메뉴 건너뛰기




Volumn 1863, Issue 6, 2016, Pages 1364-1378

ER functions of oncogenes and tumor suppressors: Modulators of intracellular Ca2+ signaling

Author keywords

Calcium; Cancer; Cell death; Endoplasmic reticulum; Oncogenes; Tumor suppressors

Indexed keywords

BECLIN 1; BRCA1 PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN BAK; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN BOK; PROTEIN KINASE B; PROTEIN MCL 1; PROTEIN P53; RAS PROTEIN; UNCLASSIFIED DRUG; CALCIUM; ONCOPROTEIN; TUMOR SUPPRESSOR PROTEIN;

EID: 84955515266     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2016.01.002     Document Type: Review
Times cited : (125)

References (187)
  • 1
  • 3
    • 0028283948 scopus 로고
    • Molecular and cellular physiology of intracellular calcium stores
    • Pozzan T., Rizzuto R., Volpe P., Meldolesi J. Molecular and cellular physiology of intracellular calcium stores. Physiol. Rev. 1994, 74(3):595-636.
    • (1994) Physiol. Rev. , vol.74 , Issue.3 , pp. 595-636
    • Pozzan, T.1    Rizzuto, R.2    Volpe, P.3    Meldolesi, J.4
  • 4
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham D.E. Calcium signaling. Cell 2007, 131(6):1047-1058.
    • (2007) Cell , vol.131 , Issue.6 , pp. 1047-1058
    • Clapham, D.E.1
  • 10
    • 84859884275 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate and its receptors
    • Parys J.B., De Smedt H. Inositol 1,4,5-trisphosphate and its receptors. Adv. Exp. Med. Biol. 2012, 740:255-279.
    • (2012) Adv. Exp. Med. Biol. , vol.740 , pp. 255-279
    • Parys, J.B.1    De Smedt, H.2
  • 12
    • 0026432666 scopus 로고
    • 3- and calcium-gated channels from endoplasmic reticulum of cerebellum
    • 3- and calcium-gated channels from endoplasmic reticulum of cerebellum. Nature 1991, 351:751-754.
    • (1991) Nature , vol.351 , pp. 751-754
    • Bezprozvanny, I.1    Watras, J.2    Ehrlich, B.E.3
  • 13
    • 0025890114 scopus 로고
    • Calcium as a coagonist of inositol 1,4,5-trisphosphate-induced calcium release
    • Finch E., Turner T., Goldin S. Calcium as a coagonist of inositol 1,4,5-trisphosphate-induced calcium release. Science 1991, 252:443-446.
    • (1991) Science , vol.252 , pp. 443-446
    • Finch, E.1    Turner, T.2    Goldin, S.3
  • 14
    • 0025193772 scopus 로고
    • 2+ release in smooth muscle cells of the guinea pig taenia caeci
    • 2+ release in smooth muscle cells of the guinea pig taenia caeci. J. Gen. Physiol. 1990, 95(6):1103-1122.
    • (1990) J. Gen. Physiol. , vol.95 , Issue.6 , pp. 1103-1122
    • Iino, M.1
  • 15
    • 34249930943 scopus 로고    scopus 로고
    • 3R) and its regulators: sometimes good and sometimes bad teamwork
    • 3R) and its regulators: sometimes good and sometimes bad teamwork. Sci. STKE 2006, 1-12.
    • (2006) Sci. STKE , pp. 1-12
    • Choe, C.U.1    Ehrlich, B.E.2
  • 17
    • 0026328450 scopus 로고
    • Effects of adenine nucleotides on inositol 1,4,5-trisphosphate-induced calcium release in vascular smooth muscle cells
    • Iino M. Effects of adenine nucleotides on inositol 1,4,5-trisphosphate-induced calcium release in vascular smooth muscle cells. J. Gen. Physiol. 1991, 98(4):681-698.
    • (1991) J. Gen. Physiol. , vol.98 , Issue.4 , pp. 681-698
    • Iino, M.1
  • 18
    • 0027210625 scopus 로고
    • ATP modulates the function of inositol 1,4,5-trisphosphate-gated channels at two sites
    • Bezprozvanny I., Ehrlich B.E. ATP modulates the function of inositol 1,4,5-trisphosphate-gated channels at two sites. Neuron 1993, 10(6):1175-1184.
    • (1993) Neuron , vol.10 , Issue.6 , pp. 1175-1184
    • Bezprozvanny, I.1    Ehrlich, B.E.2
  • 20
    • 52049124040 scopus 로고    scopus 로고
    • 2+ release by type-2 and type-3 inositol (1,4,5)-triphosphate receptors: differing ATP sensitivities and molecular determinants of action
    • 2+ release by type-2 and type-3 inositol (1,4,5)-triphosphate receptors: differing ATP sensitivities and molecular determinants of action. J. Biol. Chem. 2008, 283(31):21579-21587.
    • (2008) J. Biol. Chem. , vol.283 , Issue.31 , pp. 21579-21587
    • Betzenhauser, M.J.1    Wagner, L.E.2    Iwai, M.3    Michikawa, T.4    Mikoshiba, K.5    Yule, D.I.6
  • 21
    • 84896732956 scopus 로고    scopus 로고
    • The endoplasmic reticulum-mitochondria connection: one touch, multiple functions
    • Marchi S., Patergnani S., Pinton P. The endoplasmic reticulum-mitochondria connection: one touch, multiple functions. Biochim. Biophys. Acta Bioenerg. 2014, 1837(4):461-469.
    • (2014) Biochim. Biophys. Acta Bioenerg. , vol.1837 , Issue.4 , pp. 461-469
    • Marchi, S.1    Patergnani, S.2    Pinton, P.3
  • 24
    • 0942297436 scopus 로고    scopus 로고
    • The voltage-dependent anion channel: characterization, modulation, and role in mitochondrial function in cell life and death
    • Shoshan-Barmatz V., Gincel D. The voltage-dependent anion channel: characterization, modulation, and role in mitochondrial function in cell life and death. Cell Biochem. Biophys. 2003, 39(3):279-292.
    • (2003) Cell Biochem. Biophys. , vol.39 , Issue.3 , pp. 279-292
    • Shoshan-Barmatz, V.1    Gincel, D.2
  • 25
    • 84859780328 scopus 로고    scopus 로고
    • VDAC structure, selectivity, and dynamics
    • Colombini M. VDAC structure, selectivity, and dynamics. Biochim. Biophys. Acta Biomembr. 2012, 1818(6):1457-1465.
    • (2012) Biochim. Biophys. Acta Biomembr. , vol.1818 , Issue.6 , pp. 1457-1465
    • Colombini, M.1
  • 26
    • 84896718004 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter complex: molecular components, structure and physiopathological implications
    • Marchi S., Pinton P. The mitochondrial calcium uniporter complex: molecular components, structure and physiopathological implications. J. Physiol. 2014, 592(5):829-839.
    • (2014) J. Physiol. , vol.592 , Issue.5 , pp. 829-839
    • Marchi, S.1    Pinton, P.2
  • 34
    • 84905049169 scopus 로고    scopus 로고
    • Calcium trafficking integrates endoplasmic reticulum function with mitochondrial bioenergetics
    • Kaufman R.J., Malhotra J.D. Calcium trafficking integrates endoplasmic reticulum function with mitochondrial bioenergetics. Biochim. Biophys. Acta, Mol. Cell Res. 2014, 1843(10):2233-2239.
    • (2014) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1843 , Issue.10 , pp. 2233-2239
    • Kaufman, R.J.1    Malhotra, J.D.2
  • 39
    • 84953865828 scopus 로고    scopus 로고
    • ITPRs/inositol 1,4,5-trisphosphate receptors in autophagy: from enemy to ally
    • Decuypere J.P., Parys J.B., Bultynck G. ITPRs/inositol 1,4,5-trisphosphate receptors in autophagy: from enemy to ally. Autophagy 2015, 11(10):1944-1948.
    • (2015) Autophagy , vol.11 , Issue.10 , pp. 1944-1948
    • Decuypere, J.P.1    Parys, J.B.2    Bultynck, G.3
  • 40
    • 84925324913 scopus 로고    scopus 로고
    • Calcium homeostasis and ER stress in control of autophagy in cancer cells
    • Kania E., Pajak B., Orzechowski A. Calcium homeostasis and ER stress in control of autophagy in cancer cells. Biomed Res. Int. 2015, 2015:1-12.
    • (2015) Biomed Res. Int. , vol.2015 , pp. 1-12
    • Kania, E.1    Pajak, B.2    Orzechowski, A.3
  • 45
    • 79960759956 scopus 로고    scopus 로고
    • Calcium in tumour metastasis: new roles for known actors
    • Prevarskaya N., Skryma R., Shuba Y. Calcium in tumour metastasis: new roles for known actors. Nat. Rev. Cancer 2011, 11(8):609-618.
    • (2011) Nat. Rev. Cancer , vol.11 , Issue.8 , pp. 609-618
    • Prevarskaya, N.1    Skryma, R.2    Shuba, Y.3
  • 46
    • 42549164808 scopus 로고    scopus 로고
    • 2+ for cancer cell proliferation and survival
    • 2+ for cancer cell proliferation and survival. Nat. Rev. Cancer 2008, 8(5):361-375.
    • (2008) Nat. Rev. Cancer , vol.8 , Issue.5 , pp. 361-375
    • Roderick, H.L.1    Cook, S.J.2
  • 47
    • 84866367672 scopus 로고    scopus 로고
    • Calcium channels and pumps in cancer: changes and consequences
    • Monteith G.R., Davis F.M., Roberts-Thomson S.J. Calcium channels and pumps in cancer: changes and consequences. J. Biol. Chem. 2012, 287(38):31666-31673.
    • (2012) J. Biol. Chem. , vol.287 , Issue.38 , pp. 31666-31673
    • Monteith, G.R.1    Davis, F.M.2    Roberts-Thomson, S.J.3
  • 48
    • 84958583844 scopus 로고    scopus 로고
    • Oncogenic and oncosuppressive signal transduction at mitochondria-associated endoplasmic reticulum membranes
    • Marchi S., Giorgi C., Oparka M., Duszynski J., Wieckowski M.R., Pinton P. Oncogenic and oncosuppressive signal transduction at mitochondria-associated endoplasmic reticulum membranes. Mol. Cell. Oncol. 2014, 1(2).
    • (2014) Mol. Cell. Oncol. , vol.1 , Issue.2
    • Marchi, S.1    Giorgi, C.2    Oparka, M.3    Duszynski, J.4    Wieckowski, M.R.5    Pinton, P.6
  • 50
    • 84904982394 scopus 로고    scopus 로고
    • Bcl-2 regulation of the inositol 1,4,5-trisphosphate receptor and calcium signaling in normal and malignant lymphocytes: potential new target for cancer treatment
    • Greenberg E.F., Lavik A.R., Distelhorst C.W. Bcl-2 regulation of the inositol 1,4,5-trisphosphate receptor and calcium signaling in normal and malignant lymphocytes: potential new target for cancer treatment. Biochim. Biophys. Acta, Mol. Cell Res. 2014, 1843(10):2205-2210.
    • (2014) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1843 , Issue.10 , pp. 2205-2210
    • Greenberg, E.F.1    Lavik, A.R.2    Distelhorst, C.W.3
  • 51
    • 64849113485 scopus 로고
    • Control of mitochondrial apoptosis by the Bcl-2 family
    • Brunelle J.K., Letai A. Control of mitochondrial apoptosis by the Bcl-2 family. J. Cell Sci. 1993, 122(4):437-441.
    • (1993) J. Cell Sci. , vol.122 , Issue.4 , pp. 437-441
    • Brunelle, J.K.1    Letai, A.2
  • 55
    • 0021679848 scopus 로고
    • Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation
    • Tsujimoto Y., Finger L.R., Yunis J., Nowell P.C., Croce C.M. Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation. Science 1984, 226(4678):1097-1099.
    • (1984) Science , vol.226 , Issue.4678 , pp. 1097-1099
    • Tsujimoto, Y.1    Finger, L.R.2    Yunis, J.3    Nowell, P.C.4    Croce, C.M.5
  • 56
    • 84940868254 scopus 로고    scopus 로고
    • Inhibition of Bcl-2 sensitizes mitochondrial permeability transition pore (MPTP) opening in ischemia-damaged mitochondria
    • Chen Q., Xu H., Xu A., Ross T., Bowler E., Hu Y., Lesnefsky E.J. Inhibition of Bcl-2 sensitizes mitochondrial permeability transition pore (MPTP) opening in ischemia-damaged mitochondria. PLoS One 2015, 10(3).
    • (2015) PLoS One , vol.10 , Issue.3
    • Chen, Q.1    Xu, H.2    Xu, A.3    Ross, T.4    Bowler, E.5    Hu, Y.6    Lesnefsky, E.J.7
  • 58
    • 0000634556 scopus 로고
    • Variant translocation of the bcl-2 gene to immunoglobulin lambda light chain gene in chronic lymphocytic leukemia
    • Adachi M., Cossman J., Longo D., Croce C.M., Tsujimoto Y. Variant translocation of the bcl-2 gene to immunoglobulin lambda light chain gene in chronic lymphocytic leukemia. Proc. Natl. Acad. Sci. U. S. A. 1989, 86(8):2771-2774.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , Issue.8 , pp. 2771-2774
    • Adachi, M.1    Cossman, J.2    Longo, D.3    Croce, C.M.4    Tsujimoto, Y.5
  • 59
    • 0023918737 scopus 로고
    • The bcl-2 gene is rearranged in many diffuse B-cell lymphomas
    • Aisenberg A., Wilkes B., Jacobson J. The bcl-2 gene is rearranged in many diffuse B-cell lymphomas. Blood 1988, 71(4):969-972.
    • (1988) Blood , vol.71 , Issue.4 , pp. 969-972
    • Aisenberg, A.1    Wilkes, B.2    Jacobson, J.3
  • 60
    • 2642555698 scopus 로고    scopus 로고
    • The role of bcl-2 family members in non-small cell lung cancer
    • Daniel J.C., Smythe W.R. The role of bcl-2 family members in non-small cell lung cancer. Semin. Thorac. Cardiovasc. Surg. 2004, 16(1):19-27.
    • (2004) Semin. Thorac. Cardiovasc. Surg. , vol.16 , Issue.1 , pp. 19-27
    • Daniel, J.C.1    Smythe, W.R.2
  • 61
    • 0021821903 scopus 로고
    • Involvement of the Bcl-2 gene in human follicular lymphoma
    • Tsujimoto Y., Cossman J., Jaffe E., Croce C.M. Involvement of the Bcl-2 gene in human follicular lymphoma. Science 1985, 228(4706):1440-1443.
    • (1985) Science , vol.228 , Issue.4706 , pp. 1440-1443
    • Tsujimoto, Y.1    Cossman, J.2    Jaffe, E.3    Croce, C.M.4
  • 62
    • 34547854381 scopus 로고    scopus 로고
    • The role of microRNA and other non-coding RNA in the pathogenesis of chronic lymphocytic leukemia
    • Calin G.A., Pekarsky Y., Croce C.M. The role of microRNA and other non-coding RNA in the pathogenesis of chronic lymphocytic leukemia. Best Pract. Res. Clin. Haematol. 2007, 20(3):425-437.
    • (2007) Best Pract. Res. Clin. Haematol. , vol.20 , Issue.3 , pp. 425-437
    • Calin, G.A.1    Pekarsky, Y.2    Croce, C.M.3
  • 63
    • 0027239823 scopus 로고
    • Bcl-2 gene hypomethylation and high-level expression in B-cell chronic lymphocytic leukemia
    • Hanada M., Delia D., Aiello A., Stadtmauer E., Reed J.C. Bcl-2 gene hypomethylation and high-level expression in B-cell chronic lymphocytic leukemia. Blood 1993, 82(6):1820-1828.
    • (1993) Blood , vol.82 , Issue.6 , pp. 1820-1828
    • Hanada, M.1    Delia, D.2    Aiello, A.3    Stadtmauer, E.4    Reed, J.C.5
  • 72
    • 0344642938 scopus 로고    scopus 로고
    • Calcium-dependent interaction of calcineurin with Bcl-2 in neuronal tissue
    • Erin N., Bronson S.K., Billingsley M.L. Calcium-dependent interaction of calcineurin with Bcl-2 in neuronal tissue. Neuroscience 2003, 117(3):541-555.
    • (2003) Neuroscience , vol.117 , Issue.3 , pp. 541-555
    • Erin, N.1    Bronson, S.K.2    Billingsley, M.L.3
  • 73
    • 33846520546 scopus 로고    scopus 로고
    • 3-mediated calcium release and apoptosis by Bcl-2 involves the participation of protein phosphatase 1
    • 3-mediated calcium release and apoptosis by Bcl-2 involves the participation of protein phosphatase 1. Mol. Cell. Biochem. 2007, 295(1-2):153-165.
    • (2007) Mol. Cell. Biochem. , vol.295 , Issue.1-2 , pp. 153-165
    • Xu, L.1    Kong, D.2    Zhu, L.3    Zhu, W.4    Andrews, D.W.5    Kuo, T.H.6
  • 74
    • 84892910489 scopus 로고    scopus 로고
    • Feedback regulation mediated by Bcl-2 and DARPP-32 regulates inositol 1,4,5-trisphosphate receptor phosphorylation and promotes cell survival
    • Chang M.J., Zhong F., Lavik A.R., Parys J.B., Berridge M.J., Distelhorst C.W. Feedback regulation mediated by Bcl-2 and DARPP-32 regulates inositol 1,4,5-trisphosphate receptor phosphorylation and promotes cell survival. Proc. Natl. Acad. Sci. 2014, 111(3):1186-1191.
    • (2014) Proc. Natl. Acad. Sci. , vol.111 , Issue.3 , pp. 1186-1191
    • Chang, M.J.1    Zhong, F.2    Lavik, A.R.3    Parys, J.B.4    Berridge, M.J.5    Distelhorst, C.W.6
  • 75
    • 53549089861 scopus 로고    scopus 로고
    • Dual role of JNK1-mediated phosphorylation of Bcl-2 in autophagy and apoptosis regulation
    • Wei Y., Sinha S., Levine B. Dual role of JNK1-mediated phosphorylation of Bcl-2 in autophagy and apoptosis regulation. Autophagy 2008, 4(7):949-951.
    • (2008) Autophagy , vol.4 , Issue.7 , pp. 949-951
    • Wei, Y.1    Sinha, S.2    Levine, B.3
  • 77
    • 34547617018 scopus 로고    scopus 로고
    • Apoptosis regulation by Bcl-x(L) modulation of mammalian inositol 1,4,5-trisphosphate receptor channel isoform gating
    • Li C., Wang X., Vais H., Thompson C.B., Foskett J.K., White C. Apoptosis regulation by Bcl-x(L) modulation of mammalian inositol 1,4,5-trisphosphate receptor channel isoform gating. Proc. Natl. Acad. Sci. U. S. A. 2007, 104(30):12565-12570.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , Issue.30 , pp. 12565-12570
    • Li, C.1    Wang, X.2    Vais, H.3    Thompson, C.B.4    Foskett, J.K.5    White, C.6
  • 89
    • 84944462891 scopus 로고    scopus 로고
    • A synthetic peptide targeting the BH4 domain of Bcl-2 induces apoptosis in multiple myeloma and follicular lymphoma cells alone or in combination with agents targeting the BH3-binding pocket of Bcl-2
    • Lavik A., Zhong F., Chang M., Greenberg E., Choudhary Y., Smith M., McColl K., Pink J., Reu F., Matsuyama S., Distelhorst C. A synthetic peptide targeting the BH4 domain of Bcl-2 induces apoptosis in multiple myeloma and follicular lymphoma cells alone or in combination with agents targeting the BH3-binding pocket of Bcl-2. Oncotarget 2015, 6(29):27388-27402.
    • (2015) Oncotarget , vol.6 , Issue.29 , pp. 27388-27402
    • Lavik, A.1    Zhong, F.2    Chang, M.3    Greenberg, E.4    Choudhary, Y.5    Smith, M.6    McColl, K.7    Pink, J.8    Reu, F.9    Matsuyama, S.10    Distelhorst, C.11
  • 90
    • 85020324915 scopus 로고    scopus 로고
    • Synergistic killing of human small cell lung cancer cells by the Bcl-2-inositol 1,4,5-trisphosphate receptor disruptor BIRD-2 and the BH3-mimetic ABT-263
    • Greenberg E.F., McColl K.S., Zhong F., Wildey G., Dowlati A., Distelhorst C.W. Synergistic killing of human small cell lung cancer cells by the Bcl-2-inositol 1,4,5-trisphosphate receptor disruptor BIRD-2 and the BH3-mimetic ABT-263. Cell Death Dis. 2015, 6.
    • (2015) Cell Death Dis. , vol.6
    • Greenberg, E.F.1    McColl, K.S.2    Zhong, F.3    Wildey, G.4    Dowlati, A.5    Distelhorst, C.W.6
  • 92
    • 2342564508 scopus 로고    scopus 로고
    • Bcl-2 and calcium: controversy beneath the surface
    • Distelhorst C.W., Shore G.C. Bcl-2 and calcium: controversy beneath the surface. Oncogene 2004, 23(16):2875-2880.
    • (2004) Oncogene , vol.23 , Issue.16 , pp. 2875-2880
    • Distelhorst, C.W.1    Shore, G.C.2
  • 93
    • 0031993255 scopus 로고    scopus 로고
    • Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast
    • Xu Q., Reed J.C. Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast. Mol. Cell 1998, 1(3):337-346.
    • (1998) Mol. Cell , vol.1 , Issue.3 , pp. 337-346
    • Xu, Q.1    Reed, J.C.2
  • 96
    • 84894263970 scopus 로고    scopus 로고
    • TMBIM protein family: ancestral regulators of cell death
    • Rojas-Rivera D., Hetz C. TMBIM protein family: ancestral regulators of cell death. Oncogene 2015, 34(3):269-280.
    • (2015) Oncogene , vol.34 , Issue.3 , pp. 269-280
    • Rojas-Rivera, D.1    Hetz, C.2
  • 97
    • 45549102988 scopus 로고    scopus 로고
    • 2+ homeostasis downstream of Bcl-2 family proteins
    • 2+ homeostasis downstream of Bcl-2 family proteins. J. Biol. Chem. 2008, 283(17):11477-11484.
    • (2008) J. Biol. Chem. , vol.283 , Issue.17 , pp. 11477-11484
    • Xu, C.1    Xu, W.2    Palmer, A.E.3    Reed, J.C.4
  • 98
    • 0035941360 scopus 로고    scopus 로고
    • Transient expression of wild-type or mitochondrially targeted Bcl-2 induces apoptosis, whereas transient expression of endoplasmic reticulum-targeted Bcl-2 is protective against Bax-induced cell death
    • Wang N.S., Unkila M.T., Reineks E.Z., Distelhorst C.W. Transient expression of wild-type or mitochondrially targeted Bcl-2 induces apoptosis, whereas transient expression of endoplasmic reticulum-targeted Bcl-2 is protective against Bax-induced cell death. J. Biol. Chem. 2001, 276(47):44117-44128.
    • (2001) J. Biol. Chem. , vol.276 , Issue.47 , pp. 44117-44128
    • Wang, N.S.1    Unkila, M.T.2    Reineks, E.Z.3    Distelhorst, C.W.4
  • 99
    • 42549168101 scopus 로고    scopus 로고
    • The cellular concentration of Bcl-2 determines its pro- or anti-apoptotic effect
    • Hanson C.J., Bootman M.D., Distelhorst C.W., Maraldi T., Roderick H.L. The cellular concentration of Bcl-2 determines its pro- or anti-apoptotic effect. Cell Calcium 2008, 44(3):243-258.
    • (2008) Cell Calcium , vol.44 , Issue.3 , pp. 243-258
    • Hanson, C.J.1    Bootman, M.D.2    Distelhorst, C.W.3    Maraldi, T.4    Roderick, H.L.5
  • 101
    • 84934938163 scopus 로고    scopus 로고
    • Bcl-2 and FKBP12 bind to IP3 and ryanodine receptors at overlapping sites: the complexity of protein-protein interactions for channel regulation
    • Vervliet T., Parys J.B., Bultynck G. Bcl-2 and FKBP12 bind to IP3 and ryanodine receptors at overlapping sites: the complexity of protein-protein interactions for channel regulation. Biochem. Soc. Trans. 2015, 43(3):396-404.
    • (2015) Biochem. Soc. Trans. , vol.43 , Issue.3 , pp. 396-404
    • Vervliet, T.1    Parys, J.B.2    Bultynck, G.3
  • 102
  • 103
    • 80052001024 scopus 로고    scopus 로고
    • Functional SNP in the microRNA-367 binding site in the 3'UTR of the calcium channel ryanodine receptor gene 3 (RYR3) affects breast cancer risk and calcification
    • Zhang L., Liu Y., Song F., Zheng H., Hu L., Lu H., Liu P., Hao X., Zhang W., Chen K. Functional SNP in the microRNA-367 binding site in the 3'UTR of the calcium channel ryanodine receptor gene 3 (RYR3) affects breast cancer risk and calcification. Proc. Natl. Acad. Sci. 2011, 108(33):13653-13658.
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , Issue.33 , pp. 13653-13658
    • Zhang, L.1    Liu, Y.2    Song, F.3    Zheng, H.4    Hu, L.5    Lu, H.6    Liu, P.7    Hao, X.8    Zhang, W.9    Chen, K.10
  • 104
    • 84880910816 scopus 로고    scopus 로고
    • Assessment of gene expression of intracellular calcium channels, pumps and exchangers with epidermal growth factor-induced epithelial-mesenchymal transition in a breast cancer cell line
    • Davis F.M., Parsonage M.T., Cabot P.J., Parat M.O., Thompson E.W., Roberts-Thomson S.J., Monteith G.R. Assessment of gene expression of intracellular calcium channels, pumps and exchangers with epidermal growth factor-induced epithelial-mesenchymal transition in a breast cancer cell line. Cancer Cell Int. 2013, 13(1):76-83.
    • (2013) Cancer Cell Int. , vol.13 , Issue.1 , pp. 76-83
    • Davis, F.M.1    Parsonage, M.T.2    Cabot, P.J.3    Parat, M.O.4    Thompson, E.W.5    Roberts-Thomson, S.J.6    Monteith, G.R.7
  • 107
    • 84920129462 scopus 로고    scopus 로고
    • Bcl-xL overexpression and its association with the progress of tongue carcinoma
    • Zhang K., Jiao K., Xing Z., Zhang L., Yang J., Xie X., Yang L. Bcl-xL overexpression and its association with the progress of tongue carcinoma. Int. J. Clin. Exp. Pathol. 2014, 7(11):7360-7377.
    • (2014) Int. J. Clin. Exp. Pathol. , vol.7 , Issue.11 , pp. 7360-7377
    • Zhang, K.1    Jiao, K.2    Xing, Z.3    Zhang, L.4    Yang, J.5    Xie, X.6    Yang, L.7
  • 108
    • 0032510679 scopus 로고    scopus 로고
    • Drug resistance of human glioblastoma cells conferred by a tumor-specific mutant epidermal growth factor receptor through modulation of Bcl-XL and caspase-3-like proteases
    • Nagane M., Levitzki A., Gazit A., Cavenee W.K., Huang H.J. Drug resistance of human glioblastoma cells conferred by a tumor-specific mutant epidermal growth factor receptor through modulation of Bcl-XL and caspase-3-like proteases. Proc. Natl. Acad. Sci. U. S. A. 1998, 95(10):5724-5729.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , Issue.10 , pp. 5724-5729
    • Nagane, M.1    Levitzki, A.2    Gazit, A.3    Cavenee, W.K.4    Huang, H.J.5
  • 113
    • 0034724190 scopus 로고    scopus 로고
    • BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death
    • Shimizu S., Konishi A., Kodama T., Tsujimoto Y. BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death. Proc. Natl. Acad. Sci. U. S. A. 2000, 97(7):3100-3105.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , Issue.7 , pp. 3100-3105
    • Shimizu, S.1    Konishi, A.2    Kodama, T.3    Tsujimoto, Y.4
  • 115
    • 84863316405 scopus 로고    scopus 로고
    • Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein
    • Arbel N., Ben-Hail D., Shoshan-Barmatz V. Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein. J. Biol. Chem. 2012, 287(27):23152-23161.
    • (2012) J. Biol. Chem. , vol.287 , Issue.27 , pp. 23152-23161
    • Arbel, N.1    Ben-Hail, D.2    Shoshan-Barmatz, V.3
  • 118
  • 119
    • 47949126029 scopus 로고    scopus 로고
    • The anti-apoptotic Bcl-2 family member Mcl-1 promotes T lymphocyte survival at multiple stages
    • Dzhagalov I., Dunkle A., He Y.W. The anti-apoptotic Bcl-2 family member Mcl-1 promotes T lymphocyte survival at multiple stages. J. Immunol. 2008, 181(1):521-528.
    • (2008) J. Immunol. , vol.181 , Issue.1 , pp. 521-528
    • Dzhagalov, I.1    Dunkle, A.2    He, Y.W.3
  • 121
    • 13844319184 scopus 로고    scopus 로고
    • Obligate role of anti-apoptotic MCL-1 in the survival of hematopoietic stem cells obligate role of anti-apoptotic MCL-1 in the survival of hematopoietic stem cells
    • Opferman J.T., Iwasaki H., Ong C.C., Suh H., Mizuno S., Akashi K., Korsmeyer S.J. Obligate role of anti-apoptotic MCL-1 in the survival of hematopoietic stem cells obligate role of anti-apoptotic MCL-1 in the survival of hematopoietic stem cells. Science 2005, 307:1101-1104.
    • (2005) Science , vol.307 , pp. 1101-1104
    • Opferman, J.T.1    Iwasaki, H.2    Ong, C.C.3    Suh, H.4    Mizuno, S.5    Akashi, K.6    Korsmeyer, S.J.7
  • 123
    • 67349136004 scopus 로고    scopus 로고
    • Mcl-1 is a potential therapeutic target in multiple types of cancer
    • Akgul C. Mcl-1 is a potential therapeutic target in multiple types of cancer. Cell. Mol. Life Sci. 2009, 66(8):1326-1336.
    • (2009) Cell. Mol. Life Sci. , vol.66 , Issue.8 , pp. 1326-1336
    • Akgul, C.1
  • 125
    • 84918821230 scopus 로고    scopus 로고
    • Small molecule Mcl-1 inhibitors for the treatment of cancer
    • Belmar J., Fesik S.W. Small molecule Mcl-1 inhibitors for the treatment of cancer. Pharmacol. Ther. 2015, 145:76-84.
    • (2015) Pharmacol. Ther. , vol.145 , pp. 76-84
    • Belmar, J.1    Fesik, S.W.2
  • 127
  • 128
    • 0001003612 scopus 로고    scopus 로고
    • Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members
    • Hsu S.Y., Kaipia A., McGee E., Lomeli M., Hsueh A.J. Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members. Proc. Natl. Acad. Sci. U. S. A. 1997, 94(23):12401-12406.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , Issue.23 , pp. 12401-12406
    • Hsu, S.Y.1    Kaipia, A.2    McGee, E.3    Lomeli, M.4    Hsueh, A.J.5
  • 130
    • 84877579142 scopus 로고    scopus 로고
    • Intracellular localization of the BCL-2 family member BOK and functional implications
    • Echeverry N., Bachmann D., Ke F., Strasser A., Simon H.U., Kaufmann T. Intracellular localization of the BCL-2 family member BOK and functional implications. Cell Death Differ. 2013, 20(6):785-799.
    • (2013) Cell Death Differ. , vol.20 , Issue.6 , pp. 785-799
    • Echeverry, N.1    Bachmann, D.2    Ke, F.3    Strasser, A.4    Simon, H.U.5    Kaufmann, T.6
  • 131
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER
    • Lippincott-Schwartz J., Yuan L.C., Bonifacino J.S., Klausner R.D. Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 1989, 56(5):801-813.
    • (1989) Cell , vol.56 , Issue.5 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 132
    • 84931275602 scopus 로고    scopus 로고
    • BCL-2 family member BOK promotes apoptosis in response to endoplasmic reticulum stress
    • Carpio M.A., Michaud M., Zhou W., Fisher J.K., Walensky L.D., Katz S.G. BCL-2 family member BOK promotes apoptosis in response to endoplasmic reticulum stress. Proc. Natl. Acad. Sci. 2015, 112(23):7201-7206.
    • (2015) Proc. Natl. Acad. Sci. , vol.112 , Issue.23 , pp. 7201-7206
    • Carpio, M.A.1    Michaud, M.2    Zhou, W.3    Fisher, J.K.4    Walensky, L.D.5    Katz, S.G.6
  • 133
    • 84883403649 scopus 로고    scopus 로고
    • The Bcl-2 protein family member bok binds to the coupling domain of inositol 1,4,5-trisphosphate receptors and protects them from proteolytic cleavage
    • Schulman J.J., Wright F.A., Kaufmann T., Wojcikiewicz R.J.H. The Bcl-2 protein family member bok binds to the coupling domain of inositol 1,4,5-trisphosphate receptors and protects them from proteolytic cleavage. J. Biol. Chem. 2013, 288(35):25340-25349.
    • (2013) J. Biol. Chem. , vol.288 , Issue.35 , pp. 25340-25349
    • Schulman, J.J.1    Wright, F.A.2    Kaufmann, T.3    Wojcikiewicz, R.J.H.4
  • 134
    • 0033607673 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptor type 1 is a substrate for caspase-3 and is cleaved during apoptosis in a caspase-3-dependent manner
    • Hirota J., Furuichi T., Mikoshiba K. Inositol 1,4,5-trisphosphate receptor type 1 is a substrate for caspase-3 and is cleaved during apoptosis in a caspase-3-dependent manner. J. Biol. Chem. 1999, 274(48):34433-34437.
    • (1999) J. Biol. Chem. , vol.274 , Issue.48 , pp. 34433-34437
    • Hirota, J.1    Furuichi, T.2    Mikoshiba, K.3
  • 135
    • 5644261222 scopus 로고    scopus 로고
    • Caspase-3-induced truncation of type 1 inositol trisphosphate receptor accelerates apoptotic cell death and induces inositol trisphosphate-independent calcium release during apoptosis
    • Assefa Z., Bultynck G., Szlufcik K., Nadif Kasri N., Vermassen E., Goris J., Missiaen L., Callewaert G., Parys J.B., De Smedt H. Caspase-3-induced truncation of type 1 inositol trisphosphate receptor accelerates apoptotic cell death and induces inositol trisphosphate-independent calcium release during apoptosis. J. Biol. Chem. 2004, 279(41):43227-43236.
    • (2004) J. Biol. Chem. , vol.279 , Issue.41 , pp. 43227-43236
    • Assefa, Z.1    Bultynck, G.2    Szlufcik, K.3    Nadif Kasri, N.4    Vermassen, E.5    Goris, J.6    Missiaen, L.7    Callewaert, G.8    Parys, J.B.9    De Smedt, H.10
  • 137
    • 84904892288 scopus 로고    scopus 로고
    • 2+ homeostasis and developmental competence of mouse oocytes and eggs
    • 2+ homeostasis and developmental competence of mouse oocytes and eggs. J. Cell. Physiol. 2014, 229(11):1842-1854.
    • (2014) J. Cell. Physiol. , vol.229 , Issue.11 , pp. 1842-1854
    • Zhang, N.1    Fissore, R.A.2
  • 138
    • 84862577826 scopus 로고    scopus 로고
    • Type 1 inositol-1,4,5-trisphosphate receptor is a late substrate of caspases during apoptosis
    • Elkoreh G., Blais V., Béliveau É., Guillemette G., Denault J.B. Type 1 inositol-1,4,5-trisphosphate receptor is a late substrate of caspases during apoptosis. J. Cell. Biochem. 2012, 113(8):2775-2784.
    • (2012) J. Cell. Biochem. , vol.113 , Issue.8 , pp. 2775-2784
    • Elkoreh, G.1    Blais, V.2    Béliveau, É.3    Guillemette, G.4    Denault, J.B.5
  • 139
    • 84873523771 scopus 로고    scopus 로고
    • Caspase 3 cleavage of the inositol 1,4,5-trisphosphate receptor does not contribute to apoptotic calcium release
    • Akimzhanov A.M., Barral J.M., Boehning D. Caspase 3 cleavage of the inositol 1,4,5-trisphosphate receptor does not contribute to apoptotic calcium release. Cell Calcium 2013, 53(2):152-158.
    • (2013) Cell Calcium , vol.53 , Issue.2 , pp. 152-158
    • Akimzhanov, A.M.1    Barral, J.M.2    Boehning, D.3
  • 140
    • 84874598403 scopus 로고    scopus 로고
    • Beclin-1: autophagic regulator and therapeutic target in cancer
    • Fu L.L., Cheng Y., Liu B. Beclin-1: autophagic regulator and therapeutic target in cancer. Int. J. Biochem. Cell Biol. 2013, 45(5):921-924.
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , Issue.5 , pp. 921-924
    • Fu, L.L.1    Cheng, Y.2    Liu, B.3
  • 142
    • 79952628267 scopus 로고    scopus 로고
    • The beclin 1 network regulates autophagy and apoptosis
    • Kang R., Zeh H.J., Lotze M.T., Tang D. The beclin 1 network regulates autophagy and apoptosis. Cell Death Differ. 2011, 18(4):571-580.
    • (2011) Cell Death Differ. , vol.18 , Issue.4 , pp. 571-580
    • Kang, R.1    Zeh, H.J.2    Lotze, M.T.3    Tang, D.4
  • 143
    • 85117876522 scopus 로고    scopus 로고
    • Regulation of the autophagic bcl-2/beclin 1 interaction
    • Decuypere J.P., Parys J.B., Bultynck G. Regulation of the autophagic bcl-2/beclin 1 interaction. Cells 2012, 1(3):284-312.
    • (2012) Cells , vol.1 , Issue.3 , pp. 284-312
    • Decuypere, J.P.1    Parys, J.B.2    Bultynck, G.3
  • 144
    • 77951247552 scopus 로고    scopus 로고
    • Targeting cancer cells through autophagy for anticancer therapy
    • Turcotte S., Giaccia A.J. Targeting cancer cells through autophagy for anticancer therapy. Curr. Opin. Cell Biol. 2010, 22(2):246-251.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , Issue.2 , pp. 246-251
    • Turcotte, S.1    Giaccia, A.J.2
  • 151
    • 33645642577 scopus 로고    scopus 로고
    • Akt kinase phosphorylation of inositol 1,4,5-trisphosphate receptors
    • Khan M.T., Wagner L., Yule D.I., Bhanumathy C., Joseph S.K. Akt kinase phosphorylation of inositol 1,4,5-trisphosphate receptors. J. Biol. Chem. 2006, 281(6):3731-3737.
    • (2006) J. Biol. Chem. , vol.281 , Issue.6 , pp. 3731-3737
    • Khan, M.T.1    Wagner, L.2    Yule, D.I.3    Bhanumathy, C.4    Joseph, S.K.5
  • 155
    • 0033945128 scopus 로고    scopus 로고
    • Type 3 inositol 1,4,5-trisphosphate receptor modulates cell death
    • Hotchkiss R.S., Strasser A., Mcdunn J.E., Swanson P.E. Type 3 inositol 1,4,5-trisphosphate receptor modulates cell death. FASEB J. 2000, 14(10):1375-1379.
    • (2000) FASEB J. , vol.14 , Issue.10 , pp. 1375-1379
    • Hotchkiss, R.S.1    Strasser, A.2    Mcdunn, J.E.3    Swanson, P.E.4
  • 157
    • 0030973158 scopus 로고    scopus 로고
    • T cells deficient in inositol 1,4,5-trisphosphate receptor are resistant to apoptosis
    • Jayaraman T., Marks A.R. T cells deficient in inositol 1,4,5-trisphosphate receptor are resistant to apoptosis. Mol. Cell. Biol. 1997, 17(6):3005-3012.
    • (1997) Mol. Cell. Biol. , vol.17 , Issue.6 , pp. 3005-3012
    • Jayaraman, T.1    Marks, A.R.2
  • 159
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • Salomoni P., Pandolfi P.P. The role of PML in tumor suppression. Cell 2002, 108:165-170.
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 160
    • 44849143636 scopus 로고    scopus 로고
    • New insights into the role of PML in tumour suppression
    • Salomoni P., Ferguson B., Wyllie A., Rich T. New insights into the role of PML in tumour suppression. Cell Res. 2008, 18:622-640.
    • (2008) Cell Res. , vol.18 , pp. 622-640
    • Salomoni, P.1    Ferguson, B.2    Wyllie, A.3    Rich, T.4
  • 161
    • 80051770868 scopus 로고    scopus 로고
    • The role of PML in the control of apoptotic cell fate: a new key player at ER-mitochondria sites
    • Pinton P., Giorgi C., Pandolfi P.P. The role of PML in the control of apoptotic cell fate: a new key player at ER-mitochondria sites. Cell Death Differ. 2011, 18:1450-1456.
    • (2011) Cell Death Differ. , vol.18 , pp. 1450-1456
    • Pinton, P.1    Giorgi, C.2    Pandolfi, P.P.3
  • 162
    • 54249103056 scopus 로고    scopus 로고
    • Regulation of apoptosis by PML and the PML-NBs
    • Bernardi R., Papa A., Pandolfi P.P. Regulation of apoptosis by PML and the PML-NBs. Oncogene 2008, 27:6299-6312.
    • (2008) Oncogene , vol.27 , pp. 6299-6312
    • Bernardi, R.1    Papa, A.2    Pandolfi, P.P.3
  • 164
    • 84866256092 scopus 로고    scopus 로고
    • Mechanisms of BRCA1 tumor suppression
    • Silver D.P., Livingston D.M. Mechanisms of BRCA1 tumor suppression. Cancer Discov. 2012, 2:679-684.
    • (2012) Cancer Discov. , vol.2 , pp. 679-684
    • Silver, D.P.1    Livingston, D.M.2
  • 165
    • 84859565331 scopus 로고    scopus 로고
    • BRCA1 as tumor suppressor: lord without its RING?
    • Elia A.E., Elledge S.J. BRCA1 as tumor suppressor: lord without its RING?. Breast Cancer Res. 2012, 14(2):306.
    • (2012) Breast Cancer Res. , vol.14 , Issue.2 , pp. 306
    • Elia, A.E.1    Elledge, S.J.2
  • 166
    • 84938483489 scopus 로고    scopus 로고
    • CtIP: a DNA damage response protein at the intersection of DNA metabolism
    • Makharashvili N., Paull T.T. CtIP: a DNA damage response protein at the intersection of DNA metabolism. DNA Repair (Amst) 2015, 32:75-81.
    • (2015) DNA Repair (Amst) , vol.32 , pp. 75-81
    • Makharashvili, N.1    Paull, T.T.2
  • 168
    • 79952162878 scopus 로고    scopus 로고
    • Hereditary breast cancer and the BRCA1-associated FANCJ/BACH1/BRIP1
    • Cantor S.B., Guillemette S. Hereditary breast cancer and the BRCA1-associated FANCJ/BACH1/BRIP1. Future Oncol. 2011, 7(2):253-261.
    • (2011) Future Oncol. , vol.7 , Issue.2 , pp. 253-261
    • Cantor, S.B.1    Guillemette, S.2
  • 170
    • 84897731197 scopus 로고    scopus 로고
    • Tumor suppressor p53 and its gain-of-function mutants in cancer
    • Liu J., Zhang C., Feng Z. Tumor suppressor p53 and its gain-of-function mutants in cancer. Acta Biochim. Biophys. Sin. (Shanghai) 2014, 46(3):170-179.
    • (2014) Acta Biochim. Biophys. Sin. (Shanghai) , vol.46 , Issue.3 , pp. 170-179
    • Liu, J.1    Zhang, C.2    Feng, Z.3
  • 171
    • 84920189113 scopus 로고    scopus 로고
    • Tumor suppressor p53 and its mutants in cancer metabolism
    • Liu J., Zhang C., Hu W., Feng Z. Tumor suppressor p53 and its mutants in cancer metabolism. Cancer Lett. 2015, 356(2):197-203.
    • (2015) Cancer Lett. , vol.356 , Issue.2 , pp. 197-203
    • Liu, J.1    Zhang, C.2    Hu, W.3    Feng, Z.4
  • 174
    • 84928028767 scopus 로고    scopus 로고
    • Inside the tumor: p53 modulates calcium homeostasis
    • Giorgi C., Bonora M., Pinton P. Inside the tumor: p53 modulates calcium homeostasis. Cell Cycle 2015, 14(7):933-934.
    • (2015) Cell Cycle , vol.14 , Issue.7 , pp. 933-934
    • Giorgi, C.1    Bonora, M.2    Pinton, P.3
  • 176
    • 84930965672 scopus 로고    scopus 로고
    • Novel frontiers in calcium signaling: a possible target for chemotherapy
    • Bonora M., Giorgi C., Pinton P. Novel frontiers in calcium signaling: a possible target for chemotherapy. Pharmacol. Res. 2015, 99:82-85.
    • (2015) Pharmacol. Res. , vol.99 , pp. 82-85
    • Bonora, M.1    Giorgi, C.2    Pinton, P.3
  • 177
    • 84941637134 scopus 로고    scopus 로고
    • 2+ signaling from the endoplasmic reticulum: partners in anti-cancer therapies
    • 2+ signaling from the endoplasmic reticulum: partners in anti-cancer therapies. Oncoscience 2015, 2(3):233-238.
    • (2015) Oncoscience , vol.2 , Issue.3 , pp. 233-238
    • Bittremieux, M.1    Bultynck, G.2
  • 179
    • 33947594129 scopus 로고    scopus 로고
    • Hyperactive Ras in developmental disorders and cancer
    • Schubbert S., Shannon K., Bollag G. Hyperactive Ras in developmental disorders and cancer. Nat. Rev. Cancer 2007, 7:295-308.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 295-308
    • Schubbert, S.1    Shannon, K.2    Bollag, G.3
  • 180
    • 84896817172 scopus 로고    scopus 로고
    • Ras and autophagy in cancer development and therapy
    • Schmukler E., Kloog Y., Kramarski R.P. Ras and autophagy in cancer development and therapy. Oncotarget 2014, 5(3):577-586.
    • (2014) Oncotarget , vol.5 , Issue.3 , pp. 577-586
    • Schmukler, E.1    Kloog, Y.2    Kramarski, R.P.3
  • 181
    • 0027327282 scopus 로고
    • 2+ influx in voltage-clamped ras-transformed NIH/3 T3 fibroblasts
    • 2+ influx in voltage-clamped ras-transformed NIH/3 T3 fibroblasts. J. Biol. Chem. 1993, 268(26):19403-19410.
    • (1993) J. Biol. Chem. , vol.268 , Issue.26 , pp. 19403-19410
    • Hashii, M.1    Nozawa, Y.2    Higashida, H.3
  • 187
    • 84899965504 scopus 로고    scopus 로고
    • H-Ras-driven tumoral maintenance is sustained through caveolin-1-dependent alterations in calcium signaling
    • Rimessi A., Marchi S., Patergnani S., Pinton P. H-Ras-driven tumoral maintenance is sustained through caveolin-1-dependent alterations in calcium signaling. Oncogene 2014, 33(18):2329-2340.
    • (2014) Oncogene , vol.33 , Issue.18 , pp. 2329-2340
    • Rimessi, A.1    Marchi, S.2    Patergnani, S.3    Pinton, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.