103-5106, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5103-5106
    • Wang, J.1    Tekle, E.2    Oubrahim, H.3    Mieyal, J.J.4    Stadtman, E.R.5    Chock, P.B.6
  • 68
    • 0037423394 scopus 로고    scopus 로고
    • Nitric oxidedependent generation of reactive species in sickle cell disease. Actin tyrosine induces defective cytoskeletal polymerization
    • Aslan M, Ryan TM, Townes TM, Coward L, Kirk MC, Barnes S, Alexander CB, Rosenfeld SS and Freeman BA: Nitric oxidedependent generation of reactive species in sickle cell disease. Actin tyrosine induces defective cytoskeletal polymerization. J Biol Chem 278: 4194-4204, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 4194-4204
    • Aslan, M.1    Ryan, T.M.2    Townes, T.M.3    Coward, L.4    Kirk, M.C.5    Barnes, S.6    Alexander, C.B.7    Rosenfeld, S.S.8    Freeman, B.A.9
  • 69
    • 44849124566 scopus 로고    scopus 로고
    • Actin S-nitrosylation inhibits neutrophil beta2 integrin function
    • Thom SR, Bhopale VM, Mancini DJ and Milovanova TN: Actin S-nitrosylation inhibits neutrophil beta2 integrin function. J Biol Chem 283: 10822-10834, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 10822-10834
    • Thom, S.R.1    Bhopale, V.M.2    Mancini, D.J.3    Milovanova, T.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.