메뉴 건너뛰기




Volumn 33, Issue 3, 2000, Pages 275-296

Calcium signaling and annexins

Author keywords

Annexin; Calcium; Homeostasis; Ion channel; Membrane

Indexed keywords

ANNEXIN; CALCIUM; ION CHANNEL;

EID: 0034569633     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:33:3:275     Document Type: Article
Times cited : (57)

References (181)
  • 1
    • 0021338180 scopus 로고
    • Isolation of a calcium-dependent 35-kilodalton substrate for the epidermal growth factor receptor/kinase from A-431 cells
    • Fava, R. A. and Cohen, S. (1984) Isolation of a calcium-dependent 35-kilodalton substrate for the epidermal growth factor receptor/kinase from A-431 cells. J. Biol. Chem. 259, 2636-2645.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2636-2645
    • Fava, R.A.1    Cohen, S.2
  • 2
    • 0022517061 scopus 로고
    • Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60v-src and of the epidermal growth factor receptor/kinase
    • Huang, K. S., Wallner, B. P., Mattaliano, R. J., Tizard, R., Burne, C., Frey, et al. (1986) Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60v-src and of the epidermal growth factor receptor/kinase. Cell 46, 191-199.
    • (1986) Cell , vol.46 , pp. 191-199
    • Huang, K.S.1    Wallner, B.P.2    Mattaliano, R.J.3    Tizard, R.4    Burne, C.5    Frey6
  • 3
    • 0022527616 scopus 로고
    • Epidermal growth factor-dependent phosphorylation of lipocortin
    • Pepinsky, R. B. and Sinclair, L. K. (1986) Epidermal growth factor-dependent phosphorylation of lipocortin. Nature 321, 81-84.
    • (1986) Nature , vol.321 , pp. 81-84
    • Pepinsky, R.B.1    Sinclair, L.K.2
  • 4
    • 0021111579 scopus 로고
    • Identification and characterization of cellular targets for tyrosine protein kinases
    • Cooper, J. A. and Hunter, T. (1983) Identification and characterization of cellular targets for tyrosine protein kinases. J. Biol. Chem. 258, 1108-1115.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1108-1115
    • Cooper, J.A.1    Hunter, T.2
  • 5
    • 0021099707 scopus 로고
    • Comparison of the 34,000-Da pp60src substrate and a 38,000-Da phosphoprotein identified by monoclonal antibodies
    • Greenberg, M. E. and Edelman, G. M. (1983) Comparison of the 34,000-Da pp60src substrate and a 38,000-Da phosphoprotein identified by monoclonal antibodies. J. Biol. Chem. 258, 8497-8502.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8497-8502
    • Greenberg, M.E.1    Edelman, G.M.2
  • 6
    • 0021092918 scopus 로고
    • Isolation and characterization of a collagen-binding glycoprotein from chondrocyte membranes
    • Mollenhauer, J. and von der Mark, K. (1983) Isolation and characterization of a collagen-binding glycoprotein from chondrocyte membranes. EMBO J. 2, 45-50.
    • (1983) EMBO J. , vol.2 , pp. 45-50
    • Mollenhauer, J.1    Von Der Mark, K.2
  • 7
    • 0021250826 scopus 로고
    • Role of anchorin CII, a 31,000-mol-wt membrane protein, in the interaction of chondrocytes with type II collagen
    • Mollenhauer, J., Bee, J. A., Lizarbe, M. A., and von der Mark, K. (1984) Role of anchorin CII, a 31,000-mol-wt membrane protein, in the interaction of chondrocytes with type II collagen. J. Cell. Biol. 98, 1572-1579.
    • (1984) J. Cell. Biol. , vol.98 , pp. 1572-1579
    • Mollenhauer, J.1    Bee, J.A.2    Lizarbe, M.A.3    Von Der Mark, K.4
  • 8
    • 0025306172 scopus 로고
    • Protein terminology tangle
    • Crumpton, M. J. and Dedman, J. R. (1990) Protein terminology tangle. Nature 345, 212.
    • (1990) Nature , vol.345 , pp. 212
    • Crumpton, M.J.1    Dedman, J.R.2
  • 9
    • 0028820642 scopus 로고
    • Molecular phylogeny of annexins and identification of a primitive homologue in Giardia lamblia
    • Morgan, R. O. and Fernandez, M. P. (1995) Molecular phylogeny of annexins and identification of a primitive homologue in Giardia lamblia. Mol. Biol. Evol. 12, 967-979.
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 967-979
    • Morgan, R.O.1    Fernandez, M.P.2
  • 10
    • 0030775075 scopus 로고    scopus 로고
    • Annexin gene structures and molecular evolutionary genetics
    • Morgan, R. O. and Fernandez, M. P. (1997) Annexin gene structures and molecular evolutionary genetics. Cell. Mol. Life Sci. 53, 508-515.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 508-515
    • Morgan, R.O.1    Fernandez, M.P.2
  • 11
    • 0031766517 scopus 로고    scopus 로고
    • Identification of the first fungal annexin: Analysis of annexin gene duplications and implications for eukaryotic evolution
    • Braun, E. L., Kang, S., Nelson, M. A., and Natvig, D. O. (1998) Identification of the first fungal annexin: analysis of annexin gene duplications and implications for eukaryotic evolution. J. Mol. Evol. 47, 531-543.
    • (1998) J. Mol. Evol. , vol.47 , pp. 531-543
    • Braun, E.L.1    Kang, S.2    Nelson, M.A.3    Natvig, D.O.4
  • 13
    • 0024359919 scopus 로고
    • Phospholipid binding properties of human placental anticoagulant protein-I, a member of the lipocortin family
    • Tait, J. F., Gibson, D., and Fujikawa, K. (1989) Phospholipid binding properties of human placental anticoagulant protein-I, a member of the lipocortin family. J. Biol. Chem. 264, 7944-7949.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7944-7949
    • Tait, J.F.1    Gibson, D.2    Fujikawa, K.3
  • 14
    • 0030824406 scopus 로고    scopus 로고
    • Participation of annexins in protein phosphorylation
    • Rothhut, B. (1997) Participation of annexins in protein phosphorylation. Cell. Mol. Life Sci. 53, 522-526.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 522-526
    • Rothhut, B.1
  • 15
    • 0022928659 scopus 로고
    • Phospholipid-dependent Ca2+ binding by the 36-kDa tyrosine kinase substrate (calpactin) and its 33-kDa core
    • Glenney, J. (1986) Phospholipid-dependent Ca2+ binding by the 36-kDa tyrosine kinase substrate (calpactin) and its 33-kDa core. J. Biol. Chem. 261, 7247-7252.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7247-7252
    • Glenney, J.1
  • 16
    • 0001171815 scopus 로고
    • Amino-terminal sequence of p36 and associated p10: Identification of the site of tyrosine phosphorylation and homology with S-100
    • Glenney, J. R., Jr. and Tack, B. F. (1985) Amino-terminal sequence of p36 and associated p10: identification of the site of tyrosine phosphorylation and homology with S-100. Proc. Natl. Acad. Sci. USA 82, 7884-7888.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7884-7888
    • Glenney J.R., Jr.1    Tack, B.F.2
  • 17
    • 0025055013 scopus 로고
    • Structural analysis of p36, a Ca2+/lipid-binding protein of the annexin family, by proteolysis and chemical fragmentation
    • Johnsson, N. and Weber, K. (1990) Structural analysis of p36, a Ca2+/lipid-binding protein of the annexin family, by proteolysis and chemical fragmentation. Eur. J. Biochem. 188, 1-7.
    • (1990) Eur. J. Biochem. , vol.188 , pp. 1-7
    • Johnsson, N.1    Weber, K.2
  • 18
    • 0029887641 scopus 로고    scopus 로고
    • The crystal structure and ion channel activity of human annexin II, a peripheral membrane protein
    • Burger, A., Berendes, R., Liemann, S., Benz, J., Hofmann, A., Gottig, P., et al. (1996) The crystal structure and ion channel activity of human annexin II, a peripheral membrane protein. J. Mol. Biol. 257, 839-847.
    • (1996) J. Mol. Biol. , vol.257 , pp. 839-847
    • Burger, A.1    Berendes, R.2    Liemann, S.3    Benz, J.4    Hofmann, A.5    Gottig, P.6
  • 19
    • 0027847029 scopus 로고
    • Rat annexin V crystal structure: Ca(2+)-induced conformational changes
    • Concha, N. O., Head, J. F., Kaetzel, M. A., Dedman, J. R., and Seaton, B. A. (1993) Rat annexin V crystal structure: Ca(2+)-induced conformational changes. Science 261, 1321-1324.
    • (1993) Science , vol.261 , pp. 1321-1324
    • Concha, N.O.1    Head, J.F.2    Kaetzel, M.A.3    Dedman, J.R.4    Seaton, B.A.5
  • 20
    • 0030047497 scopus 로고    scopus 로고
    • The high-resolution crystal structure of human annexin III shows subtle differences with annexin V
    • Favier-Perron, B., Lewit Bentley, A., and Russo Marie, F. (1996) The high-resolution crystal structure of human annexin III shows subtle differences with annexin V. Biochemistry 35, 1740-1744.
    • (1996) Biochemistry , vol.35 , pp. 1740-1744
    • Favier-Perron, B.1    Lewit Bentley, A.2    Russo Marie, F.3
  • 21
    • 0025000276 scopus 로고
    • The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes
    • Huber, R., Romisch, T., and Paques, E. P. (1990) The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. EMBO J. 9, 3867-3874.
    • (1990) EMBO J. , vol.9 , pp. 3867-3874
    • Huber, R.1    Romisch, T.2    Paques, E.P.3
  • 22
    • 0026497557 scopus 로고
    • The effect of metal binding on the structure of annexin V and implications for membrane binding
    • Lewit Bentley, A., Morera, S., Huber, R., and Bodo, G. (1992) The effect of metal binding on the structure of annexin V and implications for membrane binding. Eur. J. Biochem. 210, 73-77.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 73-77
    • Lewit Bentley, A.1    Morera, S.2    Huber, R.3    Bodo, G.4
  • 23
    • 0028846237 scopus 로고
    • Crystal structure of the annexin XII hexamer and implications for bilayer insertion
    • Luecke, H., Chang, B. T., Mailliard, W. S., Schlaepfer, D. D., and Haigler, H. T. (1995) Crystal structure of the annexin XII hexamer and implications for bilayer insertion. Nature 378, 512-515.
    • (1995) Nature , vol.378 , pp. 512-515
    • Luecke, H.1    Chang, B.T.2    Mailliard, W.S.3    Schlaepfer, D.D.4    Haigler, H.T.5
  • 25
    • 0030821003 scopus 로고    scopus 로고
    • Three-dimensional structure of annexins
    • Liemann, S. and Huber, R. (1997) Three-dimensional structure of annexins. Cell. Mol. Life Sci. 53, 516-521.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 516-521
    • Liemann, S.1    Huber, R.2
  • 27
    • 0028879868 scopus 로고
    • Annexins taken to task
    • Moss, S. E. (1995) Annexins taken to task. Nature 378, 446-447.
    • (1995) Nature , vol.378 , pp. 446-447
    • Moss, S.E.1
  • 28
    • 0022387184 scopus 로고
    • Isolation and partial purification of a novel anticoagulant from arteries of human umbilical cord
    • Reutelingsperger, C. P., Hornstra, G., and Hemker, H. C. (1985) Isolation and partial purification of a novel anticoagulant from arteries of human umbilical cord. Eur. J. Biochem. 151, 625-629.
    • (1985) Eur. J. Biochem. , vol.151 , pp. 625-629
    • Reutelingsperger, C.P.1    Hornstra, G.2    Hemker, H.C.3
  • 29
    • 0018136108 scopus 로고
    • Identification and purification of an adrenal medullary protein (synexin) that causes calcium-dependent aggregation of isolated chromaffin granules
    • Creutz, C. E., Pazoles, C. J., and Pollard, H. B. (1978) Identification and purification of an adrenal medullary protein (synexin) that causes calcium-dependent aggregation of isolated chromaffin granules. J. Biol. Chem. 253, 2858-2866.
    • (1978) J. Biol. Chem. , vol.253 , pp. 2858-2866
    • Creutz, C.E.1    Pazoles, C.J.2    Pollard, H.B.3
  • 30
    • 0028212016 scopus 로고
    • Annexin-I inhibits phospholipase A2 by specific interaction, not by substrate depletion
    • Kim, K. M., Kim, D. K., Park, Y. M., Kim, C. K., and Na, D. S. (1994) Annexin-I inhibits phospholipase A2 by specific interaction, not by substrate depletion. FEBS Lett. 343, 251-255.
    • (1994) FEBS Lett. , vol.343 , pp. 251-255
    • Kim, K.M.1    Kim, D.K.2    Park, Y.M.3    Kim, C.K.4    Na, D.S.5
  • 31
    • 0030858046 scopus 로고    scopus 로고
    • Annexin V, the regulator of phosphatidylserine-caralyzed inflammation and coagulation during apoptosis
    • Reutelingsperger, C. P. and van Heerde, W. L. (1997) Annexin V, the regulator of phosphatidylserine-caralyzed inflammation and coagulation during apoptosis. Cell. Mol. Life Sci. 53, 527-532.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 527-532
    • Reutelingsperger, C.P.1    Van Heerde, W.L.2
  • 32
    • 0021299594 scopus 로고
    • Identity of p36K phosphorylated upon rous sarcoma virus transformation with a protein purified from brush borders: Calcium-dependent binding to non-erythroid spectrin and F-actin
    • Gerke, V. and Weber, K. (1984) Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders: calcium-dependent binding to non-erythroid spectrin and F-actin. EMBO J. 3, 227-233.
    • (1984) EMBO J. , vol.3 , pp. 227-233
    • Gerke, V.1    Weber, K.2
  • 33
    • 0011972017 scopus 로고
    • Two related but distinct forms of the Mr 36,000 tyrosine kinase substrate (calpactin) that interact with phospholipid and actin in a Ca2+-dependent manner
    • Glenney, J. (1986) Two related but distinct forms of the Mr 36,000 tyrosine kinase substrate (calpactin) that interact with phospholipid and actin in a Ca2+-dependent manner. Proc. Natl. Acad. Sci. USA 83, 4258-4262.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4258-4262
    • Glenney, J.1
  • 34
    • 0028656423 scopus 로고
    • New 1,4-benzothiazepine derivative, K201, demonstrates cardioprotective effects against sudden cardiac cell death and intracellular calcium blocking action
    • Kaneko, N. (1994) New 1,4-benzothiazepine derivative, K201, demonstrates cardioprotective effects against sudden cardiac cell death and intracellular calcium blocking action. Drug Dev. Res. 33, 429-438.
    • (1994) Drug Dev. Res. , vol.33 , pp. 429-438
    • Kaneko, N.1
  • 35
    • 0028226406 scopus 로고
    • Axonal transport of actin and actin-binding proteins in the rat sciatic nerve
    • Tanaka, K., Tashiro, T., Sekimoto, S., and Komiya, Y. (1994) Axonal transport of actin and actin-binding proteins in the rat sciatic nerve. Neurosci. Res. 19, 295-302.
    • (1994) Neurosci. Res. , vol.19 , pp. 295-302
    • Tanaka, K.1    Tashiro, T.2    Sekimoto, S.3    Komiya, Y.4
  • 36
    • 0023718423 scopus 로고
    • Diversity in the lipocortin/calpactin family
    • Crompton, M. R., Moss, S. E., and Crumpton, M. J. (1988) Diversity in the lipocortin/calpactin family. Cell 55, 1-3.
    • (1988) Cell , vol.55 , pp. 1-3
    • Crompton, M.R.1    Moss, S.E.2    Crumpton, M.J.3
  • 37
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
    • Raynal, P. and Pollard, H. B. (1994) Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim. Biophys. Acta 1197, 63-93.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 38
    • 0030052283 scopus 로고    scopus 로고
    • Calcium-dependent binding of S100C to the N-terminal domain of annexin I. J
    • Mailliard, W. S., Haigler, H. T., and Schlaepfer, D. D. (1996) Calcium-dependent binding of S100C to the N-terminal domain of annexin I. J. Biol. Chem. 271, 719-725.
    • (1996) Biol. Chem. , vol.271 , pp. 719-725
    • Mailliard, W.S.1    Haigler, H.T.2    Schlaepfer, D.D.3
  • 39
    • 0028033381 scopus 로고
    • Purification and characterization of a novel calcium-binding protein, S100C, from porcine heart
    • Naka, M., Qing, Z. X., Sasaki, T., Kise, H., Tawara, I., Hamaguchi, S., and Tanaka, T. (1994) Purification and characterization of a novel calcium-binding protein, S100C, from porcine heart. Biochim. Biophys. Acta 1223, 348-353.
    • (1994) Biochim. Biophys. Acta , vol.1223 , pp. 348-353
    • Naka, M.1    Qing, Z.X.2    Sasaki, T.3    Kise, H.4    Tawara, I.5    Hamaguchi, S.6    Tanaka, T.7
  • 40
    • 0029811498 scopus 로고    scopus 로고
    • Structural requirements for annexin I-S100C complex-formation
    • Seemann, J., Weber, K., and Gerke, V. (1996) Structural requirements for annexin I-S100C complex-formation. Biochim. J. 319, 123-129.
    • (1996) Biochim. J. , vol.319 , pp. 123-129
    • Seemann, J.1    Weber, K.2    Gerke, V.3
  • 41
    • 0026799425 scopus 로고
    • A calcyclin-associated protein is a newly identified member of the Ca2+/phospholipid-binding proteins, annexin family
    • Tokumitsu, H., Mizutani, A., Minami, H., Kobayashi, R., and Hidaka, H. (1992) A calcyclin-associated protein is a newly identified member of the Ca2+/phospholipid-binding proteins, annexin family. J. Biol. Chem. 267, 8919-8924.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8919-8924
    • Tokumitsu, H.1    Mizutani, A.2    Minami, H.3    Kobayashi, R.4    Hidaka, H.5
  • 42
    • 0028921025 scopus 로고
    • Annexin XIIIb: A novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane
    • Fiedler, K., Lafont, F., Parton, R. G., and Simons, K. (1995) Annexin XIIIb: a novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane. J. Cell. Biol. 128, 1043-1053.
    • (1995) J. Cell. Biol. , vol.128 , pp. 1043-1053
    • Fiedler, K.1    Lafont, F.2    Parton, R.G.3    Simons, K.4
  • 43
    • 0026575153 scopus 로고
    • A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: Characterization of a novel gut-specific N-myristoylated annexin
    • Wice, B. M. and Gordon, J. I. (1992) A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin. J. Cell. Biol. 116, 405-422.
    • (1992) J. Cell. Biol. , vol.116 , pp. 405-422
    • Wice, B.M.1    Gordon, J.I.2
  • 44
    • 0026633098 scopus 로고
    • Mapping of three unique Ca(2+)-binding sites in human annexin II
    • Jost, M., Thiel, C., Weber, K., and Gerke, V. (1992) Mapping of three unique Ca(2+)-binding sites in human annexin II. Eur. J. Biochem. 207, 923-930.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 923-930
    • Jost, M.1    Thiel, C.2    Weber, K.3    Gerke, V.4
  • 45
    • 0028280193 scopus 로고
    • Annexin II contains two types of Ca(2+)-binding sites
    • Jost, M., Weber, K., and Gerke, V. (1994) Annexin II contains two types of Ca(2+)-binding sites. Biochem. J. 3, 553-559.
    • (1994) Biochem. J. , vol.3 , pp. 553-559
    • Jost, M.1    Weber, K.2    Gerke, V.3
  • 46
    • 0027094236 scopus 로고
    • The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- and Ca(2+)-binding sites
    • Thiel, C., Osborn, M., and Gerke, V. (1992) The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- and Ca(2+)-binding sites. J. Cell. Sci. 103, 733-742.
    • (1992) J. Cell. Sci. , vol.103 , pp. 733-742
    • Thiel, C.1    Osborn, M.2    Gerke, V.3
  • 48
    • 0030580074 scopus 로고    scopus 로고
    • The crystal structure of annexin VI indicates relative rotation of the two lobes upon membrane binding
    • Kawasaki, H., Avila Sakar, A., Creutz, C. E., and Kretsinger, R. H. (1996) The crystal structure of annexin VI indicates relative rotation of the two lobes upon membrane binding. Biochim. Biophys. Acta 1313, 277-282.
    • (1996) Biochim. Biophys. Acta , vol.1313 , pp. 277-282
    • Kawasaki, H.1    Avila Sakar, A.2    Creutz, C.E.3    Kretsinger, R.H.4
  • 49
    • 0025038549 scopus 로고
    • The calcium binding sites in human annexin V by crystal structure analysis at 2.0 a resolution. Implications for membrane binding and calcium channel activity
    • Huber, R., Schneider, M., Mayr, I., Romisch, J., and Paques, E. P. (1990) The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution. Implications for membrane binding and calcium channel activity. FEBS Lett. 275, 15-21.
    • (1990) FEBS Lett. , vol.275 , pp. 15-21
    • Huber, R.1    Schneider, M.2    Mayr, I.3    Romisch, J.4    Paques, E.P.5
  • 50
    • 0026703281 scopus 로고
    • Distinct cellular expression pattern of annexins in Hydra vulgaris
    • Schlaepfer, D. D., Bode, H. R., and Haigler, H. T. (1992) Distinct cellular expression pattern of annexins in Hydra vulgaris. J. Cell. Biol. 118, 911-928.
    • (1992) J. Cell. Biol. , vol.118 , pp. 911-928
    • Schlaepfer, D.D.1    Bode, H.R.2    Haigler, H.T.3
  • 51
    • 0029865282 scopus 로고    scopus 로고
    • Identification, localization, and functional implications of an abundant nematode annexin
    • Creutz, C. E., Snyder, S. L., Daigle, S. N., and Redick, J. (1996) Identification, localization, and functional implications of an abundant nematode annexin. J. Cell. Biol. 132, 1079-1092.
    • (1996) J. Cell. Biol. , vol.132 , pp. 1079-1092
    • Creutz, C.E.1    Snyder, S.L.2    Daigle, S.N.3    Redick, J.4
  • 52
    • 0031177757 scopus 로고    scopus 로고
    • Effects of a mechanical stimulation of localization of annexin-like proteins in Bryonia dioicia internodes
    • Thonat, C., Mathieu, C., Crevecoeur, M., Penel, C., Gaspar, T., and Boyer, N. (1997) Effects of a mechanical stimulation of localization of annexin-like proteins in Bryonia dioicia internodes. Plant. Physiol. 114, 981-988.
    • (1997) Plant. Physiol. , vol.114 , pp. 981-988
    • Thonat, C.1    Mathieu, C.2    Crevecoeur, M.3    Penel, C.4    Gaspar, T.5    Boyer, N.6
  • 53
    • 0026048811 scopus 로고
    • Expression of annexin VI (p68, 67 kDa-calelectrin) in normal human tissues: Evidence for developmental regulation in B- and T-lymphocytes
    • Clark, D. M., Moss, S. E., Wright, N. A., and Crumpton, M. J. (1991) Expression of annexin VI (p68, 67 kDa-calelectrin) in normal human tissues: evidence for developmental regulation in B- and T-lymphocytes. Histochemistry 96, 405-412.
    • (1991) Histochemistry , vol.96 , pp. 405-412
    • Clark, D.M.1    Moss, S.E.2    Wright, N.A.3    Crumpton, M.J.4
  • 54
    • 0024424454 scopus 로고
    • Lipocortin I (p35) is abundant in a restricted number of differentiated cell types in adult organs
    • Fava, R. A., McKanna, J., and Cohen, S. (1989) Lipocortin I (p35) is abundant in a restricted number of differentiated cell types in adult organs. J. Cell. Physiol. 141, 284-293.
    • (1989) J. Cell. Physiol. , vol.141 , pp. 284-293
    • Fava, R.A.1    McKanna, J.2    Cohen, S.3
  • 56
    • 0029875402 scopus 로고    scopus 로고
    • Differential expression of annexins I-VI in the rat dorsal root ganglia and spinal cord
    • Naciff, J. M., Kaetzel, M. A., Behbehani, M. M., and Dedman, J. R. (1996) Differential expression of annexins I-VI in the rat dorsal root ganglia and spinal cord. J. Comp. Neurol. 368, 356-370.
    • (1996) J. Comp. Neurol. , vol.368 , pp. 356-370
    • Naciff, J.M.1    Kaetzel, M.A.2    Behbehani, M.M.3    Dedman, J.R.4
  • 57
    • 0030607223 scopus 로고    scopus 로고
    • Subcellular localization of annexin V in human foreskin fibroblasts: Nuclear localization depends on growth state
    • Barwise, J. L. and Walker, J. H. (1996) Subcellular localization of annexin V in human foreskin fibroblasts: nuclear localization depends on growth state. FEBS Lett. 394, 213-216.
    • (1996) FEBS Lett. , vol.394 , pp. 213-216
    • Barwise, J.L.1    Walker, J.H.2
  • 58
    • 0030056150 scopus 로고    scopus 로고
    • Annexins in the human neuroblastoma SH-SY5Y: Demonstration of relocation of annexins II and V to membranes in response to elevation of intracellular calcium by membrane depolarisation and by the calcium ionophore A23187
    • Blanchard, S., Barwise, J. L., Gerke, V., Goodall, A., Vaughan, P. F., and Walker, J. H. (1996) Annexins in the human neuroblastoma SH-SY5Y: demonstration of relocation of annexins II and V to membranes in response to elevation of intracellular calcium by membrane depolarisation and by the calcium ionophore A23187. J. Neurochem. 67, 805-813.
    • (1996) J. Neurochem. , vol.67 , pp. 805-813
    • Blanchard, S.1    Barwise, J.L.2    Gerke, V.3    Goodall, A.4    Vaughan, P.F.5    Walker, J.H.6
  • 62
    • 0029937217 scopus 로고    scopus 로고
    • Measurement of lipocortin 1 levels in murine peripheral blood leukocytes by flow cytometry: Modulation by glucocorticoids and inflammation
    • Perretti, M. and Flower, R. J. (1996) Measurement of lipocortin 1 levels in murine peripheral blood leukocytes by flow cytometry: modulation by glucocorticoids and inflammation. Br. J. Pharmacol. 118, 605-610.
    • (1996) Br. J. Pharmacol. , vol.118 , pp. 605-610
    • Perretti, M.1    Flower, R.J.2
  • 63
    • 85047675768 scopus 로고
    • Identification and immunolocalisation of annexins V and VI, the major cardiac annexins, in rat heart
    • Doubell, A. F., Lazure, C., Charbonneau, C., and Thibault, G. (1993) Identification and immunolocalisation of annexins V and VI, the major cardiac annexins, in rat heart. Cardiovasc. Res. 27, 1359-1367.
    • (1993) Cardiovasc. Res. , vol.27 , pp. 1359-1367
    • Doubell, A.F.1    Lazure, C.2    Charbonneau, C.3    Thibault, G.4
  • 64
    • 0028955068 scopus 로고
    • The annexins: Specific markers of midline structures and sensory neurons in the developing murine central nervous system
    • Hamre, K. M., Chepenik, K. P., and Goldowitz, D. (1995) The annexins: specific markers of midline structures and sensory neurons in the developing murine central nervous system. J. Comp. Neurol. 352, 421-435.
    • (1995) J. Comp. Neurol. , vol.352 , pp. 421-435
    • Hamre, K.M.1    Chepenik, K.P.2    Goldowitz, D.3
  • 65
    • 0029898796 scopus 로고    scopus 로고
    • Cellular and subcellular localizations of annexins I, IV, and VI in lung epithelia
    • Mayran, N., Traverso, V., Maroux, S., and Massey Harroche, D. (1996) Cellular and subcellular localizations of annexins I, IV, and VI in lung epithelia. Am. J. Physiol. 270, L863-L871.
    • (1996) Am. J. Physiol. , vol.270
    • Mayran, N.1    Traverso, V.2    Maroux, S.3    Massey Harroche, D.4
  • 66
    • 0031023457 scopus 로고    scopus 로고
    • Expression and localization of annexin V and annexin VI during limb bud formation in the rat fetus
    • Rahman, M. M., Iida, H., and Shibata, Y. (1997) Expression and localization of annexin V and annexin VI during limb bud formation in the rat fetus. Anal. Embryol. Berlin 195, 31-39.
    • (1997) Anal. Embryol. Berlin , vol.195 , pp. 31-39
    • Rahman, M.M.1    Iida, H.2    Shibata, Y.3
  • 67
    • 0025139125 scopus 로고
    • Characterization of annexins in mammalian brain
    • Woolgar, J. A., Bousfead, C. M., and Walker, J. H. (1990) Characterization of annexins in mammalian brain. J. Neurochem. 54, 62-71.
    • (1990) J. Neurochem. , vol.54 , pp. 62-71
    • Woolgar, J.A.1    Bousfead, C.M.2    Walker, J.H.3
  • 71
    • 0024516466 scopus 로고
    • The EGF receptor kinase substrate p35 in the floor plate of the embryonic rat CNS
    • McKanna, J. A. and Cohen, S. (1989) The EGF receptor kinase substrate p35 in the floor plate of the embryonic rat CNS. Science 243, 1477-1479.
    • (1989) Science , vol.243 , pp. 1477-1479
    • McKanna, J.A.1    Cohen, S.2
  • 72
    • 0028145759 scopus 로고
    • The expression of different annexins in the fish embryo is developmentally regulated
    • Ivanenkov, V. V., Weber, K., and Gerke, V. (1994) The expression of different annexins in the fish embryo is developmentally regulated. FEBS Lett. 352, 227-230.
    • (1994) FEBS Lett. , vol.352 , pp. 227-230
    • Ivanenkov, V.V.1    Weber, K.2    Gerke, V.3
  • 73
    • 0023001104 scopus 로고
    • The tyrosine phosphorylation substrate p36 is developmentally regulated in embryonic avian limb and is induced in cell culture
    • Carter, C., Hewlett, A. R., Martin, G. S., and Bissell, M. J. (1986) The tyrosine phosphorylation substrate p36 is developmentally regulated in embryonic avian limb and is induced in cell culture. J. Cell. Biol. 103, 2017-2024.
    • (1986) J. Cell. Biol. , vol.103 , pp. 2017-2024
    • Carter, C.1    Hewlett, A.R.2    Martin, G.S.3    Bissell, M.J.4
  • 74
    • 0024517357 scopus 로고
    • Developmental regulation of calcium-binding proteins (calelectrins and calpactin I) in mammary glands
    • Lozano, J. J., Silberstein, G. B., Hwang, S., Haindl, A. H., and Rocha, V. (1989) Developmental regulation of calcium-binding proteins (calelectrins and calpactin I) in mammary glands. J. Cell. Physiol. 138, 503-510.
    • (1989) J. Cell. Physiol. , vol.138 , pp. 503-510
    • Lozano, J.J.1    Silberstein, G.B.2    Hwang, S.3    Haindl, A.H.4    Rocha, V.5
  • 75
    • 0025882865 scopus 로고
    • Structure of soluble and membrane-bound human annexin V
    • Brisson, A., Mosser, G., and Huber, R. (1991) Structure of soluble and membrane-bound human annexin V. J. Mol. Biol. 220, 199-203.
    • (1991) J. Mol. Biol. , vol.220 , pp. 199-203
    • Brisson, A.1    Mosser, G.2    Huber, R.3
  • 76
    • 0026724098 scopus 로고
    • A model of the structure of human annexin VI bound to lipid monolayers
    • Driessen, H. P., Newman, R. H., Freemont, P. S., and Crumpton, M. J. (1992) A model of the structure of human annexin VI bound to lipid monolayers. FEBS Lett. 306, 75-79.
    • (1992) FEBS Lett. , vol.306 , pp. 75-79
    • Driessen, H.P.1    Newman, R.H.2    Freemont, P.S.3    Crumpton, M.J.4
  • 77
    • 0030057046 scopus 로고    scopus 로고
    • Interactions of annexin V with phospholipid monolayers
    • Mukhopadhyay, S. and Cho, W. (1996) Interactions of annexin V with phospholipid monolayers. Biochim. Biophys. Acta 1279, 58-62.
    • (1996) Biochim. Biophys. Acta , vol.1279 , pp. 58-62
    • Mukhopadhyay, S.1    Cho, W.2
  • 78
    • 0028783371 scopus 로고
    • Ca(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V
    • Swairjo, M. A., Concha, N. O., Kaetzel, M. A., Dedman, J. R., and Seaton, B. A. (1995) Ca(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V. Nat. Struct. Biol. 2, 968-974.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 968-974
    • Swairjo, M.A.1    Concha, N.O.2    Kaetzel, M.A.3    Dedman, J.R.4    Seaton, B.A.5
  • 79
    • 0026439385 scopus 로고
    • A neutron solution scattering study of the structure of annexin-V and its binding to lipid vesicles
    • Ravanat, C., Torbet, J., and Freyssinet, J. M. (1992) A neutron solution scattering study of the structure of annexin-V and its binding to lipid vesicles. J. Mol. Biol. 226, 1271-1278.
    • (1992) J. Mol. Biol. , vol.226 , pp. 1271-1278
    • Ravanat, C.1    Torbet, J.2    Freyssinet, J.M.3
  • 80
    • 0030952278 scopus 로고    scopus 로고
    • Annexin V-mediated calcium flux across membranes is dependent on the lipid composition: Implications for cartilage mineralization
    • Kirsch, T., Nah, H. D., Demuth, D. R., Harrison, G., Golub, E. E., Adams, S. L., and Pacifici, M. (1997) Annexin V-mediated calcium flux across membranes is dependent on the lipid composition: implications for cartilage mineralization. Biochemistry 36, 3359-3367.
    • (1997) Biochemistry , vol.36 , pp. 3359-3367
    • Kirsch, T.1    Nah, H.D.2    Demuth, D.R.3    Harrison, G.4    Golub, E.E.5    Adams, S.L.6    Pacifici, M.7
  • 81
    • 0026473135 scopus 로고
    • Annexin V forms calcium-dependent trimeric units on phospholipid vesicles
    • Concha, N. O., Head, J. F., Kaetzel, M. A., Dedman, J. R., and Seaton, B. A. (1992) Annexin V forms calcium-dependent trimeric units on phospholipid vesicles. FEBS Lett. 314, 159-162.
    • (1992) FEBS Lett. , vol.314 , pp. 159-162
    • Concha, N.O.1    Head, J.F.2    Kaetzel, M.A.3    Dedman, J.R.4    Seaton, B.A.5
  • 82
    • 0026029142 scopus 로고
    • Subdomain structure of lipid-bound annexin-V resolved by electron image analysis
    • Mosser, G., Ravanat, C., Freyssinet, J. M., and Brisson, A. (1991) Subdomain structure of lipid-bound annexin-V resolved by electron image analysis. J. Mol. Biol. 217, 241-245.
    • (1991) J. Mol. Biol. , vol.217 , pp. 241-245
    • Mosser, G.1    Ravanat, C.2    Freyssinet, J.M.3    Brisson, A.4
  • 83
    • 0028260025 scopus 로고
    • Formation of two-dimensional arrays of annexin V on phosphatidylserine-containing liposomes
    • Pigault, C., Follenius Wund, A., Schmutz, M., Freyssinet, J. M., and Brisson, A. (1994) Formation of two-dimensional arrays of annexin V on phosphatidylserine-containing liposomes. J. Mol. Biol. 236, 199-208.
    • (1994) J. Mol. Biol. , vol.236 , pp. 199-208
    • Pigault, C.1    Follenius Wund, A.2    Schmutz, M.3    Freyssinet, J.M.4    Brisson, A.5
  • 84
    • 0028245914 scopus 로고
    • Three-dimensional structure of membrane-bound annexin V. A correlative electron microscopy-X-ray crystallography study
    • Voges, D., Berendes, R., Burger, A., Demange, P., Baumeister, W., and Huber, R. (1994) Three-dimensional structure of membrane-bound annexin V. A correlative electron microscopy-X-ray crystallography study. J. Mol. Biol. 238, 199-213.
    • (1994) J. Mol. Biol. , vol.238 , pp. 199-213
    • Voges, D.1    Berendes, R.2    Burger, A.3    Demange, P.4    Baumeister, W.5    Huber, R.6
  • 85
    • 0025195030 scopus 로고
    • Characterization of Ca2(+)-depcndent phospholipid binding, vesicle aggregation and membrane fusion by annexins
    • Blackwood, R. A. and Ernst, J. D. (1990) Characterization of Ca2(+)-depcndent phospholipid binding, vesicle aggregation and membrane fusion by annexins. Biochem. J. 266, 195-200.
    • (1990) Biochem. J. , vol.266 , pp. 195-200
    • Blackwood, R.A.1    Ernst, J.D.2
  • 86
    • 0028124991 scopus 로고
    • Salt dependency of chromaffin granule aggregation by annexin II tetramer
    • Jones, P. G., Fitzpatrick, S., and Waisman, D. M. (1994) Salt dependency of chromaffin granule aggregation by annexin II tetramer. Biochemistry 33, 13,751-13,760.
    • (1994) Biochemistry , vol.33 , pp. 13751-13760
    • Jones, P.G.1    Fitzpatrick, S.2    Waisman, D.M.3
  • 87
    • 0023226743 scopus 로고
    • Regulation of calpactin I phospholipid binding by calpactin I light-chain binding and phosphorylation by p60v-src
    • Powell, M. A. and Glenney, J. R. (1987) Regulation of calpactin I phospholipid binding by calpactin I light-chain binding and phosphorylation by p60v-src. Biochem. J. 247, 321-328.
    • (1987) Biochem. J. , vol.247 , pp. 321-328
    • Powell, M.A.1    Glenney, J.R.2
  • 88
    • 0030013509 scopus 로고    scopus 로고
    • Annexin II in exocytosis: Catecholamine secretion requires the translocation of p36 to the subplasmalemmal region in chromaffin cells
    • Chasserot Golaz, S., Vitale, N., Sagot, I., Delouche, B., Dirrig, S., Pradel, L. A., et al. (1996) Annexin II in exocytosis: catecholamine secretion requires the translocation of p36 to the subplasmalemmal region in chromaffin cells. J. Cell. Biol. 133, 1217-1236.
    • (1996) J. Cell. Biol. , vol.133 , pp. 1217-1236
    • Chasserot Golaz, S.1    Vitale, N.2    Sagot, I.3    Delouche, B.4    Dirrig, S.5    Pradel, L.A.6
  • 89
    • 0029948679 scopus 로고    scopus 로고
    • Translocation of annexin I to plasma membranes and phagosomes in human neutrophils upon stimulation with opsonized zymosan: Possible role in phagosome function
    • Kaufman, M., Leto, T., and Levy, R. (1996) Translocation of annexin I to plasma membranes and phagosomes in human neutrophils upon stimulation with opsonized zymosan: possible role in phagosome function. Biochem. J. 316, 35-42.
    • (1996) Biochem. J. , vol.316 , pp. 35-42
    • Kaufman, M.1    Leto, T.2    Levy, R.3
  • 90
    • 0028988997 scopus 로고
    • Ca2+ concentration during binding determines the manner in which annexin V binds to membranes
    • Trotter, P. J., Orchard, M. A., and Walker, J. H. (1995) Ca2+ concentration during binding determines the manner in which annexin V binds to membranes. Biochem, J. 308, 591-598.
    • (1995) Biochem, J. , vol.308 , pp. 591-598
    • Trotter, P.J.1    Orchard, M.A.2    Walker, J.H.3
  • 91
    • 0030033374 scopus 로고    scopus 로고
    • Annexins II, IV, V and VI relocate in response to rises in intracellular calcium in human foreskin fibroblasts
    • Barwise, J. L. and Walker, J. H. (1996) Annexins II, IV, V and VI relocate in response to rises in intracellular calcium in human foreskin fibroblasts. J. Cell. Sci. 109, 247-255.
    • (1996) J. Cell. Sci. , vol.109 , pp. 247-255
    • Barwise, J.L.1    Walker, J.H.2
  • 92
    • 0029384182 scopus 로고
    • Calcium-induced relocation of annexins IV and V in the human osteosarcoma cell line MG-63
    • Mohiti, J., Caswell, A. M., and Walker, J. H. (1995) Calcium-induced relocation of annexins IV and V in the human osteosarcoma cell line MG-63. Mol. Membr. Biol. 12, 321-329.
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 321-329
    • Mohiti, J.1    Caswell, A.M.2    Walker, J.H.3
  • 93
    • 0041396395 scopus 로고    scopus 로고
    • Translocation of annexin XI to neutrophil subcellular organelles
    • Sjolin, C., Movitz, C., Lundqvist, H., and Dahlgren, C. (1997) Translocation of annexin XI to neutrophil subcellular organelles. Biochim. Biophys. Acta 1326, 149-156.
    • (1997) Biochim. Biophys. Acta , vol.1326 , pp. 149-156
    • Sjolin, C.1    Movitz, C.2    Lundqvist, H.3    Dahlgren, C.4
  • 94
    • 0028321701 scopus 로고
    • Calcium-induced translocation of annexins to subcellular organelles of human neutrophils
    • Sjolin, C., Stendahl, O., and Dahlgren, C. (1994) Calcium-induced translocation of annexins to subcellular organelles of human neutrophils. Biochem. J. 300, 325-330.
    • (1994) Biochem. J. , vol.300 , pp. 325-330
    • Sjolin, C.1    Stendahl, O.2    Dahlgren, C.3
  • 95
    • 0026724197 scopus 로고
    • Differential recognition of secretory vesicles by annexins
    • European Molecular Biology Organization Course "Advanced Techniques for Studying Secretion"
    • Creutz, C. E., Moss, S., Edwardson, J. M., Hide, I., and Gomperts, B. (1992) Differential recognition of secretory vesicles by annexins. European Molecular Biology Organization Course "Advanced Techniques for Studying Secretion". Biochem. Biophys. Res. Commun. 184, 347-352.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 347-352
    • Creutz, C.E.1    Moss, S.2    Edwardson, J.M.3    Hide, I.4    Gomperts, B.5
  • 96
    • 0032564344 scopus 로고    scopus 로고
    • A transmembrane form of annexin XII detected by site-directed spin labeling
    • Langen, R., Isas, J. M., Hubbell, W. L., and Haigler, H. T. (1998) A transmembrane form of annexin XII detected by site-directed spin labeling. Proc. Natl. Acad. Sci. USA 95, 14,060-14,065.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14060-14065
    • Langen, R.1    Isas, J.M.2    Hubbell, W.L.3    Haigler, H.T.4
  • 97
    • 0031597411 scopus 로고    scopus 로고
    • Ca2+-independent interaction of annexin I with phospholipid monolayers
    • Rosengarth, A., Wintergalen, A., Galla, H. J., Hinz, H. J., and Gerke, V. (1998) Ca2+-independent interaction of annexin I with phospholipid monolayers. FEBS Lett. 438, 279-284.
    • (1998) FEBS Lett. , vol.438 , pp. 279-284
    • Rosengarth, A.1    Wintergalen, A.2    Galla, H.J.3    Hinz, H.J.4    Gerke, V.5
  • 98
    • 0028169739 scopus 로고
    • Ca(2+)-dependent binding of endonexin (annexin IV) to membranes: Analysis of the effects of membrane lipid composition and development of a predictive model for the binding interaction
    • Junker, M. and Creutz, C. E. (1994) Ca(2+)-dependent binding of endonexin (annexin IV) to membranes: analysis of the effects of membrane lipid composition and development of a predictive model for the binding interaction. Biochemistry 33, 8930-8940.
    • (1994) Biochemistry , vol.33 , pp. 8930-8940
    • Junker, M.1    Creutz, C.E.2
  • 99
    • 0027428023 scopus 로고
    • Endonexin (annexin IV)-mediated lateral segregation of phosphatidylglycerol in phosphatidylglycerol/phosphatidyl choline membranes
    • Junker, M. and Creutz, C. E. (1993) Endonexin (annexin IV)-mediated lateral segregation of phosphatidylglycerol in phosphatidylglycerol/phosphatidyl choline membranes. Biochemistry 32, 9968-9974.
    • (1993) Biochemistry , vol.32 , pp. 9968-9974
    • Junker, M.1    Creutz, C.E.2
  • 100
    • 0027396215 scopus 로고
    • Annexin I is phosphorylated in the multivesicular body during the processing of the epidermal growth factor receptor
    • Futter, C. E., Felder, S., Schlessinger, J., Ullrich, A., and Hopkins, C. R. (1993) Annexin I is phosphorylated in the multivesicular body during the processing of the epidermal growth factor receptor. J. Cell. Biol. 120, 77-83.
    • (1993) J. Cell. Biol. , vol.120 , pp. 77-83
    • Futter, C.E.1    Felder, S.2    Schlessinger, J.3    Ullrich, A.4    Hopkins, C.R.5
  • 101
    • 0030899412 scopus 로고    scopus 로고
    • Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol
    • Harder, T., Kellner, R., Parton, R. G., and Gruenberg, J. (1997) Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol. Mol. Biol. Cell 8, 533-545.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 533-545
    • Harder, T.1    Kellner, R.2    Parton, R.G.3    Gruenberg, J.4
  • 102
    • 0030996010 scopus 로고    scopus 로고
    • Annexin II binds to the membrane of A549 cells in a calcium-dependent and calcium-independent manner
    • Liu, L., Tao, J. Q., and Zimmerman, U. J. (1997) Annexin II binds to the membrane of A549 cells in a calcium-dependent and calcium-independent manner. Cell. Signal 9, 299-304.
    • (1997) Cell. Signal , vol.9 , pp. 299-304
    • Liu, L.1    Tao, J.Q.2    Zimmerman, U.J.3
  • 103
    • 0028935062 scopus 로고
    • EGTA-resistant binding of annexin V to platelet membranes can be induced by physiological calcium concentrations
    • Trotter, P. J., Orchard, M. A., and Walker, J. H. (1995) EGTA-resistant binding of annexin V to platelet membranes can be induced by physiological calcium concentrations. Biochem. Soc. Trans. 23, 37S.
    • (1995) Biochem. Soc. Trans. , vol.23
    • Trotter, P.J.1    Orchard, M.A.2    Walker, J.H.3
  • 104
    • 0030788666 scopus 로고    scopus 로고
    • Translocation of cytosolic annexin 2 to a triton-insoluble membrane subdomain upon nicotine stimulation of chromaffin cultured cells
    • Sagot, I., Regnouf, F., Henry, J. P., and Pradel, L. A. (1997) Translocation of cytosolic annexin 2 to a Triton-insoluble membrane subdomain upon nicotine stimulation of chromaffin cultured cells. FEBS Lett. 410, 229-234.
    • (1997) FEBS Lett. , vol.410 , pp. 229-234
    • Sagot, I.1    Regnouf, F.2    Henry, J.P.3    Pradel, L.A.4
  • 105
    • 0027426724 scopus 로고
    • The subcellular distribution of early endosomes is affected by the annexin II2p11(2) complex
    • Harder, T. and Gerke, V. (1993) The subcellular distribution of early endosomes is affected by the annexin II2p11(2) complex. J. Cell. Biol. 123, 1119-1132.
    • (1993) J. Cell. Biol. , vol.123 , pp. 1119-1132
    • Harder, T.1    Gerke, V.2
  • 106
    • 0025973207 scopus 로고
    • Membrane-specific association of annexin I and annexin II in anterior pituitary cells
    • Turgeon, J. L., Cooper, R. H., and Waring, D. W. (1991) Membrane-specific association of annexin I and annexin II in anterior pituitary cells. Endocrinology 128, 96-102.
    • (1991) Endocrinology , vol.128 , pp. 96-102
    • Turgeon, J.L.1    Cooper, R.H.2    Waring, D.W.3
  • 107
    • 0028008991 scopus 로고
    • The effects of PMA and TFP and alterations in intracellular pH and calcium concentration on the membrane associations of phospholipid-binding proteins fodrin, protein kinase C and annexin II in cultured MDCK cells
    • Vaaraniemi, J., Huotari, V., Lehto, V. P., and Eskelinen, S. (1994) The effects of PMA and TFP and alterations in intracellular pH and calcium concentration on the membrane associations of phospholipid-binding proteins fodrin, protein kinase C and annexin II in cultured MDCK cells. Biochim. Biophys. Acta 1189, 21-30.
    • (1994) Biochim. Biophys. Acta , vol.1189 , pp. 21-30
    • Vaaraniemi, J.1    Huotari, V.2    Lehto, V.P.3    Eskelinen, S.4
  • 108
    • 0028019458 scopus 로고
    • Fluorescent choleretic and cholestatic bile salts take different paths across the hepatocyte: Transcytosis of glycolithocholate leads to an extensive redistribution of annexin II
    • Wilton, J. C., Matthews, G. M., Burgoyne, R. D., Mills, C. O., Chipman, J. K., and Coleman, R. (1994) Fluorescent choleretic and cholestatic bile salts take different paths across the hepatocyte: transcytosis of glycolithocholate leads to an extensive redistribution of annexin II. J. Cell. Biol. 127, 401-410.
    • (1994) J. Cell. Biol. , vol.127 , pp. 401-410
    • Wilton, J.C.1    Matthews, G.M.2    Burgoyne, R.D.3    Mills, C.O.4    Chipman, J.K.5    Coleman, R.6
  • 109
    • 0030932943 scopus 로고    scopus 로고
    • Elementary and global aspects of calcium signalling
    • Berridge, M. J. (1997) Elementary and global aspects of calcium signalling. J. Physiol. 499, 291-306.
    • (1997) J. Physiol. , vol.499 , pp. 291-306
    • Berridge, M.J.1
  • 110
    • 0026575819 scopus 로고
    • Characterization and subcellular localization of calcium-dependent phospholipid binding proteins (annexins) in normal human skin and reconstituted epidermis
    • Culard, J. F., Basset Seguin, N., Calas, B., Guilhou, J. J., and Martin, F. (1992) Characterization and subcellular localization of calcium-dependent phospholipid binding proteins (annexins) in normal human skin and reconstituted epidermis. J. Invest. Dermatol. 98, 436-141.
    • (1992) J. Invest. Dermatol. , vol.98 , pp. 436-1141
    • Culard, J.F.1    Basset Seguin, N.2    Calas, B.3    Guilhou, J.J.4    Martin, F.5
  • 112
    • 0031000753 scopus 로고    scopus 로고
    • Domains of high Ca2+ beneath the plasma membrane of living A7r5 cells
    • Marsault, R., Murgia, M., Pozzan, T., and Rizzuto, R. (1997) Domains of high Ca2+ beneath the plasma membrane of living A7r5 cells. EMBO J. 16, 1575-1581.
    • (1997) EMBO J. , vol.16 , pp. 1575-1581
    • Marsault, R.1    Murgia, M.2    Pozzan, T.3    Rizzuto, R.4
  • 113
    • 0028354493 scopus 로고
    • Highly polarized expression of carbohydrate-binding protein p33/41 (annexin IV) on the apical plasma membrane of epithelial cells in renal proximal tubules
    • Kojima, K., Utsumi, H., Ogawa, H., and Matsumoto, I. (1994) Highly polarized expression of carbohydrate-binding protein p33/41 (annexin IV) on the apical plasma membrane of epithelial cells in renal proximal tubules. FEBS Lett. 342, 313-318.
    • (1994) FEBS Lett. , vol.342 , pp. 313-318
    • Kojima, K.1    Utsumi, H.2    Ogawa, H.3    Matsumoto, I.4
  • 114
    • 0026729505 scopus 로고
    • Annexin I and involucrin are cross-linked by particulate transglutaminase into the cornified cell envelope of squamous cell carcinoma Y1
    • Moore, K. G. and Sartorelli, A. C. (1992) Annexin I and involucrin are cross-linked by particulate transglutaminase into the cornified cell envelope of squamous cell carcinoma Y1. Exp. Cell. Res. 200, 186-195.
    • (1992) Exp. Cell. Res. , vol.200 , pp. 186-195
    • Moore, K.G.1    Sartorelli, A.C.2
  • 115
    • 0026795789 scopus 로고
    • Immunocytochemical localization of annexin V (CaBP33), a Ca(2+)-dependent phospholipid- and membrane-binding protein, in the rat nervous system and skeletal muscles and in the porcine heart
    • Spreca, A., Rambotti, M. G., Giambanco, I., Pula, G., Bianchi, R., Ceccarelli, P., and Donato, R. (1992) Immunocytochemical localization of annexin V (CaBP33), a Ca(2+)-dependent phospholipid- and membrane-binding protein, in the rat nervous system and skeletal muscles and in the porcine heart. J. Cell. Physiol. 152, 587-598.
    • (1992) J. Cell. Physiol. , vol.152 , pp. 587-598
    • Spreca, A.1    Rambotti, M.G.2    Giambanco, I.3    Pula, G.4    Bianchi, R.5    Ceccarelli, P.6    Donato, R.7
  • 117
    • 0026025795 scopus 로고
    • Calcium-induced intracellular cross-linking of lipocortin I by tissue transglutaminase in A431 cells. Augmentation by membrane phospholipids
    • Ando, Y., Imamura, S., Owada, M. K., and Kannagi, R. (1991) Calcium-induced intracellular cross-linking of lipocortin I by tissue transglutaminase in A431 cells. Augmentation by membrane phospholipids. J. Biol. Chem. 266, 1101-1108.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1101-1108
    • Ando, Y.1    Imamura, S.2    Owada, M.K.3    Kannagi, R.4
  • 119
    • 0038233899 scopus 로고    scopus 로고
    • Annexin V interaction with phosphatidylserine-containing vesicles at low and neutral pH
    • Kohler, G., Hering, U., Zschornig, O., and Arnold, K. (1997) Annexin V interaction with phosphatidylserine-containing vesicles at low and neutral pH. Biochemistry 36, 8189-8194.
    • (1997) Biochemistry , vol.36 , pp. 8189-8194
    • Kohler, G.1    Hering, U.2    Zschornig, O.3    Arnold, K.4
  • 120
    • 0031038664 scopus 로고    scopus 로고
    • Identification and characterization of a novel type of annexin-membrane interaction: Ca2+ is not required for the association of annexin II with early endosomes
    • Jost, M., Zeuschner, D., Seemann, J., Weber, K., and Gerke, V. (1997) Identification and characterization of a novel type of annexin-membrane interaction: Ca2+ is not required for the association of annexin II with early endosomes. J. Cell. Sci. 110, 221-228.
    • (1997) J. Cell. Sci. , vol.110 , pp. 221-228
    • Jost, M.1    Zeuschner, D.2    Seemann, J.3    Weber, K.4    Gerke, V.5
  • 121
    • 0023666546 scopus 로고
    • Synexin-mediated fusion of bovine chromaffin granule ghosts. Effect of pH
    • Stutzin, A., Cabantchik, Z. I., Lelkes, P. I., and Pollard, H. B. (1987) Synexin-mediated fusion of bovine chromaffin granule ghosts. Effect of pH. Biochim. Biophys. Acta 905, 205-212.
    • (1987) Biochim. Biophys. Acta , vol.905 , pp. 205-212
    • Stutzin, A.1    Cabantchik, Z.I.2    Lelkes, P.I.3    Pollard, H.B.4
  • 122
    • 0026344789 scopus 로고
    • Cellular and subcellular localization of annexin IV in rabbit intestinal epithelium, pancreas and liver
    • Massey, D., Traverso, V., Rigal, A., and Maroux, S. (1991) Cellular and subcellular localization of annexin IV in rabbit intestinal epithelium, pancreas and liver. Biol. Cell 73, 151-156.
    • (1991) Biol. Cell , vol.73 , pp. 151-156
    • Massey, D.1    Traverso, V.2    Rigal, A.3    Maroux, S.4
  • 123
    • 0031739687 scopus 로고    scopus 로고
    • Polarized localizations of annexins I, II, VI and XIII in epithelial cells of intestinal, hepatic and pancreatic tissues
    • Massey-Harroche, D., Mayran, N., and Maroux, S. (1998) Polarized localizations of annexins I, II, VI and XIII in epithelial cells of intestinal, hepatic and pancreatic tissues. J. Cell. Sci. 111, 3007-3015.
    • (1998) J. Cell. Sci. , vol.111 , pp. 3007-3015
    • Massey-Harroche, D.1    Mayran, N.2    Maroux, S.3
  • 124
    • 0026704114 scopus 로고
    • Immunodetection of annexins 1 and 2 in ciliated cells from quail oviduct
    • Chailley, B. and Pradel, L. A. (1992) Immunodetection of annexins 1 and 2 in ciliated cells from quail oviduct. Biol. Cell. 75, 45-54.
    • (1992) Biol. Cell. , vol.75 , pp. 45-54
    • Chailley, B.1    Pradel, L.A.2
  • 125
    • 0025844888 scopus 로고
    • Annexin II (calpactin I) in the mouse mammary gland: Immunolocalization by light- and electron microscopy
    • Handel, S. E., Rennison, M. E., Wilde, C. J., and Burgoyne, R. D. (1991) Annexin II (calpactin I) in the mouse mammary gland: immunolocalization by light- and electron microscopy. Cell. Tissue Res. 264, 549-554.
    • (1991) Cell. Tissue Res. , vol.264 , pp. 549-554
    • Handel, S.E.1    Rennison, M.E.2    Wilde, C.J.3    Burgoyne, R.D.4
  • 126
    • 0032555901 scopus 로고    scopus 로고
    • Annexin XIIIb associates with lipid microdomains to function in apical delivery
    • Lafont, F., Lecat, S., Verkade, P., and Simons, K. (1998) Annexin XIIIb Associates with lipid microdomains to function in apical delivery. J. Cell. Biol. 142, 1413-1427.
    • (1998) J. Cell. Biol. , vol.142 , pp. 1413-1427
    • Lafont, F.1    Lecat, S.2    Verkade, P.3    Simons, K.4
  • 127
    • 0030873897 scopus 로고    scopus 로고
    • Identification and characterization of two distinct intracellular GLUT4 pools in rat skeletal muscle: Evidence for an endosomal and an insulin-sensitive GLUT4 compartment
    • Aledo, J. C., Lavoie, L., Volchuk, A., Keller, S. R., Klip, A., and Hundal, H. S. (1997) Identification and characterization of two distinct intracellular GLUT4 pools in rat skeletal muscle: evidence for an endosomal and an insulin-sensitive GLUT4 compartment. Biochem. J. 325, 727-732.
    • (1997) Biochem. J. , vol.325 , pp. 727-732
    • Aledo, J.C.1    Lavoie, L.2    Volchuk, A.3    Keller, S.R.4    Klip, A.5    Hundal, H.S.6
  • 130
    • 0029565132 scopus 로고
    • Mobilization of annexin V during the uptake of DNP-albumin by human dendritic cells
    • Larsson, M., Majeed, M., Stendahl, O., Magnusson, K. E., Ernst, J. D., and Forsum, U. (1995) Mobilization of annexin V during the uptake of DNP-albumin by human dendritic cells. APMIS 103, 855-861.
    • (1995) APMIS , vol.103 , pp. 855-861
    • Larsson, M.1    Majeed, M.2    Stendahl, O.3    Magnusson, K.E.4    Ernst, J.D.5    Forsum, U.6
  • 131
    • 0029786326 scopus 로고    scopus 로고
    • The association of annexin I with early endosomes is regulated by Ca2+ and requires an intact N-terminal domain
    • Seemann, J., Weber, K., Osborn, M., Parton, R. G., and Gerke, V. (1996) The association of annexin I with early endosomes is regulated by Ca2+ and requires an intact N-terminal domain. Mol. Biol. Cell 7, 1359-1374.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1359-1374
    • Seemann, J.1    Weber, K.2    Osborn, M.3    Parton, R.G.4    Gerke, V.5
  • 134
  • 135
    • 0028871159 scopus 로고
    • Characterization and ultrastructural localization of annexin VI from mitochondria
    • Rainteau, D., Mansuelle, P., Rochat, H., and Weinman, S. (1995) Characterization and ultrastructural localization of annexin VI from mitochondria. FEBS Lett. 360, 80-84.
    • (1995) FEBS Lett. , vol.360 , pp. 80-84
    • Rainteau, D.1    Mansuelle, P.2    Rochat, H.3    Weinman, S.4
  • 136
    • 0026469159 scopus 로고
    • Immunocytochemical localization of 67 KD Ca2+ binding protein (p67) in ventricular, skeletal, and smooth muscle cells
    • Iida, H., Hatae, T., and Shibata, Y. (1992) Immunocytochemical localization of 67 KD Ca2+ binding protein (p67) in ventricular, skeletal, and smooth muscle cells. J. Histochem. Cytochem. 40, 1899-1907.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 1899-1907
    • Iida, H.1    Hatae, T.2    Shibata, Y.3
  • 137
    • 0030601934 scopus 로고    scopus 로고
    • Detection and localization of synexin (annexin VII) in Xenopus adult and embryonic tissues using an antibody to the Xenopus N-terminal PGQM repeat domain
    • Srivastava, M., Coping, G., Caohuy, H., McPhie, P., and Pollard, H. B. (1996) Detection and localization of synexin (annexin VII) in Xenopus adult and embryonic tissues using an antibody to the Xenopus N-terminal PGQM repeat domain. Exp. Cell. Res. 229, 14-19.
    • (1996) Exp. Cell. Res. , vol.229 , pp. 14-19
    • Srivastava, M.1    Coping, G.2    Caohuy, H.3    McPhie, P.4    Pollard, H.B.5
  • 138
    • 0028873518 scopus 로고
    • Expression and localization of annexin VII (synexin) in muscle cells
    • Selbert, S., Fischer, P., Pongratz, D., Stewart, M., and Noegel, A. A. (1995) Expression and localization of annexin VII (synexin) in muscle cells. J. Cell Sci. 108, 85-95.
    • (1995) J. Cell Sci. , vol.108 , pp. 85-95
    • Selbert, S.1    Fischer, P.2    Pongratz, D.3    Stewart, M.4    Noegel, A.A.5
  • 139
    • 0029400063 scopus 로고
    • Distribution of annexins I, II, and IV in bovine mammary gland
    • Katoh, N., Suzuki, T., Yuasa, A., and Miyamoto, T. (1995) Distribution of annexins I, II, and IV in bovine mammary gland. J. Dairy Sci. 78, 2382-2387.
    • (1995) J. Dairy Sci. , vol.78 , pp. 2382-2387
    • Katoh, N.1    Suzuki, T.2    Yuasa, A.3    Miyamoto, T.4
  • 140
    • 0026620763 scopus 로고
    • Nucleolar and cytoplasmic localization of annexin V
    • Sun, J., Salem, H. H., and Bird, P. (1992) Nucleolar and cytoplasmic localization of annexin V. FEBS Lett. 314, 425-429.
    • (1992) FEBS Lett. , vol.314 , pp. 425-429
    • Sun, J.1    Salem, H.H.2    Bird, P.3
  • 141
    • 0028558828 scopus 로고
    • Levels and localization of group II phospholipase A2 and annexin i in interleukin- and dexamethasone-treated rat mesangial cells: Evidence against annexin mediation of the dexamethasone-induced inhibition of group II phospholipases A2
    • Vervoordeldonk, M. J., Schalkwijk, C. G., Vishwanath, B. S., Aarsman, A. J., and van den Bosch, H. (1994) Levels and localization of group II phospholipase A2 and annexin I in interleukin- and dexamethasone-treated rat mesangial cells: evidence against annexin mediation of the dexamethasone-induced inhibition of group II phospholipases A2. Biochim. Biophys. Acta 1224, 541-550.
    • (1994) Biochim. Biophys. Acta , vol.1224 , pp. 541-550
    • Vervoordeldonk, M.J.1    Schalkwijk, C.G.2    Vishwanath, B.S.3    Aarsman, A.J.4    Van Den Bosch, H.5
  • 142
    • 0026502305 scopus 로고
    • The role of primer recognition proteins in DNA replication: Association with nuclear matrix in HeLa cells
    • Vishwanatha J. K., Jindal, H. K., and Davis, R. G. (1992) The role of primer recognition proteins in DNA replication: association with nuclear matrix in HeLa cells. J. Cell. Sci. 101, 25-34.
    • (1992) J. Cell. Sci. , vol.101 , pp. 25-34
    • Vishwanatha J, K.1    Jindal, H.K.2    Davis, R.G.3
  • 143
    • 0027931281 scopus 로고
    • Development-related and cell-type specific nuclear localization of annexin XI: Immunolocalization analysis in rat tissues
    • Mamiya, N., Iino, S., Mizutani, A., Kobayashi, S., and Hidaka, H. (1994) Development-related and cell-type specific nuclear localization of annexin XI: immunolocalization analysis in rat tissues. Biochem. Biophys. Res. Commun. 202, 403-409.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 403-409
    • Mamiya, N.1    Iino, S.2    Mizutani, A.3    Kobayashi, S.4    Hidaka, H.5
  • 144
    • 0028958652 scopus 로고
    • The long amino-terminal tail domain of annexin XI is necessary for its nuclear localization
    • Mizutani, A., Watanabe, N., Kitao, T., Tokumitsu, H., and Hidaka, H. (1995) The long amino-terminal tail domain of annexin XI is necessary for its nuclear localization. Arch. Biochem. Biophys. 318, 157-165.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 157-165
    • Mizutani, A.1    Watanabe, N.2    Kitao, T.3    Tokumitsu, H.4    Hidaka, H.5
  • 145
    • 0028633553 scopus 로고
    • Annexin II marks astrocytic brain tumors of high histologic grade
    • Roseman, B. J., Bollen, A., Hsu, J., Lamborn, K., and Israel, M. A. (1994) Annexin II marks astrocytic brain tumors of high histologic grade. Oncol. Res. 6, 561-567.
    • (1994) Oncol. Res. , vol.6 , pp. 561-567
    • Roseman, B.J.1    Bollen, A.2    Hsu, J.3    Lamborn, K.4    Israel, M.A.5
  • 146
    • 0027196072 scopus 로고
    • The sub-cellular localization of annexin V in cultured chick-embryo fibroblasts
    • Koster, J. J., Boustead, C. M., Middleton, C. A., and Walker, J. H. (1993) The sub-cellular localization of annexin V in cultured chick-embryo fibroblasts. Biochem. J. 291, 595-600.
    • (1993) Biochem. J. , vol.291 , pp. 595-600
    • Koster, J.J.1    Boustead, C.M.2    Middleton, C.A.3    Walker, J.H.4
  • 147
    • 0031563148 scopus 로고    scopus 로고
    • The nuclear location of annexin V in the human osteosarcoma cell line MG-63 depends on serum factors and tyrosine kinase signaling pathways
    • Mohiti, J., Caswell, A. M., and Walker, J. H. (1997) The nuclear location of annexin V in the human osteosarcoma cell line MG-63 depends on serum factors and tyrosine kinase signaling pathways. Exp. Cell. Res. 234, 98-104.
    • (1997) Exp. Cell. Res. , vol.234 , pp. 98-104
    • Mohiti, J.1    Caswell, A.M.2    Walker, J.H.3
  • 148
    • 0027162018 scopus 로고
    • Involvement of annexin II in DNA replication: Evidence from cell-free extracts of Xenopus eggs
    • Vishwanatha, J. K. and Kumble, S. (1993) Involvement of annexin II in DNA replication: evidence from cell-free extracts of Xenopus eggs. J. Cell. Sci. 105, 533-540.
    • (1993) J. Cell. Sci. , vol.105 , pp. 533-540
    • Vishwanatha, J.K.1    Kumble, S.2
  • 150
    • 0028102423 scopus 로고
    • Calpactin I binds to the glial fibrillary acidic protein (GFAP) and cosediments with glial filaments in a Ca(2+)-dependent manner: Implications for concerted regulatory effects of calpactin I and s100 protein on glial filaments
    • Bianchi, R., Garbuglia, M., Verzini, M., Giambanco, I., and Donato, R. (1994) Calpactin I binds to the glial fibrillary acidic protein (GFAP) and cosediments with glial filaments in a Ca(2+)-dependent manner: implications for concerted regulatory effects of calpactin I and S100 protein on glial filaments. Biochim. Biophys. Acta 1223, 361-367.
    • (1994) Biochim. Biophys. Acta , vol.1223 , pp. 361-367
    • Bianchi, R.1    Garbuglia, M.2    Verzini, M.3    Giambanco, I.4    Donato, R.5
  • 151
    • 0028237273 scopus 로고
    • Annexin VI-binding proteins in brain. Interaction of annexin VI with a membrane skeletal protein, calspectin (brain spectrin or fodrin)
    • Watanabe, T., Inui, M., Chen, B. Y., Iga, M., and Sobue, K. (1994) Annexin VI-binding proteins in brain. Interaction of annexin VI with a membrane skeletal protein, calspectin (brain spectrin or fodrin) J. Biol. Chem. 269, 17,656-17,662.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17656-17662
    • Watanabe, T.1    Inui, M.2    Chen, B.Y.3    Iga, M.4    Sobue, K.5
  • 152
    • 0026076023 scopus 로고
    • Actin-binding proteins involved in the capping of epidermal growth factor receptors in A431 cells
    • Kwiatkowska, K., Khrebtukova, I. A., Gudkova, D. A., Pinaev, G. P., and Sobota, A. (1991) Actin-binding proteins involved in the capping of epidermal growth factor receptors in A431 cells. Exp. Cell. Res. 196, 255-263.
    • (1991) Exp. Cell. Res. , vol.196 , pp. 255-263
    • Kwiatkowska, K.1    Khrebtukova, I.A.2    Gudkova, D.A.3    Pinaev, G.P.4    Sobota, A.5
  • 153
    • 0026708526 scopus 로고
    • Ca(2+)-regulated actin and phospholipid binding protein (68 kD-protein) from bovine liver: Identification as a homologue for annexin VI and intracellular localization
    • Hosoya, H., Kobayashi, R., Tsukita, S., and Matsumura, F. (1992) Ca(2+)-regulated actin and phospholipid binding protein (68 kD-protein) from bovine liver: identification as a homologue for annexin VI and intracellular localization. Cell. Motil. Cytoskeleton 22, 200-210.
    • (1992) Cell. Motil. Cytoskeleton , vol.22 , pp. 200-210
    • Hosoya, H.1    Kobayashi, R.2    Tsukita, S.3    Matsumura, F.4
  • 154
    • 0028221436 scopus 로고
    • In vitro modulation of filament bundling in F-actin and keratins by annexin II and calcium
    • Ma, A. S., Bystol, M. E., and Tranvan, A. (1994) In vitro modulation of filament bundling in F-actin and keratins by annexin II and calcium. In Vitro Cell. Dev. Biol. Anim. 30a, 329-335.
    • (1994) In Vitro Cell. Dev. Biol. Anim. , vol.30 A , pp. 329-335
    • Ma, A.S.1    Bystol, M.E.2    Tranvan, A.3
  • 155
    • 0028794049 scopus 로고
    • Plasma membrane caveolae mediate the efflux of cellular free cholesterol
    • Fielding, P. E. and Fielding, C. J. (1995) Plasma membrane caveolae mediate the efflux of cellular free cholesterol. Biochemistry 34, 14,288-14,292.
    • (1995) Biochemistry , vol.34 , pp. 14288-14292
    • Fielding, P.E.1    Fielding, C.J.2
  • 156
    • 0031570087 scopus 로고    scopus 로고
    • Host/pathogen interactions. Subversion of the mammalian cell cytoskeleton by invasive bacteria
    • Cossart, P. (1997) Host/pathogen interactions. Subversion of the mammalian cell cytoskeleton by invasive bacteria. J. Clin. Invest. 99, 2307-2311.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2307-2311
    • Cossart, P.1
  • 157
    • 0023648069 scopus 로고
    • Membrane capacity measurements suggest a calcium-dependent insertion of synexin into phosphatidylserine bilayers
    • Rojas, E. and Pollard, H. B. (1987) Membrane capacity measurements suggest a calcium-dependent insertion of synexin into phosphatidylserine bilayers. FEBS Lett. 217, 25-31.
    • (1987) FEBS Lett. , vol.217 , pp. 25-31
    • Rojas, E.1    Pollard, H.B.2
  • 158
    • 0024007049 scopus 로고
    • Ca2+-activated synexin forms highly selective, voltage-gated Ca2+ channels in phosphatidylserine bilayer membranes
    • Pollard, H. B. and Rojas, E. (1988) Ca2+-activated synexin forms highly selective, voltage-gated Ca2+ channels in phosphatidylserine bilayer membranes. Proc. Natl. Acad. Sci. USA 85, 2974-2978.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2974-2978
    • Pollard, H.B.1    Rojas, E.2
  • 159
    • 0025635905 scopus 로고
    • Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes
    • Rojas, E., Pollard, H. B., Haigler, H. T., Parra, C., and Burns, A. L. (1990) Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes. J. Biol. Chem. 265, 21,207-21,215.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21207-21215
    • Rojas, E.1    Pollard, H.B.2    Haigler, H.T.3    Parra, C.4    Burns, A.L.5
  • 161
    • 0026711047 scopus 로고
    • Calcium channel and membrane fusion activity of synexin and other members of the Annexin gene family
    • Pollard, H. B., Guy, H. R., Arispe, N., de la Fuente, M., Lee, G., Rojas, E. M., et al. (1992) Calcium channel and membrane fusion activity of synexin and other members of the Annexin gene family. Biophys. J. 62,15-18.
    • (1992) Biophys. J. , vol.62 , pp. 15-18
    • Pollard, H.B.1    Guy, H.R.2    Arispe, N.3    De La Fuente, M.4    Lee, G.5    Rojas, E.M.6
  • 162
    • 0028263779 scopus 로고
    • Structural and electrophysiological analysis of annexin V mutants. Mutagenesis of human annexin V, an in vitro voltage-gated calcium channel, provides information about the structural features of the ion pathway, the voltage sensor and the ion selectivity filter
    • Burger, A., Voges, D., Demange, P., Perez, C. R., Huber, R., and Berendes, R. (1994) Structural and electrophysiological analysis of annexin V mutants. Mutagenesis of human annexin V, an in vitro voltage-gated calcium channel, provides information about the structural features of the ion pathway, the voltage sensor and the ion selectivity filter. J. Mol. Biol. 237, 479-499.
    • (1994) J. Mol. Biol. , vol.237 , pp. 479-499
    • Burger, A.1    Voges, D.2    Demange, P.3    Perez, C.R.4    Huber, R.5    Berendes, R.6
  • 163
    • 0027514827 scopus 로고
    • Structure-function analysis of the ion channel selectivity filter in human annexin V
    • Berendes, R., Voges, D., Demange, P., Huber, R., and Burger, A. (1993) Structure-function analysis of the ion channel selectivity filter in human annexin V. Science 262, 427-430.
    • (1993) Science , vol.262 , pp. 427-430
    • Berendes, R.1    Voges, D.2    Demange, P.3    Huber, R.4    Burger, A.5
  • 164
    • 0029918683 scopus 로고    scopus 로고
    • Structural and functional characterisation of the voltage sensor in the ion channel human annexin V
    • Liemann, S., Benz, J., Burger, A., Voges, D., Hofmann, A., Huber, R., and Gottig, P. (1996) Structural and functional characterisation of the voltage sensor in the ion channel human annexin V. J. Mol. Biol. 258, 555-561.
    • (1996) J. Mol. Biol. , vol.258 , pp. 555-561
    • Liemann, S.1    Benz, J.2    Burger, A.3    Voges, D.4    Hofmann, A.5    Huber, R.6    Gottig, P.7
  • 165
    • 0030998465 scopus 로고    scopus 로고
    • Annexins and membrane dynamics
    • Gerke, V. and Moss, S. E. (1997) Annexins and membrane dynamics. Biochim. Biophyys. Acta 1357, 129-154.
    • (1997) Biochim. Biophyys. Acta , vol.1357 , pp. 129-154
    • Gerke, V.1    Moss, S.E.2
  • 167
    • 0030747302 scopus 로고    scopus 로고
    • Annexin XII forms calcium-dependent multimers in solution and on phospholipid bilayers: A chemical cross-linking study
    • Mailliard, W. S., Luecke, H., and Haigler, H. T. (1997) Annexin XII forms calcium-dependent multimers in solution and on phospholipid bilayers: a chemical cross-linking study. Biochemistry 36, 9045-9050.
    • (1997) Biochemistry , vol.36 , pp. 9045-9050
    • Mailliard, W.S.1    Luecke, H.2    Haigler, H.T.3
  • 169
    • 0030700864 scopus 로고    scopus 로고
    • Crystal structure of annexin V with its ligand K-201 as a calcium channel activity inhibitor
    • Kaneko, N., Ago, H., Matsuda, R., Inagaki, E., and Miyano, M. (1997) Crystal structure of annexin V with its ligand K-201 as a calcium channel activity inhibitor. J. Mol. Biol. 274, 16-20.
    • (1997) J. Mol. Biol. , vol.274 , pp. 16-20
    • Kaneko, N.1    Ago, H.2    Matsuda, R.3    Inagaki, E.4    Miyano, M.5
  • 170
    • 0026694106 scopus 로고
    • Establishment of the primary structure of the major lipid-dependent Ca2+ binding proteins of chicken growth plate cartilage matrix vesicles: Identity with anchorin CII (annexin V) and annexin II
    • Genge, B. R., Cao, X., Wu, L. N., Buzzi, W. R., Showman, R. W., Arsenault, A. L., Ishikawa, Y., and Wuthier, R. E. (1992) Establishment of the primary structure of the major lipid-dependent Ca2+ binding proteins of chicken growth plate cartilage matrix vesicles: identity with anchorin CII (annexin V) and annexin II. J. Bone. Miner. Res. 7, 807-819.
    • (1992) J. Bone. Miner. Res. , vol.7 , pp. 807-819
    • Genge, B.R.1    Cao, X.2    Wu, L.N.3    Buzzi, W.R.4    Showman, R.W.5    Arsenault, A.L.6    Ishikawa, Y.7    Wuthier, R.E.8
  • 171
    • 0027418277 scopus 로고
    • Involvement of cellular metabolism of calcium and phosphate in calcification of avian growth plate cartilage
    • Wuthier, R. E. (1993) Involvement of cellular metabolism of calcium and phosphate in calcification of avian growth plate cartilage. J. Nutr. 123, 301-309.
    • (1993) J. Nutr. , vol.123 , pp. 301-309
    • Wuthier, R.E.1
  • 172
    • 0030940202 scopus 로고    scopus 로고
    • Regulated production of mineralization-competent matrix vesicles in hypertrophic chondrocytes
    • Kirsch, T., Nah, H. D., Shapiro, I. M., and Pacifici, M. (1997) Regulated production of mineralization-competent matrix vesicles in hypertrophic chondrocytes. J. Cell. Biol. 137, 1149-1160.
    • (1997) J. Cell. Biol. , vol.137 , pp. 1149-1160
    • Kirsch, T.1    Nah, H.D.2    Shapiro, I.M.3    Pacifici, M.4
  • 173
    • 0029792781 scopus 로고    scopus 로고
    • Similarity in calcium channel activity of annexin V and matrix vesicles in planar lipid bilayers
    • Arispe, N., Rojas, E., Genge, B. R., Wu, L. N., and Wuthier, R. E. (1996) Similarity in calcium channel activity of annexin V and matrix vesicles in planar lipid bilayers. Biophys. J. 71, 1764-1775.
    • (1996) Biophys. J. , vol.71 , pp. 1764-1775
    • Arispe, N.1    Rojas, E.2    Genge, B.R.3    Wu, L.N.4    Wuthier, R.E.5
  • 177
    • 0030463881 scopus 로고    scopus 로고
    • Annexin VI modulates Ca2+ and K+ conductances of spinal cord and dorsal root ganglion neurons
    • Naciff, J. M., Behbehani, M. M., Kaetzel, M. A., and Dedman, J. R. (1996) Annexin VI modulates Ca2+ and K+ conductances of spinal cord and dorsal root ganglion neurons. Am. J. Physiol. 271, C2004-2015.
    • (1996) Am. J. Physiol. , vol.271
    • Naciff, J.M.1    Behbehani, M.M.2    Kaetzel, M.A.3    Dedman, J.R.4
  • 179
    • 0029850718 scopus 로고    scopus 로고
    • Annexin II modulates volume-activated chloride currents in vascular endothelial cells
    • Nilius, B., Gerke, V., Prenen, J., Szucs, G., Heinke, S., Weber, K., and Droogmans, G. (1996) Annexin II modulates volume-activated chloride currents in vascular endothelial cells. J. Biol. Chem. 271, 30,631-30,636.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30631-30636
    • Nilius, B.1    Gerke, V.2    Prenen, J.3    Szucs, G.4    Heinke, S.5    Weber, K.6    Droogmans, G.7
  • 181
    • 0028606906 scopus 로고
    • Annexin IV inhibits calmodulin-dependent protein kinase II-activated chloride conductance. A novel mechanism for ion channel regulation
    • Chan, H. C., Kaetzel, M. A., Gotter, A. L., Dedman, J. R., and Nelson, D. J. (1994) Annexin IV inhibits calmodulin-dependent protein kinase II-activated chloride conductance. A novel mechanism for ion channel regulation. J. Biol. Chem. 269, 32,464-32,468.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32464-32468
    • Chan, H.C.1    Kaetzel, M.A.2    Gotter, A.L.3    Dedman, J.R.4    Nelson, D.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.