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Volumn 9, Issue 23, 2009, Pages 5267-5287

Identification and characterization of novel ERC-55 interacting proteins: Evidence for the existence of several ERC-55 splicing variants; including the cytosolic ERC-55-C

Author keywords

Cell biology; CREC protein; Cytosol; Endoplasmic reticulum; ERC 55 variants; Protein protein interaction

Indexed keywords

CALCYCLIN; ENDOPLASMIC RETICULUM CALCIUM BINDING PROTEIN OF 55KDA; PROTEIN S 100; UNCLASSIFIED DRUG;

EID: 73249116586     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200900321     Document Type: Article
Times cited : (17)

References (94)
  • 1
    • 65249104606 scopus 로고    scopus 로고
    • The rapidly expanding CREC protein family: Members, localization, function, and role in disease
    • Honoré, B., The rapidly expanding CREC protein family: members, localization, function, and role in disease. Bioessays 2009, 31, 262-277.
    • (2009) Bioessays , vol.31 , pp. 262-277
    • Honoré, B.1
  • 2
    • 0033978227 scopus 로고    scopus 로고
    • 2+-binding proteins localised to the secretory pathway of mammalian cells
    • 2+-binding proteins localised to the secretory pathway of mammalian cells. FEBS Lett. 2000, 466, 11-18.
    • (2000) FEBS Lett , vol.466 , pp. 11-18
    • Honoré, B.1    Vorum, H.2
  • 3
    • 0027439695 scopus 로고    scopus 로고
    • 2+-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL sequence. J. Biol. Chem. 1993, 268, 699-705.
    • 2+-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL sequence. J. Biol. Chem. 1993, 268, 699-705.
  • 4
    • 0028339802 scopus 로고
    • The endoplasmic reticulum calcium-binding protein of 55 kDa is a novel EF-hand protein retained in the endoplasmic reticulum by a carboxyl-terminal His-Asp-Glu-Leu motif
    • Weis, K., Griffiths, G., Lamond, A. I., The endoplasmic reticulum calcium-binding protein of 55 kDa is a novel EF-hand protein retained in the endoplasmic reticulum by a carboxyl-terminal His-Asp-Glu-Leu motif. J. Biol. Chem. 1994, 269, 19142-19150.
    • (1994) J. Biol. Chem , vol.269 , pp. 19142-19150
    • Weis, K.1    Griffiths, G.2    Lamond, A.I.3
  • 5
    • 33646772541 scopus 로고    scopus 로고
    • A proteomic approach reveals transient association of reticulocalbin-3, a novel member of the CREC family, with the precursor of subtilisin-like proprotein convertase, PACE4
    • Tsuji, A., Kikuchi, Y., Sato, Y., Koide, S. et al. A proteomic approach reveals transient association of reticulocalbin-3, a novel member of the CREC family, with the precursor of subtilisin-like proprotein convertase, PACE4. Biochem. J. 2006, 396, 51-59.
    • (2006) Biochem. J , vol.396 , pp. 51-59
    • Tsuji, A.1    Kikuchi, Y.2    Sato, Y.3    Koide, S.4
  • 8
    • 34347384891 scopus 로고    scopus 로고
    • A cytosolic splice variant of Cab45 interacts with Munc18b and impacts on amylase secretion by pancreatic acini
    • Lam, P. P., Hyvarinen, K., Kauppi, M., Cosen-Binker, L. et al. A cytosolic splice variant of Cab45 interacts with Munc18b and impacts on amylase secretion by pancreatic acini. Mol. Biol. Cell 2007, 18, 2473-2480.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2473-2480
    • Lam, P.P.1    Hyvarinen, K.2    Kauppi, M.3    Cosen-Binker, L.4
  • 9
    • 0030610583 scopus 로고    scopus 로고
    • 2+-binding protein retained in the endoplasmic reticulum with a novel carboxyl-terminal sequence, HDEF. J. Biol. Chem. 1997, 272, 18232-18239.
    • 2+-binding protein retained in the endoplasmic reticulum with a novel carboxyl-terminal sequence, HDEF. J. Biol. Chem. 1997, 272, 18232-18239.
  • 11
    • 0033134009 scopus 로고    scopus 로고
    • Human calumenin localizes to the secretory pathway and is secreted to the medium
    • Vorum, H., Hager, H., Christensen, B. M., Nielsen, S., Honoré, B., Human calumenin localizes to the secretory pathway and is secreted to the medium. Exp. Cell Res. 1999, 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    Honoré, B.5
  • 12
    • 0032979150 scopus 로고    scopus 로고
    • a new calcium-binding protein that is also a binding protein for crotoxin, a neurotoxic phospholipase A2
    • Hseu, M. J., Yen, C. H., Tzeng, M. C., Crocalbin: a new calcium-binding protein that is also a binding protein for crotoxin, a neurotoxic phospholipase A2. FEBS Lett. 1999, 445, 440-444.
    • (1999) FEBS Lett , vol.445 , pp. 440-444
    • Hseu, M.J.1    Yen, C.H.2    Tzeng, M.3    Crocalbin, C.4
  • 13
    • 49049101293 scopus 로고    scopus 로고
    • Novel surface expression of reticulocalbin 1 on bone endothelial cells and human prostate cancer cells is regulated by TNF-alpha
    • Cooper, C. R., Graves, B., Pruitt, F., Chaib, H. et al. Novel surface expression of reticulocalbin 1 on bone endothelial cells and human prostate cancer cells is regulated by TNF-alpha. J. Cell. Biochem. 2008, 104, 2298-2309.
    • (2008) J. Cell. Biochem , vol.104 , pp. 2298-2309
    • Cooper, C.R.1    Graves, B.2    Pruitt, F.3    Chaib, H.4
  • 14
    • 0035515246 scopus 로고    scopus 로고
    • A molecular mechanism for genetic warfarin resistance in the rat
    • Wallin, R., Hutson, S. M., Cain, D., Sweatt, A., Sane, D. C., A molecular mechanism for genetic warfarin resistance in the rat. FASEB J. 2001, 15, 2542-2544.
    • (2001) FASEB J , vol.15 , pp. 2542-2544
    • Wallin, R.1    Hutson, S.M.2    Cain, D.3    Sweatt, A.4    Sane, D.C.5
  • 15
    • 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, D. C., Hutson, S. M., Wallin, R., The inhibitory effect of calumenin on the vitamin K-dependent gamma-carboxylation system. Characterization of the system in normal and warfarin-resistant rats. J. Biol. Chem. 2004, 279, 25276-25283.
    • (2004) J. Biol. Chem , vol.279 , pp. 25276-25283
    • Wajih, N.1    Sane, D.C.2    Hutson, S.M.3    Wallin, R.4
  • 16
    • 33645108259 scopus 로고    scopus 로고
    • 2+-binding protein, interacts with ryanodine receptor-1 in rabbit skeletal sarcoplasmic reticulum
    • 2+-binding protein, interacts with ryanodine receptor-1 in rabbit skeletal sarcoplasmic reticulum. Biochem. Biophys. Res. Commun. 2006, 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
  • 17
    • 55249113945 scopus 로고    scopus 로고
    • Calumenin interacts with SERCA2 in rat cardiac sarcoplasmic reticulum
    • Sahoo, S. K., Kim do, H., Calumenin interacts with SERCA2 in rat cardiac sarcoplasmic reticulum. Mol. Cells 2008, 26, 265-269.
    • (2008) Mol. Cells , vol.26 , pp. 265-269
    • Sahoo, S.K.1    Kim do, H.2
  • 18
    • 30044442791 scopus 로고    scopus 로고
    • Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes
    • Kimura, K., Wakamatsu, A., Suzuki, Y., Ota, T. et al. Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. Genome Res. 2006, 16, 55-65.
    • (2006) Genome Res , vol.16 , pp. 55-65
    • Kimura, K.1    Wakamatsu, A.2    Suzuki, Y.3    Ota, T.4
  • 19
    • 34447636585 scopus 로고    scopus 로고
    • The genetic interaction between VKORC1 c1173t and calumenin a29809g modulates the anticoagulant response of acenocoumarol
    • Gonzalez-Conejero, R., Corral, J., Roldan, V., Ferrer, F. et al. The genetic interaction between VKORC1 c1173t and calumenin a29809g modulates the anticoagulant response of acenocoumarol. J. Thromb. Haemost. 2007, 5, 1701-1706.
    • (2007) J. Thromb. Haemost , vol.5 , pp. 1701-1706
    • Gonzalez-Conejero, R.1    Corral, J.2    Roldan, V.3    Ferrer, F.4
  • 20
    • 0029048405 scopus 로고
    • Interaction of papillomavirus E6 oncoproteins with a putative calcium-binding protein
    • Chen, J. J., Reid, C. E., Band, V., Androphy, E. J., Interaction of papillomavirus E6 oncoproteins with a putative calcium-binding protein. Science 1995, 269, 529-531.
    • (1995) Science , vol.269 , pp. 529-531
    • Chen, J.J.1    Reid, C.E.2    Band, V.3    Androphy, E.J.4
  • 21
    • 33947246003 scopus 로고    scopus 로고
    • Differentially expressed genes between high-risk human papillomavirus types in human cervical cancer cells
    • Vazquez-Ortiz, G., Garcia, J. A., Ciudad, C. J., Noe, V. et al. Differentially expressed genes between high-risk human papillomavirus types in human cervical cancer cells. Int. J. Gynecol. Cancer 2007, 17, 484-491.
    • (2007) Int. J. Gynecol. Cancer , vol.17 , pp. 484-491
    • Vazquez-Ortiz, G.1    Garcia, J.A.2    Ciudad, C.J.3    Noe, V.4
  • 22
    • 33947323154 scopus 로고    scopus 로고
    • An integrated approach of immunogenomics and bioinformatics to identify new Tumor Associated Antigens (TAA) for mammary cancer immunological prevention
    • Cavallo, F., Astolfi, A., Iezzi, M., Cordero, F. et al. An integrated approach of immunogenomics and bioinformatics to identify new Tumor Associated Antigens (TAA) for mammary cancer immunological prevention. BMC Bioinformatics 2005, 6 (Suppl 4), S7.
    • (2005) BMC Bioinformatics , vol.6 , Issue.SUPPL. 4
    • Cavallo, F.1    Astolfi, A.2    Iezzi, M.3    Cordero, F.4
  • 23
    • 0031589150 scopus 로고    scopus 로고
    • ERC-55, a binding protein for the papilloma virus E6 onco-protein, specifically interacts with vitamin D receptor among nuclear receptors
    • Imai, T., Matsuda, K., Shimojima, T., Hashimoto, T. et al. ERC-55, a binding protein for the papilloma virus E6 onco-protein, specifically interacts with vitamin D receptor among nuclear receptors. Biochem. Biophys. Res. Commun. 1997, 233, 765-769.
    • (1997) Biochem. Biophys. Res. Commun , vol.233 , pp. 765-769
    • Imai, T.1    Matsuda, K.2    Shimojima, T.3    Hashimoto, T.4
  • 24
    • 33645502295 scopus 로고    scopus 로고
    • Human mammary epithelial cells express CYP27B1 and are growth inhibited by 25-hydroxyvitamin D-3, the major circulating form of vitamin D-3
    • Kemmis, C. M., Salvador, S. M., Smith, K. M., Welsh, J., Human mammary epithelial cells express CYP27B1 and are growth inhibited by 25-hydroxyvitamin D-3, the major circulating form of vitamin D-3. J. Nutr. 2006, 136, 887-892.
    • (2006) J. Nutr , vol.136 , pp. 887-892
    • Kemmis, C.M.1    Salvador, S.M.2    Smith, K.M.3    Welsh, J.4
  • 25
    • 55649115529 scopus 로고    scopus 로고
    • Mammary epithelial cell transformation is associated with deregulation of the vitamin D pathway
    • Kemmis, C. M., Welsh, J., Mammary epithelial cell transformation is associated with deregulation of the vitamin D pathway. J. Cell. Biochem. 2008, 105, 980-988.
    • (2008) J. Cell. Biochem , vol.105 , pp. 980-988
    • Kemmis, C.M.1    Welsh, J.2
  • 26
    • 0034806436 scopus 로고    scopus 로고
    • 25-Hydroxy-vitamin d metabolism in human colon cancer cells during tumor progression
    • Bareis, P., Bises, G., Bischof, M. G., Cross, H. S., Peterlik, M., 25-Hydroxy-vitamin d metabolism in human colon cancer cells during tumor progression. Biochem. Biophys. Res. Commun. 2001, 285, 1012-1017.
    • (2001) Biochem. Biophys. Res. Commun , vol.285 , pp. 1012-1017
    • Bareis, P.1    Bises, G.2    Bischof, M.G.3    Cross, H.S.4    Peterlik, M.5
  • 27
    • 0035342721 scopus 로고    scopus 로고
    • 25-Hydroxyvitamin D(3)-1alpha-hydroxylase and vitamin D receptor gene expression in human colonic mucosa is elevated during early cancerogenesis
    • Cross, H. S., Bareis, P., Hofer, H., Bischof, M. G., 25-Hydroxyvitamin D(3)-1alpha-hydroxylase and vitamin D receptor gene expression in human colonic mucosa is elevated during early cancerogenesis. Steroids 2001, 66, 287-292.
    • (2001) Steroids , vol.66 , pp. 287-292
    • Cross, H.S.1    Bareis, P.2    Hofer, H.3    Bischof, M.G.4
  • 29
    • 51249123073 scopus 로고    scopus 로고
    • Gene expression analysis in absence epilepsy using a monozygotic twin design
    • Helbig, I., Matigian, N. A., Vadlamudi, L., Lawrence, K. M. et al. Gene expression analysis in absence epilepsy using a monozygotic twin design. Epilepsia 2008, 49, 1546-1554.
    • (2008) Epilepsia , vol.49 , pp. 1546-1554
    • Helbig, I.1    Matigian, N.A.2    Vadlamudi, L.3    Lawrence, K.M.4
  • 30
    • 0028909615 scopus 로고
    • Novel reticular calcium binding protein is purified on taipoxin columns
    • Dodds, D., Schlimgen, A. K., Lu, S. Y., Perin, M. S., Novel reticular calcium binding protein is purified on taipoxin columns. J. Neurochem. 1995, 64, 2339-2344.
    • (1995) J. Neurochem , vol.64 , pp. 2339-2344
    • Dodds, D.1    Schlimgen, A.K.2    Lu, S.Y.3    Perin, M.S.4
  • 31
    • 0030851784 scopus 로고    scopus 로고
    • Neuronal pentraxin receptor, a novel putative integral membrane pentraxin that interacts with neuronal pentraxin 1 and 2 and taipoxin-associated calcium-binding protein 49
    • Dodds, D. C., Omeis, I. A., Cushman, S. J., Helms, J. A., Perin, M. S., Neuronal pentraxin receptor, a novel putative integral membrane pentraxin that interacts with neuronal pentraxin 1 and 2 and taipoxin-associated calcium-binding protein 49. J. Biol. Chem. 1997, 272, 21488-21494.
    • (1997) J. Biol. Chem , vol.272 , pp. 21488-21494
    • Dodds, D.C.1    Omeis, I.A.2    Cushman, S.J.3    Helms, J.A.4    Perin, M.S.5
  • 32
    • 0034625344 scopus 로고    scopus 로고
    • Biochemical interactions of the neuronal pentraxins. Neuronal pentraxin (NP) receptor binds to taipoxin and taipoxin-associated calcium-binding protein 49 via NP1 and NP2
    • Kirkpatrick, L. L., Matzuk, M. M., Dodds, D. C., Perin, M. S., Biochemical interactions of the neuronal pentraxins. Neuronal pentraxin (NP) receptor binds to taipoxin and taipoxin-associated calcium-binding protein 49 via NP1 and NP2. J. Biol. Chem. 2000, 275, 17786-17792.
    • (2000) J. Biol. Chem , vol.275 , pp. 17786-17792
    • Kirkpatrick, L.L.1    Matzuk, M.M.2    Dodds, D.C.3    Perin, M.S.4
  • 33
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S., von Heijne, G., Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 1997, 10, 1-6.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 35
    • 0023752643 scopus 로고
    • Receptors for alpha 2-macroglobulin- and pregnancy zone protein-proteinase complexes in the human placental syncytiotrophoblast
    • Jensen, P. H., Moestrup, S. K., Sottrup-Jensen, L., Petersen, C. M., Gliemann, J., Receptors for alpha 2-macroglobulin- and pregnancy zone protein-proteinase complexes in the human placental syncytiotrophoblast. Placenta 1988, 9, 463-477.
    • (1988) Placenta , vol.9 , pp. 463-477
    • Jensen, P.H.1    Moestrup, S.K.2    Sottrup-Jensen, L.3    Petersen, C.M.4    Gliemann, J.5
  • 36
    • 1642420368 scopus 로고    scopus 로고
    • Changes in protein expression in p53 deleted spontaneous thymic lymphomas
    • Honoré, B., Vorum, H., Pedersen, A. E., Buus, S., Claësson, M. H., Changes in protein expression in p53 deleted spontaneous thymic lymphomas. Exp. Cell Res. 2004, 295, 91-101.
    • (2004) Exp. Cell Res , vol.295 , pp. 91-101
    • Honoré, B.1    Vorum, H.2    Pedersen, A.E.3    Buus, S.4    Claësson, M.H.5
  • 37
    • 33745697841 scopus 로고    scopus 로고
    • Proteomic profiling of fibroblasts reveals a modulating effect of extracellular calumenin on the organization of the actin cytoskeleton
    • Østergaard, M., Hansen, G. A., Vorum, H., Honoré, B., Proteomic profiling of fibroblasts reveals a modulating effect of extracellular calumenin on the organization of the actin cytoskeleton. Proteomics 2006, 6, 3509-3519.
    • (2006) Proteomics , vol.6 , pp. 3509-3519
    • Østergaard, M.1    Hansen, G.A.2    Vorum, H.3    Honoré, B.4
  • 38
    • 48649095492 scopus 로고    scopus 로고
    • Identification of differentially expressed proteins in spontaneous thymic lymphomas from knockout mice with deletion of p53
    • Honoré,B., Buus, S., Claësson, M. H., Identification of differentially expressed proteins in spontaneous thymic lymphomas from knockout mice with deletion of p53. Proteome Sci. 2008, 6, 18.
    • (2008) Proteome Sci , vol.6 , pp. 18
    • Honoré, B.1    Buus, S.2    Claësson, M.H.3
  • 39
    • 33845436674 scopus 로고    scopus 로고
    • BRF1 protein turnover and mRNA decay activity are regulated by protein kinase B at the same phosphorylation sites
    • Benjamin, D., Schmidlin, M., Min, L., Gross, B., Moroni, C., BRF1 protein turnover and mRNA decay activity are regulated by protein kinase B at the same phosphorylation sites. Mol. Cell. Biol. 2006, 26, 9497-9507.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 9497-9507
    • Benjamin, D.1    Schmidlin, M.2    Min, L.3    Gross, B.4    Moroni, C.5
  • 40
    • 0033662892 scopus 로고    scopus 로고
    • Immunoelectron microscopic localization of the electrogenic Na/HCO(3) cotransporter in rat and ambystoma kidney
    • Maunsbach, A. B., Vorum, H., Kwon, T. H., Nielsen, S. et al. Immunoelectron microscopic localization of the electrogenic Na/HCO(3) cotransporter in rat and ambystoma kidney. J. Am. Soc. Nephrol. 2000, 11, 2179-2189.
    • (2000) J. Am. Soc. Nephrol , vol.11 , pp. 2179-2189
    • Maunsbach, A.B.1    Vorum, H.2    Kwon, T.H.3    Nielsen, S.4
  • 41
    • 0033615527 scopus 로고    scopus 로고
    • 2+-dependent association of S100A6 (Calcyclin) with the plasma membrane and the nuclear envelope
    • 2+-dependent association of S100A6 (Calcyclin) with the plasma membrane and the nuclear envelope. J. Biol. Chem. 1999, 274, 31593-31596.
    • (1999) J. Biol. Chem , vol.274 , pp. 31593-31596
    • Stradal, T.B.1    Gimona, M.2
  • 42
    • 0024363287 scopus 로고
    • Hereditary and acquired deficiencies of C1 inhibitor
    • Davis 3rd. A. E. Hereditary and acquired deficiencies of C1 inhibitor. Immunodefic. Rev. 1989, 1, 207-226.
    • (1989) Immunodefic. Rev , vol.1 , pp. 207-226
    • Davis 3rd, A.E.1
  • 43
    • 0347623371 scopus 로고    scopus 로고
    • Genome-wide survey of human alternative pre-mRNA splicing with exon junction microarrays
    • Johnson, J. M., Castle, J., Garrett-Engele, P., Kan, Z. et al. Genome-wide survey of human alternative pre-mRNA splicing with exon junction microarrays. Science 2003, 302, 2141-2144.
    • (2003) Science , vol.302 , pp. 2141-2144
    • Johnson, J.M.1    Castle, J.2    Garrett-Engele, P.3    Kan, Z.4
  • 44
    • 46049107404 scopus 로고    scopus 로고
    • Alternative translation start sites and hidden coding potential of eukaryotic mRNAs
    • Kochetov, A. V., Alternative translation start sites and hidden coding potential of eukaryotic mRNAs. Bioessays 2008, 30, 683-691.
    • (2008) Bioessays , vol.30 , pp. 683-691
    • Kochetov, A.V.1
  • 45
    • 33745235807 scopus 로고    scopus 로고
    • Distribution and ultrastructural localization of GEC1 in the rat CNS
    • Wang, Y., Dun, S. L., Huang, P., Chen, C. et al. Distribution and ultrastructural localization of GEC1 in the rat CNS. Neuroscience 2006, 140, 1265-1276.
    • (2006) Neuroscience , vol.140 , pp. 1265-1276
    • Wang, Y.1    Dun, S.L.2    Huang, P.3    Chen, C.4
  • 46
    • 7644222590 scopus 로고    scopus 로고
    • GEC1, a protein related to GABARAP, interacts with tubulin and GABA(A) receptor
    • Mansuy, V., Boireau, W., Fraichard, A., Schlick, J. L. et al. GEC1, a protein related to GABARAP, interacts with tubulin and GABA(A) receptor. Biochem. Biophys. Res. Commun. 2004, 325, 639-648.
    • (2004) Biochem. Biophys. Res. Commun , vol.325 , pp. 639-648
    • Mansuy, V.1    Boireau, W.2    Fraichard, A.3    Schlick, J.L.4
  • 47
    • 0034634613 scopus 로고    scopus 로고
    • S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo
    • Deloulme, J. C., Assard, N., Mbele, G. O., Mangin, C. et al. S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo. J. Biol. Chem. 2000, 275, 35302-35310.
    • (2000) J. Biol. Chem , vol.275 , pp. 35302-35310
    • Deloulme, J.C.1    Assard, N.2    Mbele, G.O.3    Mangin, C.4
  • 48
    • 0037067749 scopus 로고    scopus 로고
    • Calcyclin is an early vasopressin-induced gene in the renal collecting duct. Role in the long term regulation of ion transport
    • Courtois-Coutry, N., Le Moellic, C., Boulkroun, S., Fay, M. et al. Calcyclin is an early vasopressin-induced gene in the renal collecting duct. Role in the long term regulation of ion transport. J. Biol. Chem. 2002, 277, 25728-25734.
    • (2002) J. Biol. Chem , vol.277 , pp. 25728-25734
    • Courtois-Coutry, N.1    Le Moellic, C.2    Boulkroun, S.3    Fay, M.4
  • 49
    • 0038504106 scopus 로고    scopus 로고
    • Calcium- and cell cycle-dependent association of annexin 11 with the nuclear envelope
    • Tomas, A., Moss, S. E., Calcium- and cell cycle-dependent association of annexin 11 with the nuclear envelope. J. Biol. Chem. 2003, 278, 20210-20216.
    • (2003) J. Biol. Chem , vol.278 , pp. 20210-20216
    • Tomas, A.1    Moss, S.E.2
  • 50
    • 0042858255 scopus 로고    scopus 로고
    • Dissecting the cellular functions of annexin XI using recombinant human annexin XI-specific autoantibodies cloned by phage display
    • Farnaes, L., Ditzel, H. J., Dissecting the cellular functions of annexin XI using recombinant human annexin XI-specific autoantibodies cloned by phage display. J. Biol. Chem. 2003, 278, 33120-33126.
    • (2003) J. Biol. Chem , vol.278 , pp. 33120-33126
    • Farnaes, L.1    Ditzel, H.J.2
  • 51
    • 0038690308 scopus 로고    scopus 로고
    • Expression analysis of S100 proteins and RAGE in human tumors using tissue microarrays
    • Hsieh, H. L., Schafer, B. W., Sasaki, N., Heizmann, C. W., Expression analysis of S100 proteins and RAGE in human tumors using tissue microarrays. Biochem. Biophys. Res. Commun. 2003, 307, 375-381.
    • (2003) Biochem. Biophys. Res. Commun , vol.307 , pp. 375-381
    • Hsieh, H.L.1    Schafer, B.W.2    Sasaki, N.3    Heizmann, C.W.4
  • 52
    • 0032968473 scopus 로고    scopus 로고
    • Subcellular distribution of S100 proteins in tumor cells and their relocation in response to calcium activation
    • Mueller, A., Bachi, T., Hochli, M., Schafer, B. W., Heizmann, C. W., Subcellular distribution of S100 proteins in tumor cells and their relocation in response to calcium activation. Histochem. Cell Biol. 1999, 111, 453-459.
    • (1999) Histochem. Cell Biol , vol.111 , pp. 453-459
    • Mueller, A.1    Bachi, T.2    Hochli, M.3    Schafer, B.W.4    Heizmann, C.W.5
  • 53
    • 0029665074 scopus 로고    scopus 로고
    • 2+ in sarcoplasmic reticulum in perfused rabbit heart loaded with 1,2-bis(2-amino-5,6-difluorophenoxy)ethane-N,N,N′, N′-tetraacetic acid by 19F NMR
    • 2+ in sarcoplasmic reticulum in perfused rabbit heart loaded with 1,2-bis(2-amino-5,6-difluorophenoxy)ethane-N,N,N′, N′-tetraacetic acid by 19F NMR. J. Biol. Chem. 1996, 271, 7398-7403.
    • (1996) J. Biol. Chem , vol.271 , pp. 7398-7403
    • Chen, W.1    Steenbergen, C.2    Levy, L.A.3    Vance, J.4
  • 55
    • 0024336546 scopus 로고
    • Dehydrogenases of the pentose phosphate pathway in rat liver peroxisomes
    • Antonenkov, V. D., Dehydrogenases of the pentose phosphate pathway in rat liver peroxisomes. Eur. J. Biochem. 1989, 183, 75-82.
    • (1989) Eur. J. Biochem , vol.183 , pp. 75-82
    • Antonenkov, V.D.1
  • 56
    • 0026594072 scopus 로고    scopus 로고
    • Furthmayr, H., Lankes, W., Amieva, M., Moesin, a new cytoskeletal protein and constituent of filopodia: its role in cellular functions. Kidney Int. 1992, 41, 665-670.
    • Furthmayr, H., Lankes, W., Amieva, M., Moesin, a new cytoskeletal protein and constituent of filopodia: its role in cellular functions. Kidney Int. 1992, 41, 665-670.
  • 57
    • 0026697728 scopus 로고
    • Identification of ezrin as an 81-kDa tyrosine-phosphorylated protein in T cells
    • Egerton, M., Burgess, W. H., Chen, D., Druker, B. J. et al. Identification of ezrin as an 81-kDa tyrosine-phosphorylated protein in T cells. J. Immunol. 1992, 149, 1847-1852.
    • (1992) J. Immunol , vol.149 , pp. 1847-1852
    • Egerton, M.1    Burgess, W.H.2    Chen, D.3    Druker, B.J.4
  • 58
    • 0027154678 scopus 로고
    • Molecular cloning, cDNA sequence, and chromosomal assignment of the human radixin gene and two dispersed pseudogenes
    • Wilgenbus, K. K., Milatovich, A., Francke, U., Furthmayr, H., Molecular cloning, cDNA sequence, and chromosomal assignment of the human radixin gene and two dispersed pseudogenes. Genomics 1993, 16, 199-206.
    • (1993) Genomics , vol.16 , pp. 199-206
    • Wilgenbus, K.K.1    Milatovich, A.2    Francke, U.3    Furthmayr, H.4
  • 59
    • 0028935060 scopus 로고
    • Subcellular localization of annexins in human foreskin fibroblasts
    • Barwise, J. L., Walker, J. H., Subcellular localization of annexins in human foreskin fibroblasts. Biochem. Soc. Trans. 1995, 23, 35S.
    • (1995) Biochem. Soc. Trans , vol.23
    • Barwise, J.L.1    Walker, J.H.2
  • 60
    • 0033951316 scopus 로고    scopus 로고
    • Immunolocalization of annexins IV, V and VI in the failing and non-failing human heart
    • Matteo, R. G., Moravec, C. S., Immunolocalization of annexins IV, V and VI in the failing and non-failing human heart. Cardiovasc. Res. 2000, 45, 961-970.
    • (2000) Cardiovasc. Res , vol.45 , pp. 961-970
    • Matteo, R.G.1    Moravec, C.S.2
  • 61
    • 0842265979 scopus 로고    scopus 로고
    • Expression, subcellular localization and phosphorylation status of annexins 1 and 5 in human pituitary adenomas and a growth hormone-secreting carcinoma
    • Mulla, A., Christian, H. C., Solito, E., Mendoza, N. et al. Expression, subcellular localization and phosphorylation status of annexins 1 and 5 in human pituitary adenomas and a growth hormone-secreting carcinoma. Clin. Endocrinol. (Oxf) 2004, 60, 107-119.
    • (2004) Clin. Endocrinol. (Oxf) , vol.60 , pp. 107-119
    • Mulla, A.1    Christian, H.C.2    Solito, E.3    Mendoza, N.4
  • 62
    • 0029043888 scopus 로고
    • A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V
    • Vermes, I., Haanen, C., Steffens-Nakken, H., Reutelingsperger, C., A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V. J. Immunol. Methods 1995, 184, 39-51.
    • (1995) J. Immunol. Methods , vol.184 , pp. 39-51
    • Vermes, I.1    Haanen, C.2    Steffens-Nakken, H.3    Reutelingsperger, C.4
  • 63
    • 0035216870 scopus 로고    scopus 로고
    • Secretion of annexin V from cultured cells requires a signal peptide
    • Wang, X., Campos, B., Kaetzel, M. A., Dedman, J. R., Secretion of annexin V from cultured cells requires a signal peptide. Placenta 2001, 22, 837-845.
    • (2001) Placenta , vol.22 , pp. 837-845
    • Wang, X.1    Campos, B.2    Kaetzel, M.A.3    Dedman, J.R.4
  • 64
    • 0022387184 scopus 로고
    • Isolation and partial purification of a novel anticoagulant from arteries of human umbilical cord
    • Reutelingsperger, C. P., Hornstra, G., Hemker, H. C., Isolation and partial purification of a novel anticoagulant from arteries of human umbilical cord. Eur. J. Biochem. 1985, 151, 625-629.
    • (1985) Eur. J. Biochem , vol.151 , pp. 625-629
    • Reutelingsperger, C.P.1    Hornstra, G.2    Hemker, H.C.3
  • 66
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: Tool for the unification of biology. The Gene Ontology Consortium
    • Ashburner, M., Ball, C. A., Blake, J. A., Botstein, D. et al. Gene ontology: tool for the unification of biology. The Gene Ontology Consortium. Nat. Genet. 2000, 25, 25-29.
    • (2000) Nat. Genet , vol.25 , pp. 25-29
    • Ashburner, M.1    Ball, C.A.2    Blake, J.A.3    Botstein, D.4
  • 67
    • 0026515937 scopus 로고
    • Isolation of a lactoferrin cDNA clone and its expression in human breast cancer
    • Campbell, T., Skilton, R. A., Coombes, R. C., Shousha, S. et al. Isolation of a lactoferrin cDNA clone and its expression in human breast cancer. Br. J. Cancer 1992, 65, 19-26.
    • (1992) Br. J. Cancer , vol.65 , pp. 19-26
    • Campbell, T.1    Skilton, R.A.2    Coombes, R.C.3    Shousha, S.4
  • 69
    • 0036191387 scopus 로고    scopus 로고
    • The physiology of lactoferrin
    • Brock, J. H., The physiology of lactoferrin. Biochem. Cell Biol. 2002, 80, 1-6.
    • (2002) Biochem. Cell Biol , vol.80 , pp. 1-6
    • Brock, J.H.1
  • 70
    • 0141450720 scopus 로고    scopus 로고
    • Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria
    • Masschalck, B., Michiels, C. W., Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria. Crit. Rev. Microbiol. 2003, 29, 191-214.
    • (2003) Crit. Rev. Microbiol , vol.29 , pp. 191-214
    • Masschalck, B.1    Michiels, C.W.2
  • 71
    • 18844400905 scopus 로고    scopus 로고
    • Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism
    • Manevich, Y., Fisher, A. B., Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. Free Radic. Biol. Med. 2005, 38, 1422-1432.
    • (2005) Free Radic. Biol. Med , vol.38 , pp. 1422-1432
    • Manevich, Y.1    Fisher, A.B.2
  • 73
    • 0033935825 scopus 로고    scopus 로고
    • Towards understanding the kallikrein-kinin system: Insights from measurement of kinin peptides
    • Campbell, D. J., Towards understanding the kallikrein-kinin system: insights from measurement of kinin peptides. Braz. J. Med. Biol. Res. 2000, 33, 665-677.
    • (2000) Braz. J. Med. Biol. Res , vol.33 , pp. 665-677
    • Campbell, D.J.1
  • 74
    • 0344630172 scopus 로고    scopus 로고
    • The blood coagulation system as a molecular machine
    • Spronk, H. M., Govers-Riemslag, J. W., ten Cate, H., The blood coagulation system as a molecular machine. Bioessays 2003, 25, 1220-1228.
    • (2003) Bioessays , vol.25 , pp. 1220-1228
    • Spronk, H.M.1    Govers-Riemslag, J.W.2    ten Cate, H.3
  • 75
    • 58049176372 scopus 로고    scopus 로고
    • 2+-dependent complex with thrombospondin-1. A potential role in haemostasis and thrombosis
    • 2+-dependent complex with thrombospondin-1. A potential role in haemostasis and thrombosis. Mol. Cell. Biochem. 2009, 320, 25-33.
    • (2009) Mol. Cell. Biochem , vol.320 , pp. 25-33
    • Hansen, G.A.1    Vorum, H.2    Jacobsen, C.3    Honoré, B.4
  • 76
    • 3042705857 scopus 로고    scopus 로고
    • Warfarin and the vitamin K-dependent gamma-carboxylation system
    • Wallin, R., Hutson, S. M., Warfarin and the vitamin K-dependent gamma-carboxylation system. Trends Mol. Med. 2004, 10, 299-302.
    • (2004) Trends Mol. Med , vol.10 , pp. 299-302
    • Wallin, R.1    Hutson, S.M.2
  • 78
    • 0027993347 scopus 로고
    • Use of 1.4-nm immunogold particles for immunocytochemistry on ultra-thin cryosections
    • Takizawa, T., Robinson, J. M., Use of 1.4-nm immunogold particles for immunocytochemistry on ultra-thin cryosections. J. Histochem. Cytochem. 1994, 42, 1615-1623.
    • (1994) J. Histochem. Cytochem , vol.42 , pp. 1615-1623
    • Takizawa, T.1    Robinson, J.M.2
  • 79
    • 33846073182 scopus 로고    scopus 로고
    • Full length and delta lactoferrin display differential cell localization dynamics, but do not act as tumor markers or significantly affect the expression of other genes
    • Goldberg, G. S., Kunimoto, T., Alexander, D. B., Suenaga, K. et al. Full length and delta lactoferrin display differential cell localization dynamics, but do not act as tumor markers or significantly affect the expression of other genes. Med. Chem. 2005, 1, 57-64.
    • (2005) Med. Chem , vol.1 , pp. 57-64
    • Goldberg, G.S.1    Kunimoto, T.2    Alexander, D.B.3    Suenaga, K.4
  • 80
    • 17744405513 scopus 로고    scopus 로고
    • Lactoferrin down-regulates the LPS-induced cytokine production in monocytic cells via NFkappa B
    • Haversen, L., Ohlsson, B. G., Hahn-Zoric, M., Hanson, L. A., Mattsby-Baltzer, I., Lactoferrin down-regulates the LPS-induced cytokine production in monocytic cells via NFkappa B. Cell. Immunol. 2002, 220, 83-95.
    • (2002) Cell. Immunol , vol.220 , pp. 83-95
    • Haversen, L.1    Ohlsson, B.G.2    Hahn-Zoric, M.3    Hanson, L.A.4    Mattsby-Baltzer, I.5
  • 81
    • 0029821431 scopus 로고    scopus 로고
    • Cultured leptomeningeal cells secrete cerebrospinal fluid proteins
    • Ohe, Y., Ishikawa, K., Itoh, Z., Tatemoto, K., Cultured leptomeningeal cells secrete cerebrospinal fluid proteins. J. Neurochem. 1996, 67, 964-971.
    • (1996) J. Neurochem , vol.67 , pp. 964-971
    • Ohe, Y.1    Ishikawa, K.2    Itoh, Z.3    Tatemoto, K.4
  • 83
    • 0027406716 scopus 로고
    • Molecular cloning of human von Ebner's gland protein, a member of the lipocalin superfamily highly expressed in lingual salivary glands
    • Blaker, M., Kock, K., Ahlers, C., Buck, F., Schmale, H., Molecular cloning of human von Ebner's gland protein, a member of the lipocalin superfamily highly expressed in lingual salivary glands. Biochim. Biophys. Acta 1993, 1172, 131-137.
    • (1993) Biochim. Biophys. Acta , vol.1172 , pp. 131-137
    • Blaker, M.1    Kock, K.2    Ahlers, C.3    Buck, F.4    Schmale, H.5
  • 84
    • 0034919997 scopus 로고    scopus 로고
    • The subcellular distribution of GABARAP and its ability to interact with NSF suggest a role for this protein in the intracellular transport of GABA(A) receptors
    • Kittler, J. T., Rostaing, P., Schiavo, G., Fritschy, J. M. et al. The subcellular distribution of GABARAP and its ability to interact with NSF suggest a role for this protein in the intracellular transport of GABA(A) receptors. Mol. Cell. Neurosci. 2001, 18, 13-25.
    • (2001) Mol. Cell. Neurosci , vol.18 , pp. 13-25
    • Kittler, J.T.1    Rostaing, P.2    Schiavo, G.3    Fritschy, J.M.4
  • 85
    • 17644423479 scopus 로고    scopus 로고
    • Peroxiredoxins, oxidative stress, and cell proliferation
    • Immenschuh, S., Baumgart-Vogt, E., Peroxiredoxins, oxidative stress, and cell proliferation. Antioxid. Redox Signal 2005, 7, 768-777.
    • (2005) Antioxid. Redox Signal , vol.7 , pp. 768-777
    • Immenschuh, S.1    Baumgart-Vogt, E.2
  • 87
    • 0031870090 scopus 로고    scopus 로고
    • Distinct subcellular localization of calcium binding S100 proteins in human smooth muscle cells and their relocation in response to rises in intracellular calcium
    • Mandinova, A., Atar, D., Schafer, B. W., Spiess, M. et al. Distinct subcellular localization of calcium binding S100 proteins in human smooth muscle cells and their relocation in response to rises in intracellular calcium. J. Cell Sci. 1998, 111 (Pt 14), 2043-2054.
    • (1998) J. Cell Sci , vol.111 , Issue.PART 14 , pp. 2043-2054
    • Mandinova, A.1    Atar, D.2    Schafer, B.W.3    Spiess, M.4
  • 88
    • 19944385563 scopus 로고    scopus 로고
    • Expression of S100P and its novel binding partner S100PBPR in early pancreatic cancer
    • Dowen, S. E., Crnogorac-Jurcevic, T., Gangeswaran, R., Hansen, M. et al. Expression of S100P and its novel binding partner S100PBPR in early pancreatic cancer. Am. J. Pathol. 2005, 166, 81-92.
    • (2005) Am. J. Pathol , vol.166 , pp. 81-92
    • Dowen, S.E.1    Crnogorac-Jurcevic, T.2    Gangeswaran, R.3    Hansen, M.4
  • 89
    • 31544449414 scopus 로고    scopus 로고
    • Induction of metastasis by S100P in a rat mammary model and its association with poor survival of breast cancer patients
    • Wang, G., Platt-Higgins, A., Carroll, J., de Silva Rudland, S. et al. Induction of metastasis by S100P in a rat mammary model and its association with poor survival of breast cancer patients. Cancer Res. 2006, 66, 1199-1207.
    • (2006) Cancer Res , vol.66 , pp. 1199-1207
    • Wang, G.1    Platt-Higgins, A.2    Carroll, J.3    de Silva Rudland, S.4
  • 91
    • 0027275994 scopus 로고
    • Moesin, like ezrin, colocalizes with actin in the cortical cytoskeleton in cultured cells, but its expression is more variable
    • Franck, Z., Gary, R., Bretscher, A., Moesin, like ezrin, colocalizes with actin in the cortical cytoskeleton in cultured cells, but its expression is more variable. J. Cell Sci. 1993, 105 (Pt 1), 219-231.
    • (1993) J. Cell Sci , vol.105 , Issue.PART 1 , pp. 219-231
    • Franck, Z.1    Gary, R.2    Bretscher, A.3
  • 92
    • 0037900705 scopus 로고    scopus 로고
    • Induction of apoptosis in human corneal and HeLa cells by mutated BIGH3
    • Morand, S., Buchillier, V., Maurer, F., Bonny, C. et al. Induction of apoptosis in human corneal and HeLa cells by mutated BIGH3. Invest. Ophthalmol. Vis. Sci. 2003, 44, 2973-2979.
    • (2003) Invest. Ophthalmol. Vis. Sci , vol.44 , pp. 2973-2979
    • Morand, S.1    Buchillier, V.2    Maurer, F.3    Bonny, C.4
  • 93
    • 0036083481 scopus 로고    scopus 로고
    • Ligand-regulated secretion of recombinant annexin V from cultured thyroid epithelial cells
    • Wang, X., Kaetzel, M. A., Yoo, S. E., Kim, P. S., Dedman, J. R., Ligand-regulated secretion of recombinant annexin V from cultured thyroid epithelial cells. Am. J. Physiol. Cell Physiol. 2002, 282, C1313-C1321.
    • (2002) Am. J. Physiol. Cell Physiol , vol.282
    • Wang, X.1    Kaetzel, M.A.2    Yoo, S.E.3    Kim, P.S.4    Dedman, J.R.5
  • 94
    • 39749189017 scopus 로고    scopus 로고
    • Measuring cell death mediated by cytotoxic lymphocytes or their granule effector molecules
    • Sutton, V. R., Waterhouse, N. J., Baran, K., Browne, K., Measuring cell death mediated by cytotoxic lymphocytes or their granule effector molecules. Methods 2008, 44, 241-249.
    • (2008) Methods , vol.44 , pp. 241-249
    • Sutton, V.R.1    Waterhouse, N.J.2    Baran, K.3    Browne, K.4


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