메뉴 건너뛰기




Volumn 11, Issue 4, 2004, Pages 390-402

hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria

Author keywords

Apoptosis; Bax; CHOP; Molecular chaperone; Nitric oxide

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; CYTOCHROME C; ESCHERICHIA COLI LIPOPOLYSACCHARIDE; GAMMA INTERFERON; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; HEAT SHOCK PROTEIN 70; MUTANT PROTEIN; NITRIC OXIDE; PROTEIN BAX; PROTEIN BCL 2; PROTEIN DNAJ; PROTEIN DNAJ1; PROTEIN DNAJ2; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 1842843854     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401369     Document Type: Review
Times cited : (311)

References (59)
  • 2
    • 0031416664 scopus 로고    scopus 로고
    • Nitric oxide and apoptosis: Another paradigm for the double-edged role of nitric oxide
    • Dimmeler S and Zeiher AM (1997) Nitric oxide and apoptosis: another paradigm for the double-edged role of nitric oxide. Nitric Oxide 1: 275-281
    • (1997) Nitric Oxide , vol.1 , pp. 275-281
    • Dimmeler, S.1    Zeiher, A.M.2
  • 3
    • 0344936731 scopus 로고    scopus 로고
    • Nitric oxide: Cytotoxicity versus cytoprotection - How, why, when, and where?
    • Kröncke KD, Fehsel K and Kolb-Bachofen V (1997) Nitric oxide: cytotoxicity versus cytoprotection - how, why, when, and where? Nitric Oxide 1: 107-120
    • (1997) Nitric Oxide , vol.1 , pp. 107-120
    • Kröncke, K.D.1    Fehsel, K.2    Kolb-Bachofen, V.3
  • 4
    • 0036244305 scopus 로고    scopus 로고
    • Nitric oxide and cell signaling pathways in mitochondrial-dependent apoptosis
    • Boyd CS and Cadenas E (2002) Nitric oxide and cell signaling pathways in mitochondrial-dependent apoptosis. Biol. Chem. 383: 411-423
    • (2002) Biol. Chem. , vol.383 , pp. 411-423
    • Boyd, C.S.1    Cadenas, E.2
  • 6
    • 0035812912 scopus 로고    scopus 로고
    • Induction of CHOP and apoptosis by nitric oxide in p53-deficient microglial cells
    • Kawahara K, Oyadomari S, Gotoh T, Kohsaka S, Nakayama H and Mori M (2001) Induction of CHOP and apoptosis by nitric oxide in p53-deficient microglial cells. FEBS Lett. 506: 135-139
    • (2001) FEBS Lett. , vol.506 , pp. 135-139
    • Kawahara, K.1    Oyadomari, S.2    Gotoh, T.3    Kohsaka, S.4    Nakayama, H.5    Mori, M.6
  • 7
    • 0037023726 scopus 로고    scopus 로고
    • Nitric oxide-induced apoptosis in RAW 264.7 macrophages is mediated by endoplasmic reticulum stress pathway involving ATF6 and CHOP
    • Gotoh T, Oyadomari S, Mori K and Mori M (2002) Nitric oxide-induced apoptosis in RAW 264.7 macrophages is mediated by endoplasmic reticulum stress pathway involving ATF6 and CHOP. J. Biol. Chem. 277: 12343-12350
    • (2002) J. Biol. Chem. , vol.277 , pp. 12343-12350
    • Gotoh, T.1    Oyadomari, S.2    Mori, K.3    Mori, M.4
  • 8
    • 0032101239 scopus 로고    scopus 로고
    • The unfolded protein response: An intracellular signalling pathway with many surprising features
    • Sidrauski C, Chapman R and Walter P (1998) The unfolded protein response: an intracellular signalling pathway with many surprising features. Trends Cell Biol. 8: 245-249
    • (1998) Trends Cell Biol. , vol.8 , pp. 245-249
    • Sidrauski, C.1    Chapman, R.2    Walter, P.3
  • 10
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman RJ (1999) Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13: 1211-1233
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 11
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri KF and Kroemer G (2001) Organelle-specific initiation of cell death pathways. Nat. Cell Biol. 3: E255-E263
    • (2001) Nat. Cell Biol. , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 12
    • 0035966320 scopus 로고    scopus 로고
    • The unfolding tale of the unfolded protein response
    • Ma Y and Hendershot LM (2001) The unfolding tale of the unfolded protein response. Cell 107: 827-830
    • (2001) Cell , vol.107 , pp. 827-830
    • Ma, Y.1    Hendershot, L.M.2
  • 13
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H, Matsui T, Yamamoto A, Okada T and Mori K (2001) XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107: 881-891
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 15
    • 0037083755 scopus 로고    scopus 로고
    • IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response
    • Lee K, Tirasophon W, Shen X, Michalak M, Prywes R, Okada T, Yoshida H, Mori K and Kaufman RJ (2002) IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev. 16: 452-466
    • (2002) Genes Dev. , vol.16 , pp. 452-466
    • Lee, K.1    Tirasophon, W.2    Shen, X.3    Michalak, M.4    Prywes, R.5    Okada, T.6    Yoshida, H.7    Mori, K.8    Kaufman, R.J.9
  • 16
    • 0033118409 scopus 로고    scopus 로고
    • Complexes containing activating transcription factor (ATF)/cAMP-responsive-element-binding protein (CREB) interact with the CCAAT/enhancer-binding protein (C/EBP)-ATF composite siteto regulate Gadd153 expression during the stress response
    • Fawcett TW, Martindale JL, Guyton KZ, Hai T and Holbrook NJ (1999) Complexes containing activating transcription factor (ATF)/cAMP-responsive-element-binding protein (CREB) interact with the CCAAT/enhancer-binding protein (C/EBP)-ATF composite siteto regulate Gadd153 expression during the stress response. Biochem. J. 339: 135-141
    • (1999) Biochem. J. , vol.339 , pp. 135-141
    • Fawcett, T.W.1    Martindale, J.L.2    Guyton, K.Z.3    Hai, T.4    Holbrook, N.J.5
  • 17
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding HP, Novoa I, Zhang Y, Zeng H, Wek R, Schapira M and Ron D (2000) Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6: 1099-1108
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 18
    • 0030597160 scopus 로고    scopus 로고
    • Ectopic expression of CHOP (GADD153) induces apoptosis in M1 myeloblastic leukemia cells
    • Matsumoto M, Minami M, Takeda K, Sakao Y and Akira S (1996) Ectopic expression of CHOP (GADD153) induces apoptosis in M1 myeloblastic leukemia cells. FEBS Lett. 395: 143-147
    • (1996) FEBS Lett. , vol.395 , pp. 143-147
    • Matsumoto, M.1    Minami, M.2    Takeda, K.3    Sakao, Y.4    Akira, S.5
  • 20
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state
    • McCullough KD, Martindale JL, Klotz LO, Aw TY and Holbrook NJ (2001) Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol. Cell. Biol. 21: 1249-1259
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.O.3    Aw, T.Y.4    Holbrook, N.J.5
  • 21
    • 0032440847 scopus 로고    scopus 로고
    • Heat shock proteins: Regulators of stress response and apoptosis
    • Samali A and Orrenius S (1998) Heat shock proteins: regulators of stress response and apoptosis. Cell Stress Chaperones 3: 228-236
    • (1998) Cell Stress Chaperones , vol.3 , pp. 228-236
    • Samali, A.1    Orrenius, S.2
  • 22
    • 0032416104 scopus 로고    scopus 로고
    • Molecular chaperones: Biology and prospects for pharmacological intervention
    • Smith DF, Whitesell L and Katsanis E (1998) Molecular chaperones: biology and prospects for pharmacological intervention. Pharmacol. Rev. 50: 493-514
    • (1998) Pharmacol. Rev. , vol.50 , pp. 493-514
    • Smith, D.F.1    Whitesell, L.2    Katsanis, E.3
  • 23
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B and Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 24
    • 0030809270 scopus 로고    scopus 로고
    • Protein folding in vivo: Unraveling complex pathways
    • Johnson JL and Craig EA (1997) Protein folding in vivo: unraveling complex pathways. Cell 90: 201-204
    • (1997) Cell , vol.90 , pp. 201-204
    • Johnson, J.L.1    Craig, E.A.2
  • 25
    • 0032005026 scopus 로고    scopus 로고
    • Protein folding in the cytosol: Chaperonin-dependent and -independent mechanisms
    • Netzer WJ and Hartl FU (1998) Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms. Trends Biochem. Sci. 23: 68-73
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 68-73
    • Netzer, W.J.1    Hartl, F.U.2
  • 27
    • 0032103439 scopus 로고    scopus 로고
    • The J-domain family and the recruitment of chaperone power
    • Kelley WL (1998) The J-domain family and the recruitment of chaperone power. Trends Biochem Sci. 23: 222-227
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 222-227
    • Kelley, W.L.1
  • 28
    • 0030830249 scopus 로고    scopus 로고
    • The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding
    • Terada K, Kanazawa M, Bukau B and Mori M (1997) The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding. J. Cell Biol. 139: 1089-1095
    • (1997) J. Cell Biol. , vol.139 , pp. 1089-1095
    • Terada, K.1    Kanazawa, M.2    Bukau, B.3    Mori, M.4
  • 29
    • 0035042529 scopus 로고    scopus 로고
    • hsp70-DnaJ chaperone pairs prevent nitric oxide-mediated apoptosis in RAW 264.7 macrophages
    • Gotoh T, Terada K and Mori M (2001) hsp70-DnaJ chaperone pairs prevent nitric oxide-mediated apoptosis in RAW 264.7 macrophages. Cell Death Differ. 8: 357-366
    • (2001) Cell Death Differ. , vol.8 , pp. 357-366
    • Gotoh, T.1    Terada, K.2    Mori, M.3
  • 30
    • 0033535039 scopus 로고    scopus 로고
    • Arginase II downregulates nitric oxide (NO) production and prevents NO- mediated apoptosis in murine macrophage-derived RAW 264.7 cells
    • Gotoh T and Mori M (1999) Arginase II downregulates nitric oxide (NO) production and prevents NO- mediated apoptosis in murine macrophage-derived RAW 264.7 cells. J. Cell Biol. 144: 427-434
    • (1999) J. Cell Biol. , vol.144 , pp. 427-434
    • Gotoh, T.1    Mori, M.2
  • 31
    • 0033815971 scopus 로고    scopus 로고
    • ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
    • Yoshida H, Okada T, Haze K, Yanagi H, Yura T, Negishi M and Mori K (2000) ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol. Cell. Biol. 20: 6755-6767
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6755-6767
    • Yoshida, H.1    Okada, T.2    Haze, K.3    Yanagi, H.4    Yura, T.5    Negishi, M.6    Mori, K.7
  • 32
    • 2642689664 scopus 로고    scopus 로고
    • The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors
    • Demand J, Luders J and Hohfeld J (1998) The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors. Mol. Cell. Biol. 18: 2023-2028
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2023-2028
    • Demand, J.1    Luders, J.2    Hohfeld, J.3
  • 33
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY and Patterson C (1999) Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cell. Biol. 19: 4535-4545
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 34
    • 0030988405 scopus 로고    scopus 로고
    • HSDJ, a human homolog of DnaJ, is farnesylated and is involved in protein import into mitochondria
    • Kanazawa M, Terada K, Kato S and Mori M (1997) HSDJ, a human homolog of DnaJ, is farnesylated and is involved in protein import into mitochondria. J. Biochem. (Tokyo) 121: 890-895
    • (1997) J. Biochem. (Tokyo) , vol.121 , pp. 890-895
    • Kanazawa, M.1    Terada, K.2    Kato, S.3    Mori, M.4
  • 35
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang X (2001) The expanding role of mitochondria in apoptosis. Genes Dev. 15: 2922-2933
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 36
    • 0035890335 scopus 로고    scopus 로고
    • Damage-induced Bax N-terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate
    • Makin GW, Corfe BM, Griffiths GJ, Thistlethwaite A, Hickman JA and Dive C (2001) Damage-induced Bax N-terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate. EMBO J. 20: 6306-6315
    • (2001) EMBO J. , vol.20 , pp. 6306-6315
    • Makin, G.W.1    Corfe, B.M.2    Griffiths, G.J.3    Thistlethwaite, A.4    Hickman, J.A.5    Dive, C.6
  • 37
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR and Reed JC (1998) Mitochondria and apoptosis. Science 281: 1309-1312
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 38
    • 0035575679 scopus 로고    scopus 로고
    • Programmed cell death: Alive and well in the new millennium
    • Kaufmann SH and Hengartner MO (2001) Programmed cell death: alive and well in the new millennium. Trends Cell Biol. 11: 526-534
    • (2001) Trends Cell Biol. , vol.11 , pp. 526-534
    • Kaufmann, S.H.1    Hengartner, M.O.2
  • 40
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki M, Youle RJ and Tjandra N (2000) Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103: 645-654
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 42
    • 0032528118 scopus 로고    scopus 로고
    • Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis
    • Gross A, Jockel J, Wei MC and Korsmeyer SJ (1998) Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis. EMBO J. 17: 3878-3885
    • (1998) EMBO J. , vol.17 , pp. 3878-3885
    • Gross, A.1    Jockel, J.2    Wei, M.C.3    Korsmeyer, S.J.4
  • 43
    • 0035931765 scopus 로고    scopus 로고
    • Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells
    • Shimizu S, Matsuoka Y, Shinohara Y, Yoneda Y and Tsujimoto Y (2001) Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells. J. Cell Biol. 152: 237-250
    • (2001) J. Cell Biol. , vol.152 , pp. 237-250
    • Shimizu, S.1    Matsuoka, Y.2    Shinohara, Y.3    Yoneda, Y.4    Tsujimoto, Y.5
  • 44
    • 0039137646 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinases in S-nitrosoglutathione-induced macrophage apoptosis
    • Callsen D and Brüne B (1999) Role of mitogen-activated protein kinases in S-nitrosoglutathione-induced macrophage apoptosis. Biochemistry 38: 2279-2286
    • (1999) Biochemistry , vol.38 , pp. 2279-2286
    • Callsen, D.1    Brüne, B.2
  • 45
    • 0033559903 scopus 로고    scopus 로고
    • Overexpression of protein kinase C isoforms protects RAW 264.7 macrophages from nitric oxide-induced apoptosis: Involvement of c-Jun N-terminal kinase/stress-activated protein kinase, p38 kinase, and CPP-32 protease pathways
    • Jun CD, Oh CD, Kwak HJ, Pae HO, Yoo JC, Choi BM, Chun JS, Park RK and Chung HT (1999) Overexpression of protein kinase C isoforms protects RAW 264.7 macrophages from nitric oxide-induced apoptosis: involvement of c-Jun N-terminal kinase/stress-activated protein kinase, p38 kinase, and CPP-32 protease pathways. J. Immunol. 162: 3395-3401
    • (1999) J. Immunol. , vol.162 , pp. 3395-3401
    • Jun, C.D.1    Oh, C.D.2    Kwak, H.J.3    Pae, H.O.4    Yoo, J.C.5    Choi, B.M.6    Chun, J.S.7    Park, R.K.8    Chung, H.T.9
  • 46
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong WX, Lindsten T, Ross AJ, MacGregor GR and Thompson CB (2001) BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev. 15: 1481-1486
    • (2001) Genes Dev. , vol.15 , pp. 1481-1486
    • Zong, W.X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5
  • 48
    • 0035182221 scopus 로고    scopus 로고
    • Stress management-heat shock protein-70 and the regulation of apoptosis
    • Beere HM and Green R (2001) Stress management-heat shock protein-70 and the regulation of apoptosis. Trends Cell Biol. 11: 6-10
    • (2001) Trends Cell Biol. , vol.11 , pp. 6-10
    • Beere, H.M.1    Green, R.2
  • 50
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis
    • Mosser DD, Caron AW, Bourget L, Denis-Larose C and Massie B (1997) Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol. Cell. Biol. 17: 5317-5327
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5317-5327
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 52
    • 0036234472 scopus 로고    scopus 로고
    • Hsp72 and stress kinase c-jun N-terminal kinase regulate the bid-dependent pathway in tumor necrosis factor-induced apoptosis
    • Gabai VL, Mabuchi K, Mosser DD and Sherman MY (2002) Hsp72 and stress kinase c-jun N-terminal kinase regulate the bid-dependent pathway in tumor necrosis factor-induced apoptosis. Mol. Cell. Biol. 22: 3415-3424
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3415-3424
    • Gabai, V.L.1    Mabuchi, K.2    Mosser, D.D.3    Sherman, M.Y.4
  • 53
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jäättelä M, Wissing D, Kokhol K, Kallunki T and Egeblad M (1998) Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J. 17: 6124-6134
    • (1998) EMBO J. , vol.17 , pp. 6124-6134
    • Jäättelä, M.1    Wissing, D.2    Kokhol, K.3    Kallunki, T.4    Egeblad, M.5
  • 54
    • 0031570448 scopus 로고    scopus 로고
    • Overexpression of the heat shock protein 70 enhances the TCR/CD3- and Fas/Apo-1/CD95-mediated apoptotic cell death in Jurkat T cells
    • Liossis S-NC, Ding XZ, Kiang JG and Tsokos GC (1997) Overexpression of the heat shock protein 70 enhances the TCR/CD3- and Fas/Apo-1/CD95-mediated apoptotic cell death in Jurkat T cells. J. Immunol. 158: 5668-5675
    • (1997) J. Immunol. , vol.158 , pp. 5668-5675
    • Liossis, S.-N.C.1    Ding, X.Z.2    Kiang, J.G.3    Tsokos, G.C.4
  • 56
    • 0034682748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation
    • Li CY, Lee JS, Ko YG, Kim JI and Seo JS (2000) Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation. J. Biol. Chem. 275: 25665-25671
    • (2000) J. Biol. Chem. , vol.275 , pp. 25665-25671
    • Li, C.Y.1    Lee, J.S.2    Ko, Y.G.3    Kim, J.I.4    Seo, J.S.5
  • 57
    • 0035890265 scopus 로고    scopus 로고
    • Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53
    • King FW, Wawrzynow A, Hohfeld J and Zylicz M (2001) Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53. EMBO J. 20: 6297-6305
    • (2001) EMBO J. , vol.20 , pp. 6297-6305
    • King, F.W.1    Wawrzynow, A.2    Hohfeld, J.3    Zylicz, M.4
  • 58
    • 0032500553 scopus 로고    scopus 로고
    • Functional analysis of human mitochondrial receptor Tom20 for protein import into mitochondria
    • Yano M, Kanazawa M, Terada K, Takeya M, Hoogenraad N and Mori M (1998) Functional analysis of human mitochondrial receptor Tom20 for protein import into mitochondria. J. Biol. Chem. 273: 26844-26851
    • (1998) J. Biol. Chem. , vol.273 , pp. 26844-26851
    • Yano, M.1    Kanazawa, M.2    Terada, K.3    Takeya, M.4    Hoogenraad, N.5    Mori, M.6
  • 59
    • 0032799629 scopus 로고    scopus 로고
    • Regulation of the genes for arginase isoforms and related enzymes in mouse macrophages by lipopolysaccharide
    • Salimuddin, Nagasaki A, Gotoh T, Isobe H and Mori M (1999) Regulation of the genes for arginase isoforms and related enzymes in mouse macrophages by lipopolysaccharide. Am. J. Physiol. 277: E110-E117
    • (1999) Am. J. Physiol. , vol.277
    • Salimuddin, A.1    Nagasaki, A.2    Gotoh, T.3    Isobe, H.4    Mori, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.