메뉴 건너뛰기




Volumn 95, Issue 5, 2005, Pages 1042-1056

Compartmentalization of hnRNP-K during cell cycle progression and its interaction with calponin in the cytoplasm

Author keywords

2D gel electrophoresis; Cycloheximide; ERK1 2; Isoforms; K protein; Protein partners; Smooth muscle

Indexed keywords

CALPONIN; CYCLOHEXIMIDE; HETEROGENOUS NUCLEAR RIBONUCLEOPROTEIN COMPLEX K PROTEIN; ISOPROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG;

EID: 26444568259     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcb.20486     Document Type: Article
Times cited : (24)

References (57)
  • 2
  • 3
    • 0033105787 scopus 로고    scopus 로고
    • Binding of hnRNP H to an exonic splicing silencer is involved in the regulation of alternative splicing of the rat beta-tropomyosin gene
    • Chen C, Kobayashi R, Helfman D. 1999. Binding of hnRNP H to an exonic splicing silencer is involved in the regulation of alternative splicing of the rat beta-tropomyosin gene. Genes Dev 13:593-606.
    • (1999) Genes Dev , vol.13 , pp. 593-606
    • Chen, C.1    Kobayashi, R.2    Helfman, D.3
  • 4
    • 0022454143 scopus 로고
    • Acute effects of angioplasty on vascular smooth muscle
    • Consigny P, Tulenko T, Nicosia R. 1986. Acute effects of angioplasty on vascular smooth muscle. Arteriosclerosis 6:265-276.
    • (1986) Arteriosclerosis , vol.6 , pp. 265-276
    • Consigny, P.1    Tulenko, T.2    Nicosia, R.3
  • 5
    • 2542477014 scopus 로고    scopus 로고
    • RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers
    • de Hoog CL, Foster LJ, Mann M. 2004. RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers. Cell 117:649-662.
    • (2004) Cell , vol.117 , pp. 649-662
    • Hoog, C.L.1    Foster, L.J.2    Mann, M.3
  • 6
    • 0028216121 scopus 로고
    • Identification, molecular cloning, expression, and chromosome mapping of a family of transformation upregulated hnRNP-K proteins derived by alternative splicing
    • Dejgaard K, Leffers H, Rasmussen HH, Madssen P, Kruse TA, Cesser B, Nielsen H, E CJ. 1994. Identification, molecular cloning, expression, and chromosome mapping of a family of transformation upregulated hnRNP-K proteins derived by alternative splicing. J Mol Biol 236:33-48.
    • (1994) J Mol Biol , vol.236 , pp. 33-48
    • Dejgaard, K.1    Leffers, H.2    Rasmussen, H.H.3    Madssen, P.4    Kruse, T.A.5    Cesser, B.6    Nielsen, H.7
  • 7
    • 0029926495 scopus 로고    scopus 로고
    • Zik1, transcriptional represser that interacts with the heterogeneous nuclear ribonucleoprotein particle K protein
    • Denisenko O, O'Neill B, Ostrowski J, Van Seuningen I, Bomsztyk K. 1996. Zik1, transcriptional represser that interacts with the heterogeneous nuclear ribonucleoprotein particle K protein. J Biol Chem 271:27701-27706.
    • (1996) J Biol Chem , vol.271 , pp. 27701-27706
    • Denisenko, O.1    O'Neill, B.2    Ostrowski, J.3    Van Seuningen, I.4    Bomsztyk, K.5
  • 8
    • 0032584731 scopus 로고    scopus 로고
    • Differential effects of heterogeneous nuclear ribonucleoprotein K on Sp1- and Sp3-mediated transcriptional activation of a neuronal nicotinic acetylcholine receptor promoter
    • Du Q, Melnikova I, Gardner P. 1998. Differential effects of heterogeneous nuclear ribonucleoprotein K on Sp1- and Sp3-mediated transcriptional activation of a neuronal nicotinic acetylcholine receptor promoter. J Biol Chem 273:19877-19883.
    • (1998) J Biol Chem , vol.273 , pp. 19877-19883
    • Du, Q.1    Melnikova, I.2    Gardner, P.3
  • 9
    • 0037053297 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein (hnRNP) K is a component of an intronic splicing enhancer complex that activates the splicing of the alternative exon 6A from chicken b-tropomyosin pre-mRNA
    • Expert-Bezancon A, Le Caer J, Marie J. 2002. Heterogeneous nuclear ribonucleoprotein (hnRNP) K is a component of an intronic splicing enhancer complex that activates the splicing of the alternative exon 6A from chicken b-tropomyosin pre-mRNA. J Biol Chem 277:16614-16623.
    • (2002) J Biol Chem , vol.277 , pp. 16614-16623
    • Expert-Bezancon, A.1    Le Caer, J.2    Marie, J.3
  • 10
    • 0032520936 scopus 로고    scopus 로고
    • Critical analysis of coronary artery bypass graft surgery: A 30 year journey
    • Favaloro R. 1998. Critical analysis of coronary artery bypass graft surgery: A 30 year journey. J Am Coll Cardiol 31:1B-63B.
    • (1998) J Am Coll Cardiol , vol.31
    • Favaloro, R.1
  • 11
    • 0029055767 scopus 로고
    • Analysis of the hormone-dependent regulation of a JunD-estrogen receptor chimera
    • Francis MK, Phinney DG, Ryder K. 1995. Analysis of the hormone-dependent regulation of a JunD-estrogen receptor chimera. J Biol Chem 270:11052-11513.
    • (1995) J Biol Chem , vol.270 , pp. 11052-11513
    • Francis, M.K.1    Phinney, D.G.2    Ryder, K.3
  • 12
    • 0036739920 scopus 로고    scopus 로고
    • Progression of atheroma: A struggle between death and procreation
    • Geng Y, Libby P. 2002. Progression of atheroma: A struggle between death and procreation. Arterioscler Thromb Vasc Biol 22:1370-1380.
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , pp. 1370-1380
    • Geng, Y.1    Libby, P.2
  • 13
    • 0030970597 scopus 로고    scopus 로고
    • Predictors of graft patency 3 years after coronary bypass graft surgery
    • Goldman S, et al. 1997. Predictors of graft patency 3 years after coronary bypass graft surgery. J Am Coll Cardiol 29:1563-1568.
    • (1997) J Am Coll Cardiol , vol.29 , pp. 1563-1568
    • Goldman, S.1
  • 14
    • 0346230952 scopus 로고    scopus 로고
    • Two-dimensional PAGE using carrier ampholyte pH gradients in the first dimension
    • Walker J, editor. Totowa, New Jersey: Humana Press, Inc.
    • Gravel P, Golaz O. 1996. Two-dimensional PAGE using carrier ampholyte pH gradients in the first dimension. In: Walker J, editor. The Protein Protocols Handbook. Totowa, New Jersey: Humana Press, Inc. pp 127-142.
    • (1996) The Protein Protocols Handbook , pp. 127-142
    • Gravel, P.1    Golaz, O.2
  • 15
    • 0035947671 scopus 로고    scopus 로고
    • Identification of new JNK substrate using ATP pocket mutant JNK and a corresponding ATP analogue
    • Habelhah H, Shah K, Huang L, Burlingame A, Shokat K, Ronai Z. 2001a. Identification of new JNK substrate using ATP pocket mutant JNK and a corresponding ATP analogue. J Biol Chem 276:18090-18095.
    • (2001) J Biol Chem , vol.276 , pp. 18090-18095
    • Habelhah, H.1    Shah, K.2    Huang, L.3    Burlingame, A.4    Shokat, K.5    Ronai, Z.6
  • 18
    • 1842868514 scopus 로고    scopus 로고
    • Proteomic analysis of stable protein methylation in lymphoblastoid cells
    • Huang H, Tam M, Tam T, Chen D, Hsieh M, Li C. 2002. Proteomic analysis of stable protein methylation in lymphoblastoid cells. J Biochem 132:813-818.
    • (2002) J Biochem , vol.132 , pp. 813-818
    • Huang, H.1    Tam, M.2    Tam, T.3    Chen, D.4    Hsieh, M.5    Li, C.6
  • 19
    • 0037219006 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc in a cell cycle phase-dependent manner
    • Kim J, Paek K, Choi K, Kim T, Hahm B, Kim K, Jang S. 2003. Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc in a cell cycle phase-dependent manner. Mol Cell Biol 23:708-720.
    • (2003) Mol Cell Biol , vol.23 , pp. 708-720
    • Kim, J.1    Paek, K.2    Choi, K.3    Kim, T.4    Hahm, B.5    Kim, K.6    Jang, S.7
  • 20
    • 2442477755 scopus 로고    scopus 로고
    • Heterogenous nuclear ribonucleoprotein K interacts with and is proteolyzed by calpain in vivo
    • Kimura E, Abe K, Suzuki K, Sorimachi H. 2003. Heterogenous nuclear ribonucleoprotein K interacts with and is proteolyzed by calpain in vivo. Biosci Biotechnol Biochem 67:1786-1796.
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 1786-1796
    • Kimura, E.1    Abe, K.2    Suzuki, K.3    Sorimachi, H.4
  • 22
    • 0037378607 scopus 로고    scopus 로고
    • CK2 protein kinase is stimulated and redistributed by functional herpes simplex virus ICP27 protein
    • Koffa M, Kean J, Zachos G, Rice S, Clements J. 2003. CK2 protein kinase is stimulated and redistributed by functional herpes simplex virus ICP27 protein. J Virol 77:4315-4325.
    • (2003) J Virol , vol.77 , pp. 4315-4325
    • Koffa, M.1    Kean, J.2    Zachos, G.3    Rice, S.4    Clements, J.5
  • 23
    • 0033526807 scopus 로고    scopus 로고
    • Expression of the heterogeneous nuclear ribonucleoprotein complex K protein and the prolyl-4-hydroxylase a-subunit in atherosclerotic arterial smooth muscle cells
    • Laury-Kleintop LD, Gleason M, Tulenko TN. 1999. Expression of the heterogeneous nuclear ribonucleoprotein complex K protein and the prolyl-4-hydroxylase a-subunit in atherosclerotic arterial smooth muscle cells. Biochem Biophys Res Comm 260:382-389.
    • (1999) Biochem Biophys Res Comm , vol.260 , pp. 382-389
    • Laury-Kleintop, L.D.1    Gleason, M.2    Tulenko, T.N.3
  • 24
    • 0029671095 scopus 로고    scopus 로고
    • trans-Activation by the hnRNP-K protein involves and increase in RNA synthesis from the reporter genes
    • Lee MH, Mori S, Raychaudhuri P. 1996. trans-Activation by the hnRNP-K protein involves and increase in RNA synthesis from the reporter genes. J Biol Chem 271:3420-3427.
    • (1996) J Biol Chem , vol.271 , pp. 3420-3427
    • Lee, M.H.1    Mori, S.2    Raychaudhuri, P.3
  • 25
    • 0033571710 scopus 로고    scopus 로고
    • Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of antin-binding proteins
    • Leinweber B, Leavis P, Grabarek Z, Wang C, Morgan K. 1999. Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of antin-binding proteins. Biochem J 344:117-123.
    • (1999) Biochem J , vol.344 , pp. 117-123
    • Leinweber, B.1    Leavis, P.2    Grabarek, Z.3    Wang, C.4    Morgan, K.5
  • 26
    • 0034971252 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein-H plays a suppressive role in visceral myogenesis
    • Liu J, Beqaj S, Yang Y, Honore B, Schuger L. 2001. Heterogeneous nuclear ribonucleoprotein-H plays a suppressive role in visceral myogenesis. Mech Dev 104:79-87.
    • (2001) Mech Dev , vol.104 , pp. 79-87
    • Liu, J.1    Beqaj, S.2    Yang, Y.3    Honore, B.4    Schuger, L.5
  • 28
    • 0026515523 scopus 로고
    • Characterization and primary structure of the poly (C)-binding heterogeneous nuclear riboprotein complex K protein
    • Matunis M, Michael WM, Dreyfuss G. 1992. Characterization and primary structure of the poly (C)-binding heterogeneous nuclear riboprotein complex K protein. Molec and Cell Biol 12:164-171.
    • (1992) Molec and Cell Biol , vol.12 , pp. 164-171
    • Matunis, M.1    Michael, W.M.2    Dreyfuss, G.3
  • 29
    • 0030868556 scopus 로고    scopus 로고
    • Calponin and mitogen-activated protein kinasae signaling in differentiated vascular smooth muscle
    • Menice C, Hulvershorn J, Adam L, Wang C-L, Morgan K. 1997. Calponin and mitogen-activated protein kinasae signaling in differentiated vascular smooth muscle. J Biol Chem 272:25157-25161.
    • (1997) J Biol Chem , vol.272 , pp. 25157-25161
    • Menice, C.1    Hulvershorn, J.2    Adam, L.3    Wang, C.-L.4    Morgan, K.5
  • 30
    • 0032562765 scopus 로고    scopus 로고
    • Identification of heterogeneous nuclear ribonucleoprotein K (hnRNP K) as a represser of C/EBPb-mediated gene activation
    • Miau L, Chang C, Shen B, Tsai W, Lee S. 1998. Identification of heterogeneous nuclear ribonucleoprotein K (hnRNP K) as a represser of C/EBPb-mediated gene activation. J Biol Chem 273:10784-10791.
    • (1998) J Biol Chem , vol.273 , pp. 10784-10791
    • Miau, L.1    Chang, C.2    Shen, B.3    Tsai, W.4    Lee, S.5
  • 31
    • 0030978415 scopus 로고    scopus 로고
    • The K nuclear shuttling domain: A novel signal for nuclear import and nuclear export in the hnRNP K protein
    • Micheal W, Eder P, Dreyfuss G. 1997. The K nuclear shuttling domain: A novel signal for nuclear import and nuclear export in the hnRNP K protein. EMBO J 16:3587-3598.
    • (1997) EMBO J , vol.16 , pp. 3587-3598
    • Micheal, W.1    Eder, P.2    Dreyfuss, G.3
  • 33
    • 0034921574 scopus 로고    scopus 로고
    • Signal transduction in smooth muscle. Invited review: Cross-bridge regulation by thin filament-associated proteins
    • Morgan K, Gangopadhyay S. 2001. Signal transduction in smooth muscle. Invited review: Cross-bridge regulation by thin filament-associated proteins. J Appl Physiol 91:953-962.
    • (2001) J Appl Physiol , vol.91 , pp. 953-962
    • Morgan, K.1    Gangopadhyay, S.2
  • 34
    • 0034553833 scopus 로고    scopus 로고
    • Considerations in developing successful, population-based molecular screening and prevention of lung cancer
    • Mulshine J, De Luca L, Dedrick R, Tockman M, Webster R, Placke M. 2000. Considerations in developing successful, population-based molecular screening and prevention of lung cancer. Cancer 89:2465-2467.
    • (2000) Cancer , vol.89 , pp. 2465-2467
    • Mulshine, J.1    De Luca, L.2    Dedrick, R.3    Tockman, M.4    Webster, R.5    Placke, M.6
  • 37
    • 0242490528 scopus 로고    scopus 로고
    • Nuclear shift of hnRNP K protein in neoplasms and other states of enhanced cell proliferation
    • Ostrowski J, Bomsztyk K. 2003. Nuclear shift of hnRNP K protein in neoplasms and other states of enhanced cell proliferation. Br J Cancer 89:1493-1501.
    • (2003) Br J Cancer , vol.89 , pp. 1493-1501
    • Ostrowski, J.1    Bomsztyk, K.2
  • 38
    • 0034603039 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation in the regulation of the interaction of heterogenous nuclear riboprotein K protein with its protein and RNA partners
    • Ostrowski J, Schullery D, Denisenko O, Higaki Y, Watts J, Aebersold R, Stempka L, Gschwendt M, Bomsztyk K. 2000. Role of tyrosine phosphorylation in the regulation of the interaction of heterogenous nuclear riboprotein K protein with its protein and RNA partners. J Biol Chem 275:3619-3628.
    • (2000) J Biol Chem , vol.275 , pp. 3619-3628
    • Ostrowski, J.1    Schullery, D.2    Denisenko, O.3    Higaki, Y.4    Watts, J.5    Aebersold, R.6    Stempka, L.7    Gschwendt, M.8    Bomsztyk, K.9
  • 39
    • 0037155164 scopus 로고    scopus 로고
    • Hetergenous nuclear ribonucleoprotein K protein associates with multiple mitochondrial transcripts within the organelle
    • Ostrowski J, Wyrwicz L, Rychlewski L, Bomsztyk K. 2002. Hetergenous nuclear ribonucleoprotein K protein associates with multiple mitochondrial transcripts within the organelle. J Biol Chem 277:6303-6310.
    • (2002) J Biol Chem , vol.277 , pp. 6303-6310
    • Ostrowski, J.1    Wyrwicz, L.2    Rychlewski, L.3    Bomsztyk, K.4
  • 41
    • 0022591979 scopus 로고
    • The pathogenesis of atherosclerosis - An update
    • Ross R. 1986. The pathogenesis of atherosclerosis-an update. N Engl J Med 314:488-500.
    • (1986) N Engl J Med , vol.314 , pp. 488-500
    • Ross, R.1
  • 42
    • 0025350739 scopus 로고
    • Localization of PDGF-B protein in macrophages in all phases of atherogenesis
    • Ross R, Masuda J, Raines EW, et al. 1990. Localization of PDGF-B protein in macrophages in all phases of atherogenesis. Science 248:1009-1012.
    • (1990) Science , vol.248 , pp. 1009-1012
    • Ross, R.1    Masuda, J.2    Raines, E.W.3
  • 43
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells
    • Schreiber E, Matthias P, Muller M, Schaffner W. 1989. Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells. Nucl Acid Res 17:6419.
    • (1989) Nucl Acid Res , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.3    Schaffner, W.4
  • 45
    • 0033555522 scopus 로고    scopus 로고
    • Regulation of human vascular endothelial growth factor mRNA stability in hypoxia by heterogeneous nuclear ribonucleoprotein L
    • Shih S, Claffey K. 1999. Regulation of human vascular endothelial growth factor mRNA stability in hypoxia by heterogeneous nuclear ribonucleoprotein L. J Biol Chem 274:1359-1365.
    • (1999) J Biol Chem , vol.274 , pp. 1359-1365
    • Shih, S.1    Claffey, K.2
  • 46
    • 0034686029 scopus 로고    scopus 로고
    • Interaction of two multifunctional proteins: Heterogeneous nuclear ribonucleoprotein K and Y-box-binding protein
    • Shnyreva M, Schullery D, Suzuki H, Higaki Y, Bomsztyk K. 2000. Interaction of two multifunctional proteins: Heterogeneous nuclear ribonucleoprotein K and Y-box-binding protein. J Biol Chem 275:15498-15503.
    • (2000) J Biol Chem , vol.275 , pp. 15498-15503
    • Shnyreva, M.1    Schullery, D.2    Suzuki, H.3    Higaki, Y.4    Bomsztyk, K.5
  • 47
    • 0037423817 scopus 로고    scopus 로고
    • Posttranscriptional control of renin synthesis. Identification of proteins interacting with renin mRNA 3′-untranslated region
    • Skalweit A, Doller A, Huth A, Katme T, Persson P, Thiele B. 2003. Posttranscriptional control of renin synthesis. Identification of proteins interacting with renin mRNA 3′-untranslated region. Circ Res 92:419-427.
    • (2003) Circ Res , vol.92 , pp. 419-427
    • Skalweit, A.1    Doller, A.2    Huth, A.3    Katme, T.4    Persson, P.5    Thiele, B.6
  • 48
    • 0035873882 scopus 로고    scopus 로고
    • Cell cycle in vasculoproliferative diseases: Potential inteventions and routes of delivery
    • Sriram V, Patterson C. 2001. Cell cycle in vasculoproliferative diseases: Potential inteventions and routes of delivery. Circulation 103:2414-2419.
    • (2001) Circulation , vol.103 , pp. 2414-2419
    • Sriram, V.1    Patterson, C.2
  • 49
    • 0037013303 scopus 로고    scopus 로고
    • Rapid phosphorylation of heterogeneous nuclear ribonucleoprotein C1/C2 in response to physiologic levels of hydrogen peroxide in human endothelial cells
    • Stone J, Collins T. 2002. Rapid phosphorylation of heterogeneous nuclear ribonucleoprotein C1/C2 in response to physiologic levels of hydrogen peroxide in human endothelial cells. J Biol Chem 277:15621-15628.
    • (2002) J Biol Chem , vol.277 , pp. 15621-15628
    • Stone, J.1    Collins, T.2
  • 50
    • 0037432070 scopus 로고    scopus 로고
    • Basal and hydrogen peroxide stimulated sites of phosphorylation in heterogeneous nuclear ribonucleoprotein C1/C2
    • Stone J, Maki J, Collins T. 2003. Basal and hydrogen peroxide stimulated sites of phosphorylation in heterogeneous nuclear ribonucleoprotein C1/C2. Biochemistry 42:1301-1308.
    • (2003) Biochemistry , vol.42 , pp. 1301-1308
    • Stone, J.1    Maki, J.2    Collins, T.3
  • 51
    • 0027182876 scopus 로고
    • Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter, in vitro
    • Takimoto M, Tomonaga T, Matunis M, Avigan M, Krutzsch H, Dreyfuss G, Levens D. 1993. Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter, in vitro. J Biol Chem 268:18249-18258.
    • (1993) J Biol Chem , vol.268 , pp. 18249-18258
    • Takimoto, M.1    Tomonaga, T.2    Matunis, M.3    Avigan, M.4    Krutzsch, H.5    Dreyfuss, G.6    Levens, D.7
  • 52
    • 0033105845 scopus 로고    scopus 로고
    • Hetergeneous nuclear ribonucleoprotein DOB is a asequence-specific DNA-binding protein
    • Tolnay M, Vereshchagina L, Tsokos G. 1999. Hetergeneous nuclear ribonucleoprotein DOB is a asequence-specific DNA-binding protein. Biochem J 338:417-425.
    • (1999) Biochem J , vol.338 , pp. 417-425
    • Tolnay, M.1    Vereshchagina, L.2    Tsokos, G.3
  • 53
    • 0036534730 scopus 로고    scopus 로고
    • Protein kinase A enhances, whereas glycogen sythase kinase-3b inhibits, the activity of the exon 2-encoded transactivator domain of heterogeneous nuclear ribonucleoprotein D in a hierarchical fashion
    • Tolnay M, Juang Y, Tsokos G. 2002. Protein kinase A enhances, whereas glycogen sythase kinase-3b inhibits, the activity of the exon 2-encoded transactivator domain of heterogeneous nuclear ribonucleoprotein D in a hierarchical fashion. Biochem J 363:127-136.
    • (2002) Biochem J , vol.363 , pp. 127-136
    • Tolnay, M.1    Juang, Y.2    Tsokos, G.3
  • 54
    • 0028834524 scopus 로고
    • The K protein domain that recruits the Interleukin 1-responsive K protein kinase lies adjacent to a cluster of c-Src and Vav SH3-binding sites
    • Van Seuningen I, Ostrowski J, Bustelo X, Sleath P, Bomsztyk K. 1995. The K protein domain that recruits the Interleukin 1-responsive K protein kinase lies adjacent to a cluster of c-Src and Vav SH3-binding sites. J Biol Chem 270:26976-26985.
    • (1995) J Biol Chem , vol.270 , pp. 26976-26985
    • Van Seuningen, I.1    Ostrowski, J.2    Bustelo, X.3    Sleath, P.4    Bomsztyk, K.5
  • 55
    • 0020530724 scopus 로고
    • A detergent-trypsin method for the preparation of nuclei for flow cytometric DNA analysis
    • Vindelov L, Christensen I, Nissen N. 1983. A detergent-trypsin method for the preparation of nuclei for flow cytometric DNA analysis. Cytometry 3:323-327.
    • (1983) Cytometry , vol.3 , pp. 323-327
    • Vindelov, L.1    Christensen, I.2    Nissen, N.3
  • 56
    • 0037135695 scopus 로고    scopus 로고
    • Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy
    • Wada K, Inoue K, Hagiwara M. 2002. Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy. Biochim Biophys Acta 1591:1-10.
    • (2002) Biochim Biophys Acta , vol.1591 , pp. 1-10
    • Wada, K.1    Inoue, K.2    Hagiwara, M.3
  • 57
    • 0032878244 scopus 로고    scopus 로고
    • The multifunctional herpes simplex virus IE63 protein interacts with heterogenous ribonucleoprotein K and with casein kinase 2
    • Wadd S, Bryant H, Filhol O, Scott J, Hsieh T-Y, Everett R, Clements J. 1999. The multifunctional herpes simplex virus IE63 protein interacts with heterogenous ribonucleoprotein K and with casein kinase 2. J Biol Chem 274:28991-28998.
    • (1999) J Biol Chem , vol.274 , pp. 28991-28998
    • Wadd, S.1    Bryant, H.2    Filhol, O.3    Scott, J.4    Hsieh, T.-Y.5    Everett, R.6    Clements, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.