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Volumn 11, Issue 6, 2013, Pages

Control of Cellular Bcl-xL Levels by Deamidation-Regulated Degradation

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINASE; ASPARTIC ACID; CALPAIN; CISPLATIN; CYCLOHEXIMIDE; ETOPOSIDE;

EID: 84879397353     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001588     Document Type: Article
Times cited : (30)

References (78)
  • 1
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: opposing activities that mediate cell death
    • Youle RJ, Strasser A, (2008) The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 9: 47-59.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 3
    • 33847328289 scopus 로고    scopus 로고
    • The Bcl-2 apoptotic switch in cancer development and therapy
    • Adams JM, Cory S, (2007) The Bcl-2 apoptotic switch in cancer development and therapy. Oncogene 26: 1324-1337.
    • (2007) Oncogene , vol.26 , pp. 1324-1337
    • Adams, J.M.1    Cory, S.2
  • 4
    • 0032471711 scopus 로고    scopus 로고
    • Moderate activation of the apoptosis inhibitor bcl-xL worsens the prognosis in pancreatic cancer
    • Friess H, Lu Z, Andren-Sandberg A, Berberat P, Zimmermann A, et al. (1998) Moderate activation of the apoptosis inhibitor bcl-xL worsens the prognosis in pancreatic cancer. Ann Surg 228: 780-787.
    • (1998) Ann Surg , vol.228 , pp. 780-787
    • Friess, H.1    Lu, Z.2    Andren-Sandberg, A.3    Berberat, P.4    Zimmermann, A.5
  • 5
    • 38049175034 scopus 로고    scopus 로고
    • Clinicopathological correlations of Bcl-xL and Bax expression in differentiated thyroid carcinoma
    • Martinez-Brocca MA, Castilla C, Navarro E, Amaya MJ, Travado P, et al. (2008) Clinicopathological correlations of Bcl-xL and Bax expression in differentiated thyroid carcinoma. Clin Endocrinol (Oxf) 68: 190-197.
    • (2008) Clin Endocrinol (Oxf) , vol.68 , pp. 190-197
    • Martinez-Brocca, M.A.1    Castilla, C.2    Navarro, E.3    Amaya, M.J.4    Travado, P.5
  • 6
    • 9144220128 scopus 로고    scopus 로고
    • Prognostic significance of bcl-xL gene expression and apoptotic cell counts in follicular lymphoma
    • Zhao WL, Daneshpouy ME, Mounier N, Briere J, Leboeuf C, et al. (2004) Prognostic significance of bcl-xL gene expression and apoptotic cell counts in follicular lymphoma. Blood 103: 695-697.
    • (2004) Blood , vol.103 , pp. 695-697
    • Zhao, W.L.1    Daneshpouy, M.E.2    Mounier, N.3    Briere, J.4    Leboeuf, C.5
  • 7
    • 34247880320 scopus 로고    scopus 로고
    • Expression of factors involved in regulation of DNA mismatch repair- and apoptosis pathways in ovarian cancer patients
    • Materna V, Surowiak P, Markwitz E, Spaczynski M, Drag-Zalesinska M, et al. (2007) Expression of factors involved in regulation of DNA mismatch repair- and apoptosis pathways in ovarian cancer patients. Oncol Rep 17: 505-516.
    • (2007) Oncol Rep , vol.17 , pp. 505-516
    • Materna, V.1    Surowiak, P.2    Markwitz, E.3    Spaczynski, M.4    Drag-Zalesinska, M.5
  • 8
    • 12344266609 scopus 로고    scopus 로고
    • Expression of Bcl-xL in ovarian carcinoma is associated with chemoresistance and recurrent disease
    • Williams J, Lucas PC, Griffith KA, Choi M, Fogoros S, et al. (2005) Expression of Bcl-xL in ovarian carcinoma is associated with chemoresistance and recurrent disease. Gynecol Oncol 96: 287-295.
    • (2005) Gynecol Oncol , vol.96 , pp. 287-295
    • Williams, J.1    Lucas, P.C.2    Griffith, K.A.3    Choi, M.4    Fogoros, S.5
  • 9
    • 3042585770 scopus 로고    scopus 로고
    • Prognostic significance of Bcl-xL in human hepatocellular carcinoma
    • Watanabe J, Kushihata F, Honda K, Sugita A, Tateishi N, et al. (2004) Prognostic significance of Bcl-xL in human hepatocellular carcinoma. Surgery 135: 604-612.
    • (2004) Surgery , vol.135 , pp. 604-612
    • Watanabe, J.1    Kushihata, F.2    Honda, K.3    Sugita, A.4    Tateishi, N.5
  • 10
    • 33748754286 scopus 로고    scopus 로고
    • Bcl-xL is overexpressed in hormone-resistant prostate cancer and promotes survival of LNCaP cells via interaction with proapoptotic Bak
    • Castilla C, Congregado B, Chinchon D, Torrubia FJ, Japon MA, et al. (2006) Bcl-xL is overexpressed in hormone-resistant prostate cancer and promotes survival of LNCaP cells via interaction with proapoptotic Bak. Endocrinology 147: 4960-4967.
    • (2006) Endocrinology , vol.147 , pp. 4960-4967
    • Castilla, C.1    Congregado, B.2    Chinchon, D.3    Torrubia, F.J.4    Japon, M.A.5
  • 11
    • 0035916363 scopus 로고    scopus 로고
    • Involvement of the hepatocyte growth factor/scatter factor receptor c-met and of Bcl-xL in the resistance of oropharyngeal cancer to ionizing radiation
    • Aebersold DM, Kollar A, Beer KT, Laissue J, Greiner RH, et al. (2001) Involvement of the hepatocyte growth factor/scatter factor receptor c-met and of Bcl-xL in the resistance of oropharyngeal cancer to ionizing radiation. Int J Cancer 96: 41-54.
    • (2001) Int J Cancer , vol.96 , pp. 41-54
    • Aebersold, D.M.1    Kollar, A.2    Beer, K.T.3    Laissue, J.4    Greiner, R.H.5
  • 12
    • 0034327411 scopus 로고    scopus 로고
    • An informatics approach identifying markers of chemosensitivity in human cancer cell lines
    • Amundson SA, Myers TG, Scudiero D, Kitada S, Reed JC, et al. (2000) An informatics approach identifying markers of chemosensitivity in human cancer cell lines. Cancer Res 60: 6101-6110.
    • (2000) Cancer Res , vol.60 , pp. 6101-6110
    • Amundson, S.A.1    Myers, T.G.2    Scudiero, D.3    Kitada, S.4    Reed, J.C.5
  • 13
    • 0028982183 scopus 로고
    • Expression of bcl-xL can confer a multidrug resistance phenotype
    • Minn AJ, Rudin CM, Boise LH, Thompson CB, (1995) Expression of bcl-xL can confer a multidrug resistance phenotype. Blood 86: 1903-1910.
    • (1995) Blood , vol.86 , pp. 1903-1910
    • Minn, A.J.1    Rudin, C.M.2    Boise, L.H.3    Thompson, C.B.4
  • 14
    • 33749016520 scopus 로고    scopus 로고
    • A small-molecule inhibitor of Bcl-XL potentiates the activity of cytotoxic drugs in vitro and in vivo
    • Shoemaker AR, Oleksijew A, Bauch J, Belli BA, Borre T, et al. (2006) A small-molecule inhibitor of Bcl-XL potentiates the activity of cytotoxic drugs in vitro and in vivo. Cancer Res 66: 8731-8739.
    • (2006) Cancer Res , vol.66 , pp. 8731-8739
    • Shoemaker, A.R.1    Oleksijew, A.2    Bauch, J.3    Belli, B.A.4    Borre, T.5
  • 15
    • 43949111975 scopus 로고    scopus 로고
    • Bcl-xL antisense oligonucleotide and cisplatin combination therapy extends survival in SCID mice with established mesothelioma xenografts
    • Littlejohn JE, Cao X, Miller SD, Ozvaran MK, Jupiter D, et al. (2008) Bcl-xL antisense oligonucleotide and cisplatin combination therapy extends survival in SCID mice with established mesothelioma xenografts. Int J Cancer 123: 202-208.
    • (2008) Int J Cancer , vol.123 , pp. 202-208
    • Littlejohn, J.E.1    Cao, X.2    Miller, S.D.3    Ozvaran, M.K.4    Jupiter, D.5
  • 16
    • 18644376568 scopus 로고    scopus 로고
    • Bcl-xL deamidation is a critical switch in the regulation of the response to DNA damage
    • Deverman BE, Cook BL, Manson SR, Niederhoff RA, Langer EM, et al. (2002) Bcl-xL deamidation is a critical switch in the regulation of the response to DNA damage. Cell 111: 51-62.
    • (2002) Cell , vol.111 , pp. 51-62
    • Deverman, B.E.1    Cook, B.L.2    Manson, S.R.3    Niederhoff, R.A.4    Langer, E.M.5
  • 17
    • 27644564949 scopus 로고    scopus 로고
    • A moderate reduction of Bcl-x(L) expression protects against tumorigenesis; however, it also increases susceptibility to tissue injury
    • Henderson CC, Zhang Z, Manson SR, Riehm JJ, Kataoka M, et al. (2005) A moderate reduction of Bcl-x(L) expression protects against tumorigenesis; however, it also increases susceptibility to tissue injury. Oncogene 24: 7120-7124.
    • (2005) Oncogene , vol.24 , pp. 7120-7124
    • Henderson, C.C.1    Zhang, Z.2    Manson, S.R.3    Riehm, J.J.4    Kataoka, M.5
  • 18
    • 0141630633 scopus 로고    scopus 로고
    • Antisense oligonucleotide inhibition of Bcl-xL and Bid expression in liver regulates responses in a mouse model of Fas-induced fulminant hepatitis
    • Zhang H, Taylor J, Luther D, Johnston J, Murray S, et al. (2003) Antisense oligonucleotide inhibition of Bcl-xL and Bid expression in liver regulates responses in a mouse model of Fas-induced fulminant hepatitis. J Pharmacol Exp Ther 307: 24-33.
    • (2003) J Pharmacol Exp Ther , vol.307 , pp. 24-33
    • Zhang, H.1    Taylor, J.2    Luther, D.3    Johnston, J.4    Murray, S.5
  • 19
    • 0032861255 scopus 로고    scopus 로고
    • Differential protective effects of Bcl-xL and Bcl-2 on apoptotic liver injury in transgenic mice
    • de la Coste A, Fabre M, McDonell N, Porteu A, Gilgenkrantz H, et al. (1999) Differential protective effects of Bcl-xL and Bcl-2 on apoptotic liver injury in transgenic mice. Am J Physiol 277: G702-G708.
    • (1999) Am J Physiol , vol.277
    • de la Coste, A.1    Fabre, M.2    McDonell, N.3    Porteu, A.4    Gilgenkrantz, H.5
  • 20
    • 0035021244 scopus 로고    scopus 로고
    • Expression of Bcl-2 family reduces apoptotic hepatocytes after excessive hepatectomy
    • Kamimukai N, Togo S, Hasegawa S, Kubota T, Kurosawa H, et al. (2001) Expression of Bcl-2 family reduces apoptotic hepatocytes after excessive hepatectomy. Eur Surg Res 33: 8-15.
    • (2001) Eur Surg Res , vol.33 , pp. 8-15
    • Kamimukai, N.1    Togo, S.2    Hasegawa, S.3    Kubota, T.4    Kurosawa, H.5
  • 21
    • 0030996170 scopus 로고    scopus 로고
    • Expression of Bcl-2 family during liver regeneration and identification of Bcl-x as a delayed early response gene
    • Tzung SP, Fausto N, Hockenbery DM, (1997) Expression of Bcl-2 family during liver regeneration and identification of Bcl-x as a delayed early response gene. Am J Pathol 150: 1985-1995.
    • (1997) Am J Pathol , vol.150 , pp. 1985-1995
    • Tzung, S.P.1    Fausto, N.2    Hockenbery, D.M.3
  • 22
    • 0142231979 scopus 로고    scopus 로고
    • Modification of insulin-like growth factor 1 receptor, c-Src, and Bcl-XL protein expression during the progression of Barrett's neoplasia
    • Iravani S, Zhang HQ, Yuan ZQ, Cheng JQ, Karl RC, et al. (2003) Modification of insulin-like growth factor 1 receptor, c-Src, and Bcl-XL protein expression during the progression of Barrett's neoplasia. Hum Pathol 34: 975-982.
    • (2003) Hum Pathol , vol.34 , pp. 975-982
    • Iravani, S.1    Zhang, H.Q.2    Yuan, Z.Q.3    Cheng, J.Q.4    Karl, R.C.5
  • 23
    • 1642430927 scopus 로고    scopus 로고
    • An oncogenic tyrosine kinase inhibits DNA repair and DNA-damage-induced Bcl-xL deamidation in T cell transformation
    • Zhao R, Yang FT, Alexander DR, (2004) An oncogenic tyrosine kinase inhibits DNA repair and DNA-damage-induced Bcl-xL deamidation in T cell transformation. Cancer Cell 5: 37-49.
    • (2004) Cancer Cell , vol.5 , pp. 37-49
    • Zhao, R.1    Yang, F.T.2    Alexander, D.R.3
  • 24
    • 33646337675 scopus 로고    scopus 로고
    • Involvement of Bcl-X(L) deamidation in E1A-mediated cisplatin sensitization of ovarian cancer cells
    • Chang CY, Lin YM, Lee WP, Hsu HH, Chen EI, (2006) Involvement of Bcl-X(L) deamidation in E1A-mediated cisplatin sensitization of ovarian cancer cells. Oncogene 25: 2656-2665.
    • (2006) Oncogene , vol.25 , pp. 2656-2665
    • Chang, C.Y.1    Lin, Y.M.2    Lee, W.P.3    Hsu, H.H.4    Chen, E.I.5
  • 25
    • 0035836730 scopus 로고    scopus 로고
    • Prediction of protein deamidation rates from primary and three-dimensional structure
    • Robinson NE, Robinson AB, (2001) Prediction of protein deamidation rates from primary and three-dimensional structure. Proc Natl Acad Sci U S A 98: 4367-4372.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 4367-4372
    • Robinson, N.E.1    Robinson, A.B.2
  • 26
    • 5244224827 scopus 로고    scopus 로고
    • X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death
    • Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, et al. (1996) X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Nature 381: 335-341.
    • (1996) Nature , vol.381 , pp. 335-341
    • Muchmore, S.W.1    Sattler, M.2    Liang, H.3    Meadows, R.P.4    Harlan, J.E.5
  • 31
    • 0032826179 scopus 로고    scopus 로고
    • Identifying DNA and protein patterns with statistically significant alignments of multiple sequences
    • Hertz GZ, Stormo GD, (1999) Identifying DNA and protein patterns with statistically significant alignments of multiple sequences. Bioinformatics 15: 563-577.
    • (1999) Bioinformatics , vol.15 , pp. 563-577
    • Hertz, G.Z.1    Stormo, G.D.2
  • 32
    • 54049125005 scopus 로고    scopus 로고
    • Discovering novel sequence motifs with MEME
    • Unit 2 4
    • Bailey TL, (2002) Discovering novel sequence motifs with MEME. Curr Protoc Bioinformatics Chapter 2: Unit 2 4.
    • (2002) Curr Protoc Bioinformatics Chapter , vol.2
    • Bailey, T.L.1
  • 34
    • 58149089846 scopus 로고    scopus 로고
    • Inhibition of the Bcl-xL deamidation pathway in myeloproliferative disorders
    • Zhao R, Follows GA, Beer PA, Scott LM, Huntly BJ, et al. (2008) Inhibition of the Bcl-xL deamidation pathway in myeloproliferative disorders. N Engl J Med 359: 2778-2789.
    • (2008) N Engl J Med , vol.359 , pp. 2778-2789
    • Zhao, R.1    Follows, G.A.2    Beer, P.A.3    Scott, L.M.4    Huntly, B.J.5
  • 35
    • 0038746592 scopus 로고    scopus 로고
    • Suppression of Bcl-xL deamidation in human hepatocellular carcinomas
    • Takehara T, Takahashi H, (2003) Suppression of Bcl-xL deamidation in human hepatocellular carcinomas. Cancer Res 63: 3054-3057.
    • (2003) Cancer Res , vol.63 , pp. 3054-3057
    • Takehara, T.1    Takahashi, H.2
  • 36
    • 10744232698 scopus 로고    scopus 로고
    • Erratum to: Bcl-xL deamidation is a critical switch in the regulation of the response to DNA damage
    • Deverman BE, Cook BL, Manson SR, Niederhoff RA, Langer EM, et al. (2003) Erratum to: Bcl-xL deamidation is a critical switch in the regulation of the response to DNA damage. Cell 115: 503.
    • (2003) Cell , vol.115 , pp. 503
    • Deverman, B.E.1    Cook, B.L.2    Manson, S.R.3    Niederhoff, R.A.4    Langer, E.M.5
  • 37
    • 33846356039 scopus 로고    scopus 로고
    • DNA damage-induced Bcl-xL deamidation is mediated by NHE-1 antiport regulated intracellular pH
    • doi: 10.1371/journal.pbio.0050001
    • Zhao R, Oxley D, Smith TS, Follows GA, Green AR, et al. (2006) DNA damage-induced Bcl-xL deamidation is mediated by NHE-1 antiport regulated intracellular pH. PLoS Biol 5: e1 doi:10.1371/journal.pbio.0050001.
    • (2006) PLoS Biol , vol.5
    • Zhao, R.1    Oxley, D.2    Smith, T.S.3    Follows, G.A.4    Green, A.R.5
  • 39
    • 0030822420 scopus 로고    scopus 로고
    • Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family
    • Aritomi M, Kunishima N, Inohara N, Ishibashi Y, Ohta S, et al. (1997) Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family. J Biol Chem 272: 27886-27892.
    • (1997) J Biol Chem , vol.272 , pp. 27886-27892
    • Aritomi, M.1    Kunishima, N.2    Inohara, N.3    Ishibashi, Y.4    Ohta, S.5
  • 40
    • 33845981493 scopus 로고    scopus 로고
    • PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-regulated Keap1-dependent ubiquitin ligase complex
    • Lo SC, Hannink M, (2006) PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-regulated Keap1-dependent ubiquitin ligase complex. J Biol Chem 281: 37893-37903.
    • (2006) J Biol Chem , vol.281 , pp. 37893-37903
    • Lo, S.C.1    Hannink, M.2
  • 41
    • 0842278331 scopus 로고    scopus 로고
    • Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis
    • Chipuk JE, Kuwana T, Bouchier-Hayes L, Droin NM, Newmeyer DD, et al. (2004) Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis. Science 303: 1010-1014.
    • (2004) Science , vol.303 , pp. 1010-1014
    • Chipuk, J.E.1    Kuwana, T.2    Bouchier-Hayes, L.3    Droin, N.M.4    Newmeyer, D.D.5
  • 43
    • 0037513376 scopus 로고    scopus 로고
    • p53 triggers apoptosis in oncogene-expressing fibroblasts by the induction of Noxa and mitochondrial Bax translocation
    • Schuler M, Maurer U, Goldstein JC, Breitenbucher F, Hoffarth S, et al. (2003) p53 triggers apoptosis in oncogene-expressing fibroblasts by the induction of Noxa and mitochondrial Bax translocation. Cell Death Differ 10: 451-460.
    • (2003) Cell Death Differ , vol.10 , pp. 451-460
    • Schuler, M.1    Maurer, U.2    Goldstein, J.C.3    Breitenbucher, F.4    Hoffarth, S.5
  • 44
    • 0033081618 scopus 로고    scopus 로고
    • Bcl-xL regulates apoptosis by heterodimerization-dependent and -independent mechanisms
    • Minn AJ, Kettlun CS, Liang H, Kelekar A, Vander Heiden MG, et al. (1999) Bcl-xL regulates apoptosis by heterodimerization-dependent and-independent mechanisms. EMBO J 18: 632-643.
    • (1999) EMBO J , vol.18 , pp. 632-643
    • Minn, A.J.1    Kettlun, C.S.2    Liang, H.3    Kelekar, A.4    Vander Heiden, M.G.5
  • 45
    • 1842332735 scopus 로고    scopus 로고
    • Bcl-x(L) forms an ion channel in synthetic lipid membranes
    • Minn AJ, Velez P, Schendel SL, Liang H, Muchmore SW, et al. (1997) Bcl-x(L) forms an ion channel in synthetic lipid membranes. Nature 385: 353-357.
    • (1997) Nature , vol.385 , pp. 353-357
    • Minn, A.J.1    Velez, P.2    Schendel, S.L.3    Liang, H.4    Muchmore, S.W.5
  • 47
    • 14944366436 scopus 로고    scopus 로고
    • In vitro maturation of nascent reticulocytes to erythrocytes
    • Koury MJ, Koury ST, Kopsombut P, Bondurant MC, (2005) In vitro maturation of nascent reticulocytes to erythrocytes. Blood 105: 2168-2174.
    • (2005) Blood , vol.105 , pp. 2168-2174
    • Koury, M.J.1    Koury, S.T.2    Kopsombut, P.3    Bondurant, M.C.4
  • 48
    • 52449094382 scopus 로고    scopus 로고
    • Protein isoaspartate methyltransferase prevents apoptosis induced by oxidative stress in endothelial cells: role of Bcl-Xl deamidation and methylation
    • doi: 10.1371/journal.pone.0003258
    • Cimmino A, Capasso R, Muller F, Sambri I, Masella L, et al. (2008) Protein isoaspartate methyltransferase prevents apoptosis induced by oxidative stress in endothelial cells: role of Bcl-Xl deamidation and methylation. PLoS One 3: e3258 doi:10.1371/journal.pone.0003258.
    • (2008) PLoS One , vol.3
    • Cimmino, A.1    Capasso, R.2    Muller, F.3    Sambri, I.4    Masella, L.5
  • 49
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M, Rogers SW, (1996) PEST sequences and regulation by proteolysis. Trends Biochem Sci 21: 267-271.
    • (1996) Trends Biochem Sci , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 50
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis
    • Rogers S, Wells R, Rechsteiner M, (1986) Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234: 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 51
    • 0023645302 scopus 로고
    • Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate
    • Thorsness PE, Koshland DE Jr, (1987) Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate. J Biol Chem 262: 10422-10425.
    • (1987) J Biol Chem , vol.262 , pp. 10422-10425
    • Thorsness, P.E.1    Koshland Jr., D.E.2
  • 52
    • 65949123582 scopus 로고    scopus 로고
    • Na+/H+ exchanger mediates TNF-alpha-induced hepatocyte apoptosis via the calpain-dependent degradation of Bcl-xL
    • Liu Z, Wang S, Zhou H, Yang Y, Zhang M, (2009) Na+/H+ exchanger mediates TNF-alpha-induced hepatocyte apoptosis via the calpain-dependent degradation of Bcl-xL. J Gastroenterol Hepatol 24: 879-885.
    • (2009) J Gastroenterol Hepatol , vol.24 , pp. 879-885
    • Liu, Z.1    Wang, S.2    Zhou, H.3    Yang, Y.4    Zhang, M.5
  • 53
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • Nakagawa T, Yuan J, (2000) Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol 150: 887-894.
    • (2000) J Cell Biol , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 55
    • 0141844589 scopus 로고    scopus 로고
    • Phosphorylation of a pest sequence in ABCA1 promotes calpain degradation and is reversed by ApoA-I
    • Martinez LO, Agerholm-Larsen B, Wang N, Chen W, Tall AR, (2003) Phosphorylation of a pest sequence in ABCA1 promotes calpain degradation and is reversed by ApoA-I. J Biol Chem 278: 37368-37374.
    • (2003) J Biol Chem , vol.278 , pp. 37368-37374
    • Martinez, L.O.1    Agerholm-Larsen, B.2    Wang, N.3    Chen, W.4    Tall, A.R.5
  • 56
    • 0033595636 scopus 로고    scopus 로고
    • The PEST domain of IkappaBalpha is necessary and sufficient for in vitro degradation by mu-calpain
    • Shumway SD, Maki M, Miyamoto S, (1999) The PEST domain of IkappaBalpha is necessary and sufficient for in vitro degradation by mu-calpain. J Biol Chem 274: 30874-30881.
    • (1999) J Biol Chem , vol.274 , pp. 30874-30881
    • Shumway, S.D.1    Maki, M.2    Miyamoto, S.3
  • 57
    • 0037253264 scopus 로고    scopus 로고
    • A PEST sequence in ABCA1 regulates degradation by calpain protease and stabilization of ABCA1 by apoA-I
    • Wang N, Chen W, Linsel-Nitschke P, Martinez LO, Agerholm-Larsen B, et al. (2003) A PEST sequence in ABCA1 regulates degradation by calpain protease and stabilization of ABCA1 by apoA-I. J Clin Invest 111: 99-107.
    • (2003) J Clin Invest , vol.111 , pp. 99-107
    • Wang, N.1    Chen, W.2    Linsel-Nitschke, P.3    Martinez, L.O.4    Agerholm-Larsen, B.5
  • 58
    • 0032505124 scopus 로고    scopus 로고
    • Acceleration of apoptotic cell death after the cleavage of Bcl-XL protein by caspase-3-like proteases
    • Fujita N, Nagahashi A, Nagashima K, Rokudai S, Tsuruo T, (1998) Acceleration of apoptotic cell death after the cleavage of Bcl-XL protein by caspase-3-like proteases. Oncogene 17: 1295-1304.
    • (1998) Oncogene , vol.17 , pp. 1295-1304
    • Fujita, N.1    Nagahashi, A.2    Nagashima, K.3    Rokudai, S.4    Tsuruo, T.5
  • 59
    • 33745826605 scopus 로고    scopus 로고
    • Ubiquitous calpains promote both apoptosis and survival signals in response to different cell death stimuli
    • Tan Y, Wu C, De Veyra T, Greer PA, (2006) Ubiquitous calpains promote both apoptosis and survival signals in response to different cell death stimuli. J Biol Chem 281: 17689-17698.
    • (2006) J Biol Chem , vol.281 , pp. 17689-17698
    • Tan, Y.1    Wu, C.2    De Veyra, T.3    Greer, P.A.4
  • 60
    • 0030048987 scopus 로고    scopus 로고
    • Apoptosis induced in Jurkat cells by several agents is preceded by intracellular acidification
    • Gottlieb RA, Nordberg J, Skowronski E, Babior BM, (1996) Apoptosis induced in Jurkat cells by several agents is preceded by intracellular acidification. Proc Natl Acad Sci U S A 93: 654-658.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 654-658
    • Gottlieb, R.A.1    Nordberg, J.2    Skowronski, E.3    Babior, B.M.4
  • 61
    • 0033776271 scopus 로고    scopus 로고
    • Changes in intramitochondrial and cytosolic pH: early events that modulate caspase activation during apoptosis
    • Matsuyama S, Llopis J, Deveraux QL, Tsien RY, Reed JC, (2000) Changes in intramitochondrial and cytosolic pH: early events that modulate caspase activation during apoptosis. Nat Cell Biol 2: 318-325.
    • (2000) Nat Cell Biol , vol.2 , pp. 318-325
    • Matsuyama, S.1    Llopis, J.2    Deveraux, Q.L.3    Tsien, R.Y.4    Reed, J.C.5
  • 62
    • 0028802545 scopus 로고
    • Effects of Na+/H+ antiport and intracellular pH in the regulation of HL-60 cell apoptosis
    • Zhu WH, Loh TT, (1995) Effects of Na+/H+ antiport and intracellular pH in the regulation of HL-60 cell apoptosis. Biochim Biophys Acta 1269: 122-128.
    • (1995) Biochim Biophys Acta , vol.1269 , pp. 122-128
    • Zhu, W.H.1    Loh, T.T.2
  • 63
    • 57049160417 scopus 로고    scopus 로고
    • Apoptosis-induced alkalinization by the Na+/H+ exchanger isoform 1 is mediated through phosphorylation of amino acids Ser726 and Ser729
    • Grenier AL, Abu-ihweij K, Zhang G, Ruppert SM, Boohaker R, et al. (2008) Apoptosis-induced alkalinization by the Na+/H+ exchanger isoform 1 is mediated through phosphorylation of amino acids Ser726 and Ser729. Am J Physiol Cell Physiol 295: C883-896.
    • (2008) Am J Physiol Cell Physiol , vol.295
    • Grenier, A.L.1    Abu-ihweij, K.2    Zhang, G.3    Ruppert, S.M.4    Boohaker, R.5
  • 64
    • 0030210268 scopus 로고    scopus 로고
    • Activation of the Na(+)/H(+) antiporter, Na+/HCO3(-)/CO3(2-) cotransporter, or Cl(-)/HCO3(-) exchanger in spontaneous thymocyte apoptosis
    • Tsao N, Lei HY, (1996) Activation of the Na(+)/H(+) antiporter, Na+/HCO3(-)/CO3(2-) cotransporter, or Cl(-)/HCO3(-) exchanger in spontaneous thymocyte apoptosis. J Immunol 157: 1107-1116.
    • (1996) J Immunol , vol.157 , pp. 1107-1116
    • Tsao, N.1    Lei, H.Y.2
  • 65
    • 0031820404 scopus 로고    scopus 로고
    • Increase of intracellular pH in p53-dependent apoptosis of thymocytes induced by gamma radiation
    • Dai HY, Tsao N, Leung WC, Lei HY, (1998) Increase of intracellular pH in p53-dependent apoptosis of thymocytes induced by gamma radiation. Radiat Res 150: 183-189.
    • (1998) Radiat Res , vol.150 , pp. 183-189
    • Dai, H.Y.1    Tsao, N.2    Leung, W.C.3    Lei, H.Y.4
  • 66
    • 0034780077 scopus 로고    scopus 로고
    • Trophic factor withdrawal: p38 mitogen-activated protein kinase activates NHE1, which induces intracellular alkalinization
    • Khaled AR, Moor AN, Li A, Kim K, Ferris DK, et al. (2001) Trophic factor withdrawal: p38 mitogen-activated protein kinase activates NHE1, which induces intracellular alkalinization. Mol Cell Biol 21: 7545-7557.
    • (2001) Mol Cell Biol , vol.21 , pp. 7545-7557
    • Khaled, A.R.1    Moor, A.N.2    Li, A.3    Kim, K.4    Ferris, D.K.5
  • 67
    • 1442265705 scopus 로고    scopus 로고
    • Identification of Na+/H+ exchange as a new target for toxic polycyclic aromatic hydrocarbons
    • Huc L, Sparfel L, Rissel M, Dimanche-Boitrel MT, Guillouzo A, et al. (2004) Identification of Na+/H+ exchange as a new target for toxic polycyclic aromatic hydrocarbons. Faseb J 18: 344-346.
    • (2004) Faseb J , vol.18 , pp. 344-346
    • Huc, L.1    Sparfel, L.2    Rissel, M.3    Dimanche-Boitrel, M.T.4    Guillouzo, A.5
  • 69
    • 0014408806 scopus 로고
    • Multiple forms of cytochrome c in the rat. Precursor-product relationship between the main component Cy I and the minor components Cy II and Cy III in vivo
    • Flatmark T, Sletten K, (1968) Multiple forms of cytochrome c in the rat. Precursor-product relationship between the main component Cy I and the minor components Cy II and Cy III in vivo. J Biol Chem 243: 1623-1629.
    • (1968) J Biol Chem , vol.243 , pp. 1623-1629
    • Flatmark, T.1    Sletten, K.2
  • 70
    • 0033548661 scopus 로고    scopus 로고
    • Deamidation and isoaspartate formation in smeared tau in paired helical filaments. Unusual properties of the microtubule-binding domain of tau
    • Watanabe A, Takio K, Ihara Y, (1999) Deamidation and isoaspartate formation in smeared tau in paired helical filaments. Unusual properties of the microtubule-binding domain of tau. J Biol Chem 274: 7368-7378.
    • (1999) J Biol Chem , vol.274 , pp. 7368-7378
    • Watanabe, A.1    Takio, K.2    Ihara, Y.3
  • 71
    • 0025151227 scopus 로고
    • The sequences of two peptides from cataract lenses suggest they arise by deamidation
    • Takemoto L, Emmons T, Granstrom D, (1990) The sequences of two peptides from cataract lenses suggest they arise by deamidation. Curr Eye Res 9: 793-797.
    • (1990) Curr Eye Res , vol.9 , pp. 793-797
    • Takemoto, L.1    Emmons, T.2    Granstrom, D.3
  • 72
    • 0041367295 scopus 로고    scopus 로고
    • Deamidation and isoaspartate formation in proteins: unwanted alterations or surreptitious signals?
    • Reissner KJ, Aswad DW, (2003) Deamidation and isoaspartate formation in proteins: unwanted alterations or surreptitious signals? Cell Mol Life Sci 60: 1281-1295.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1281-1295
    • Reissner, K.J.1    Aswad, D.W.2
  • 73
    • 0030271335 scopus 로고    scopus 로고
    • A question of balance: the role of cyclin-kinase inhibitors in development and tumorigenesis
    • Elledge SJ, Winston J, Harper JW, (1996) A question of balance: the role of cyclin-kinase inhibitors in development and tumorigenesis. Trends Cell Biol 6: 388-392.
    • (1996) Trends Cell Biol , vol.6 , pp. 388-392
    • Elledge, S.J.1    Winston, J.2    Harper, J.W.3
  • 74
    • 0016360069 scopus 로고
    • Deamidation of glutaminyl and asparaginyl residues in peptides and proteins
    • Robinson AB, Rudd CJ, (1974) Deamidation of glutaminyl and asparaginyl residues in peptides and proteins. Curr Top Cell Regul 8: 247-295.
    • (1974) Curr Top Cell Regul , vol.8 , pp. 247-295
    • Robinson, A.B.1    Rudd, C.J.2
  • 75
    • 0001155613 scopus 로고
    • A co-evolution theory of the genetic code
    • Wong JT, (1975) A co-evolution theory of the genetic code. Proc Natl Acad Sci U S A 72: 1909-1912.
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 1909-1912
    • Wong, J.T.1
  • 77
    • 0037385168 scopus 로고    scopus 로고
    • Transcription activation by the ecdysone receptor (EcR/USP): identification of activation functions
    • Hu X, Cherbas L, Cherbas P, (2003) Transcription activation by the ecdysone receptor (EcR/USP): identification of activation functions. Mol Endocrinol 17: 716-731.
    • (2003) Mol Endocrinol , vol.17 , pp. 716-731
    • Hu, X.1    Cherbas, L.2    Cherbas, P.3
  • 78
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: the European Molecular Biology Open Software Suite
    • Rice P, Longden I, Bleasby A, (2000) EMBOSS: the European Molecular Biology Open Software Suite. Trends Genet 16: 276-277.
    • (2000) Trends Genet , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3


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