메뉴 건너뛰기




Volumn 7, Issue 5, 2009, Pages 689-702

The human host defense peptide LL-37 induces apoptosis in a calpain- and apoptosis-inducing factor-dependent manner involving Bax activity

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS INDUCING FACTOR; CALCIUM ION; CALPAIN; CASPASE; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; PROTEIN BAK; PROTEIN BAX;

EID: 66349099109     PISSN: 15417786     EISSN: None     Source Type: Journal    
DOI: 10.1158/1541-7786.MCR-08-0274     Document Type: Article
Times cited : (74)

References (68)
  • 1
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002;415:389-395 (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 2
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • DOI 10.1016/j.coi.2005.11.004, PII S0952791505001998, Innate Immunity/Antigen Processing and Recognition
    • Brown KL, Hancock RE. Cationic host defense (antimicrobial) peptides. Curr Opin Immunol 2006;18:24-30. (Pubitemid 43049644)
    • (2006) Current Opinion in Immunology , vol.18 , Issue.1 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.W.2
  • 3
    • 18044397724 scopus 로고    scopus 로고
    • Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines
    • DOI 10.1158/1535-7163.MCT-04-0077
    • Mader JS, Salsman J, Conrad DM, Hoskin DW. Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines. Mol Cancer Ther 2005;4:612-624 (Pubitemid 40601843)
    • (2005) Molecular Cancer Therapeutics , vol.4 , Issue.4 , pp. 612-624
    • Mader, J.S.1    Salsman, J.2    Conrad, D.M.3    Hoskin, D.W.4
  • 4
    • 0033787423 scopus 로고    scopus 로고
    • The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis. Part 2. Sequence determination using electrospray mass spectrometry
    • Rozek T, Bowie JH, Wallace JC, Tyler MJ. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis. Part 2. Sequence determination using electrospray mass spectrometry. Rapid Commun Mass Spectrom 2000;14:2002-2011
    • (2000) Rapid Commun Mass Spectrom , vol.14 , pp. 2002-2011
    • Rozek, T.1    Bowie, J.H.2    Wallace, J.C.3    Tyler, M.J.4
  • 5
    • 0028504387 scopus 로고
    • Preliminary experimental anticancer activity of cacropins
    • Moore AJ, Devine DA, Bibby MC. Preliminary experimental anticancer activity of cacropins. Pept Res 1994;7:265-269
    • (1994) Pept Res , vol.7 , pp. 265-269
    • Moore, A.J.1    Devine, D.A.2    Bibby, M.C.3
  • 6
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Søresen OE, Follin P, Johnsen AH, et al. Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 2001;97:3951-3959
    • (2001) Blood , vol.97 , pp. 3951-3959
    • Søresen, O.E.1    Follin, P.2    Johnsen, A.H.3
  • 8
    • 0034332193 scopus 로고    scopus 로고
    • The human antimicrobial and chemotactic peptides LL-37 and α-defensins are expressed by specific lymphocyte and monocyte populations
    • Agerberth B, Charo J, Werr J, et al. The human antimicrobial and chemotactic peptides LL-37 and α-defensins are expressed by specific lymphocyte and monocyte populations. Blood 2000;96:3086-3093
    • (2000) Blood , vol.96 , pp. 3086-3093
    • Agerberth, B.1    Charo, J.2    Werr, J.3
  • 9
    • 11144320719 scopus 로고    scopus 로고
    • Expression and secretion of cathelicidin antimicrobial peptides in murine mammary glands and human milk
    • DOI 10.1203/01.PDR.0000148068.32201.50
    • Murakami M, Dorschner RA, Stern LJ, Lin KH, Gallo RL. Expression and secretion of cathelicidin antimicrobial peptides in murine mammary glands and human milk. Pediatr Res 2005;57:10-15 (Pubitemid 40039886)
    • (2005) Pediatric Research , vol.57 , Issue.1 , pp. 10-15
    • Murakami, M.1    Dorschner, R.A.2    Stern, L.J.3    Lin, K.H.4    Gallo, R.L.5
  • 10
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule-and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells
    • Yang D, Chen Q, Schmidt AP, Anderson GM, Wang JM, Wooters JJ. LL-37, the neutrophil granule-and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J Exp Med 2000;192:1069-1074
    • (2000) J Exp Med , vol.192 , pp. 1069-1074
    • Yang, D.1    Chen, Q.2    Schmidt, A.P.3    Anderson, G.M.4    Wang, J.M.5    Wooters, J.J.6
  • 12
    • 33644511380 scopus 로고    scopus 로고
    • 7
    • Nagaoka I, Tamura H, Hirata M. An antimicrobial cathelicidin peptide, human CAP18/LL-37, suppresses neutrophil apoptosis via the activation of formylpeptide receptor-like 1 and P2X71. J Immunol 2006;176:3044-3052 (Pubitemid 43306966)
    • (2006) Journal of Immunology , vol.176 , Issue.5 , pp. 3044-3052
    • Nagaoka, I.1    Tamura, H.2    Hirata, M.3
  • 15
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • DOI 10.1038/74994
    • Kroemer G, Reed JC. Mitochondrial control of cell death. Nat Med 2000;6:513-519 (Pubitemid 30305900)
    • (2000) Nature Medicine , vol.6 , Issue.5 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 16
    • 0037401562 scopus 로고    scopus 로고
    • Cell death regulation by the Bcl-2 protein family in the mitochondria
    • DOI 10.1002/jcp.10254
    • Tsujimoto Y. Cell death regulation by the Bcl-2 protein family in the mitochondria. J Cell Physiol 2003;195:158-167 (Pubitemid 36384290)
    • (2003) Journal of Cellular Physiology , vol.195 , Issue.2 , pp. 158-167
    • Tsujimoto, Y.1
  • 19
    • 36348997653 scopus 로고    scopus 로고
    • Mitochondria, calcium, and calpain are key mediators of resveratrol-induced apoptosis in breast cancer
    • DOI 10.1124/mol.107.039040
    • Sareen D, Darjatmoko SR, Albert DM, Polans AS. Mitochondria, calcium, and calpain are key mediators of resveratrol-induced apoptosis in breast cancer. Mol Pharmacol 2007;72:1466-1475 (Pubitemid 350146084)
    • (2007) Molecular Pharmacology , vol.72 , Issue.6 , pp. 1466-1475
    • Sareen, D.1    Darjatmoko, S.R.2    Albert, D.M.3    Polans, A.S.4
  • 20
    • 0141481980 scopus 로고    scopus 로고
    • Cleavage of Bax to p18 Bax accelerates stress-induced apoptosis, and a cathepsin-like protease may rapidly degrade p18 Bax
    • DOI 10.1182/blood-2003-01-0211
    • Cao X, Deng X, May WS. Cleavage of Bax to p18 Bax accelerates stress-induced apoptosis, and a cathepsin-like protease may rapidly degrade p18 Bax. Blood 2003;102:2605-2614 (Pubitemid 37193602)
    • (2003) Blood , vol.102 , Issue.7 , pp. 2605-2614
    • Cao, X.1    Deng, X.2    May, W.S.3
  • 21
    • 33748961826 scopus 로고    scopus 로고
    • Mitochondria as the target of the pro-apoptotic protein Bax
    • DOI 10.1016/j.bbabio.2006.05.032, PII S0005272806001708, Mitochondria: from Molecular Insight to Physiology and Pathology
    • Er E, Oliver L, Cartron P-F, Juin P, Manon S, Vallette FM. Mitochondria as the target of the pro-apoptotic protein Bax. Biochim Biophys Acta 2006;1757:1301-1311 (Pubitemid 44442128)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.9-10 , pp. 1301-1311
    • Er, E.1    Oliver, L.2    Cartron, P.-F.3    Juin, P.4    Manon, S.5    Vallette, F.M.6
  • 24
    • 17844394478 scopus 로고    scopus 로고
    • Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space
    • DOI 10.1038/sj.emboj.7600614
    • Otera H, Ohsakaya S, Nagaura Z, Ishihara N, Mihara K. Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space. EMBO J 2005;24:1375-1386 (Pubitemid 40593058)
    • (2005) EMBO Journal , vol.24 , Issue.7 , pp. 1375-1386
    • Otera, H.1    Ohsakaya, S.2    Nagaura, Z.-I.3    Ishihara, N.4    Mihara, K.5
  • 26
    • 33845570251 scopus 로고    scopus 로고
    • Activation-induced cell death of human melanoma specific cytotoxic T lymphocytes is mediated by apoptosis-inducing factor
    • DOI 10.1002/eji.200636550
    • Chhabra A, Mehrotra S, Chakraborty NG, Dorsky DI, Mukherji B. Activation-induced cell death of human melanoma specific cytotoxic T lymphocytes is mediated by apoptosis-inducing factor. Eur J Immunol 2006;36:3167-3174 (Pubitemid 44932718)
    • (2006) European Journal of Immunology , vol.36 , Issue.12 , pp. 3167-3174
    • Chhabra, A.1    Mehrotra, S.2    Chakraborty, N.G.3    Dorsky, D.I.4    Mukherji, B.5
  • 27
    • 38549123294 scopus 로고    scopus 로고
    • Therapeutic potential of AIF-mediated caspase-independent programmed cell death
    • Lorenzo HK, Susin SA. Therapeutic potential of AIF-mediated caspase-independent programmed cell death. Drug Resist Updat 2007;10:235-255
    • (2007) Drug Resist Updat , vol.10 , pp. 235-255
    • Lorenzo, H.K.1    Susin, S.A.2
  • 29
    • 33745602175 scopus 로고    scopus 로고
    • Apoptosis-inducing factor: Vital and lethal
    • DOI 10.1016/j.tcb.2006.03.008, PII S0962892406000882
    • Modjtahedi N, Giordanetto F, Madeo F, Kroemer G. Apoptosis-inducing factor: vital and lethal. Trends Cell Biol 2006;16:264-272 (Pubitemid 44250822)
    • (2006) Trends in Cell Biology , vol.16 , Issue.5 , pp. 264-272
    • Modjtahedi, N.1    Giordanetto, F.2    Madeo, F.3    Kroemer, G.4
  • 30
    • 33847134493 scopus 로고    scopus 로고
    • Apoptosis-inducing factor: A matter of neuron life and death
    • DOI 10.1016/j.pneurobio.2006.12.002, PII S0301008206001638
    • Krantic S, Mechawar N, Reix S, Quirion R. Apoptosis-inducing factor: a matter of neuron life and death. Prog Neurobiol 2007;81:179-196 (Pubitemid 46282274)
    • (2007) Progress in Neurobiology , vol.81 , Issue.3 , pp. 179-196
    • Krantic, S.1    Mechawar, N.2    Reix, S.3    Quirion, R.4
  • 31
    • 3242889844 scopus 로고    scopus 로고
    • C-terminal domain of human CAP18 antimicrobial peptide induces apoptosis in oral squamous cell carcinoma SAS-H1 cells
    • DOI 10.1016/j.canlet.2004.04.006, PII S0304383504002794
    • Okumura K, Itoh A, Isogai E, et al. C-terminal domain of human CAP18 antimicrobial peptide induces apoptosis in oral squamous cell carcinoma SAS-H1 cells. Cancer Lett 2004;212:185-194 (Pubitemid 38997974)
    • (2004) Cancer Letters , vol.212 , Issue.2 , pp. 185-194
    • Okumura, K.1    Itoh, A.2    Isogai, E.3    Hirose, K.4    Hosokawa, Y.5    Abiko, Y.6    Shibata, T.7    Hirata, M.8    Isogai, H.9
  • 32
    • 33646516620 scopus 로고    scopus 로고
    • Mechanisms of cell death induced by the neutrophil antimicrobial peptides α-defensins and LL-37
    • Aarbiou J, Tjabringa GS, Verhoosel RM, et al. Mechanisms of cell death induced by the neutrophil antimicrobial peptides α-defensins and LL-37. Inflamm Res 2006;55:119-127
    • (2006) Inflamm Res , vol.55 , pp. 119-127
    • Aarbiou, J.1    Tjabringa, G.S.2    Verhoosel, R.M.3
  • 33
    • 0038012805 scopus 로고    scopus 로고
    • Inactivation of Cdc13p triggers MEC1-dependent apoptotic signals in yeast
    • DOI 10.1074/jbc.M212808200
    • Haiyan Q, Kuo D, Nur-E-Kamal A, Liu LF, Tsai-Kun L. Inactivation of Cdc13p triggers MEC1-dependent apoptotic signals in yeast. J Biol Chem 2003;278:15136-15141 (Pubitemid 36799847)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.17 , pp. 15136-15141
    • Qi, H.1    Li, T.-K.2    Kuo, D.3    Nur-E-Kamal, A.4    Liu, L.F.5
  • 35
    • 0037164865 scopus 로고    scopus 로고
    • Mitochondrial release of apoptosis-inducing factor occurs downstream of cytochrome c release in response to several proapoptotic stimuli
    • DOI 10.1083/jcb.200207071
    • Arnoult D, Parone P, Martinou J-C, Antonsson B, Estaquier J, Ameisen JC. Mitochondrial release of apoptosis-inducing factor occurs downstream of cytochrome c release in response to several proapoptotic stimuli. J Cell Biol 2002;159:923-929 (Pubitemid 36055747)
    • (2002) Journal of Cell Biology , vol.159 , Issue.6 , pp. 923-929
    • Arnoult, D.1    Parone, P.2    Martinou, J.-C.3    Antonsson, B.4    Estaquier, J.5    Ameisen, J.C.6
  • 36
    • 34250883860 scopus 로고    scopus 로고
    • Bovine lactoferricin causes apoptosis in Jurkat T-leukemia cells by sequential permeabilization of the cell membrane and targeting of mitochondria
    • DOI 10.1016/j.yexcr.2007.05.015, PII S0014482707002388
    • Mader JS, Richardson A, Salsman J, et al. Bovine lactoferricin causes apoptosis in Jurkat T-leukemia cells by sequential permeabilization of the cell membrane and targeting of mitochondria. Exp Cell Res 2007;313:2634-2650 (Pubitemid 46977347)
    • (2007) Experimental Cell Research , vol.313 , Issue.12 , pp. 2634-2650
    • Mader, J.S.1    Richardson, A.2    Salsman, J.3    Top, D.4    De Antueno, R.5    Duncan, R.6    Hoskin, D.W.7
  • 39
    • 33845341103 scopus 로고    scopus 로고
    • Interaction of HCV core protein with 14-3-3epsilon protein releases Bax to activate apoptosis
    • DOI 10.1016/j.bbrc.2006.11.098, PII S0006291X0602568X
    • Lee SK, Park SO, Joe CO, Kim YS. Interaction of HCV core protein with 14-3-3epsilon protein releases Bax to activate apoptosis. Biochem Biophys Res Commun 2007;352:756-762 (Pubitemid 44880320)
    • (2007) Biochemical and Biophysical Research Communications , vol.352 , Issue.3 , pp. 756-762
    • Lee, S.K.1    Park, S.O.2    Joe, C.O.3    Kim, Y.S.4
  • 40
    • 21644454595 scopus 로고    scopus 로고
    • Bax translocates from cytosol to mitochondria in cardiac cells during apoptosis: Development of a GFP-Bax-stable H9c2 cell line for apoptosis analysis
    • DOI 10.1152/ajpheart.00879.2004
    • Hou Q, Hsu YT. Bax translocates from cytosol to mitochondria in cardiac cells during apoptosis: development of a GFP-Bax-stable H9c2 cell line for apoptosis analysis. Am J Physiol Heart Circ Physiol 2005;289:H477-87. (Pubitemid 40934135)
    • (2005) American Journal of Physiology - Heart and Circulatory Physiology , vol.289 , Issue.1
    • Hou, Q.1    Hsu, Y.-T.2
  • 43
    • 0037057645 scopus 로고    scopus 로고
    • Endogenous antimicrobial peptides and skin infections in atopic dermatitis
    • Ong PY, Ohtake T, Brandt C, et al. Endogenous antimicrobial peptides and skin infections in atopic dermatitis. N Engl J Med 2002;347:1151-1160
    • (2002) N Engl J Med , vol.347 , pp. 1151-1160
    • Ong, P.Y.1    Ohtake, T.2    Brandt, C.3
  • 44
    • 0037180757 scopus 로고    scopus 로고
    • Inflammation and cancer
    • Coussens LM, Werb Z. Inflammation and cancer. Nature 2002;420:860-867
    • (2002) Nature , vol.420 , pp. 860-867
    • Coussens, L.M.1    Werb, Z.2
  • 45
    • 47949121662 scopus 로고    scopus 로고
    • Linking inflammation reactions to cancer: Novel targets for therapeutic strategies
    • Mantovani A, Marchesi F, Portal C, Allavena P, Sica A. Linking inflammation reactions to cancer: novel targets for therapeutic strategies. Adv Exp Med Biol 2008;610:112-127
    • (2008) Adv Exp Med Biol , vol.610 , pp. 112-127
    • Mantovani, A.1    Marchesi, F.2    Portal, C.3    Allavena, P.4    Sica, A.5
  • 46
    • 34247345833 scopus 로고    scopus 로고
    • The apoptosome: Signalling platform of cell death
    • DOI 10.1038/nrm2153, PII NRM2153
    • Riedl SJ, Salvesen GS. The apoptosome: signaling platform of cell death. Nat Rev Mol Cell Biol 2007;8:405-413 (Pubitemid 46643237)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.5 , pp. 405-413
    • Riedl, S.J.1    Salvesen, G.S.2
  • 47
    • 22544444514 scopus 로고    scopus 로고
    • Caspase-independent cell death
    • DOI 10.1038/nm1263
    • Kroemer G, Martin SJ. Caspase-independent cell death. Nat Med 2005;11:725-730 (Pubitemid 41021204)
    • (2005) Nature Medicine , vol.11 , Issue.7 , pp. 725-730
    • Kroemer, G.1    Martin, S.J.2
  • 48
    • 33749617086 scopus 로고    scopus 로고
    • Nuclear translocation of endonuclease G and apoptosis-inducing factor during acetaminophen-induced liver cell injury
    • DOI 10.1093/toxsci/kfl077
    • Bajt ML, Cover C, Lemasters JJ, Jaeschke H. Nuclear translocation of endonuclease G and apoptosis-inducing factor during acetaminophen-induced liver cell injury. Toxicol Sci 2006;94:217-225 (Pubitemid 44542344)
    • (2006) Toxicological Sciences , vol.94 , Issue.1 , pp. 217-225
    • Bajt, M.L.1    Cover, C.2    Lemasters, J.J.3    Jaeschke, H.4
  • 52
    • 0036323443 scopus 로고    scopus 로고
    • Apoptosis-inducing factor is involved in the regulation of caspase-independent neuronal cell death
    • Cregan SP, Fortin A, MacLaurin JG, et al. Apoptosis-inducing factor is involved in the regulation of caspase-independent neuronal cell death. J Cell Biol 2002;158:507-517
    • (2002) J Cell Biol , vol.158 , pp. 507-517
    • Cregan, S.P.1    Fortin, A.2    MacLaurin, J.G.3
  • 53
    • 0034967241 scopus 로고    scopus 로고
    • Cleavage of Bax is mediated by caspase-dependent or -independent calpain activation in dopaminergic neuronal cells: Protective role of Bcl-2
    • DOI 10.1046/j.1471-4159.2001.00368.x
    • Choi WS, Lee EH, Chung CW, et al. Cleavage of Bax is mediated by caspase-dependent or -independent calpain activation in dopaminergic neuronal cells: protective role of Bcl-2. J Neurochem 2001;77:1531-1541 (Pubitemid 32574488)
    • (2001) Journal of Neurochemistry , vol.77 , Issue.6 , pp. 1531-1541
    • Choi, W.-S.1    Lee, E.-H.2    Chung, C.-W.3    Jung, Y.-K.4    Jin, B.K.5    Kim, S.U.6    Oh, T.H.7    Saido, T.C.8    Oh, Y.J.9
  • 54
    • 14844328621 scopus 로고    scopus 로고
    • Calpain I induces cleavage and release of apoptosis-inducing factor from isolated mitochondria
    • DOI 10.1074/jbc.M413269200
    • Polster BM, Basañez G, Etxebarria A, Hardwick JM, Nicholls DG. Calpain I induces cleavage and release of apoptosis-inducing factor from isolated mitochondria. J Biol Chem 2005;280:6447-6454 (Pubitemid 40341192)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.8 , pp. 6447-6454
    • Polster, B.M.1    Basanez, G.2    Etxebarria, A.3    Hardwick, J.M.4    Nicholls, D.G.5
  • 56
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • DOI 10.1074/jbc.M301911200
    • Bidere N, Lorenzo HK, Carmona S, et al. cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase of apoptosis. J Biol Chem 2003;278:31401-31411 (Pubitemid 36994661)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3    Laforge, M.4    Harper, F.5    Dumont, C.6    Senik, A.7
  • 60
    • 3342900223 scopus 로고    scopus 로고
    • 2+-dependent proteases in ischemic neuronal death A conserved "calpain-cathepsin caspase" from nematodes to primates
    • 2+-dependent proteases in ischemic neuronal death A conserved "calpain-cathepsin caspase" from nematodes to primates. Cell Calcium 2004;36:285-293
    • (2004) Cell Calcium , vol.36 , pp. 285-293
    • Yamashima, T.1
  • 62
    • 21444456146 scopus 로고    scopus 로고
    • Antimicrobial and chemoattractant activity, lipopolysaccharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37
    • DOI 10.1128/AAC.49.7.2845-2850.2005
    • Ciornei CD, Sigurdardóttir T, Schmidtchen A, Bodelsson M. Antimicrobial and chemoattractant activity, lipopolysaccharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37. Antimicrob Agents Chemother 2005;49:2845-2850 (Pubitemid 40917601)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.7 , pp. 2845-2850
    • Ciornei, C.D.1    Sigurdardottir, T.2    Schmidtchen, A.3    Bodelsson, M.4
  • 63
    • 23444451770 scopus 로고    scopus 로고
    • High-throughput generation of small antibacterial peptides with improved activity
    • DOI 10.1038/nbt1113
    • Hilpert K, Volkmer-Engert R, Walter T, Hancock REW. High-throughput generation of small antibacterial peptides with improved activity. Nat Biotechnol 2005;23:1008-1012 (Pubitemid 41114036)
    • (2005) Nature Biotechnology , vol.23 , Issue.8 , pp. 1008-1012
    • Hilpert, K.1    Volkmer-Engert, R.2    Walter, T.3    Hancock, R.E.W.4
  • 64
    • 0034694083 scopus 로고    scopus 로고
    • Granzyme B-mediated cytochrome c release is regulated by the Bcl-2 family members Bid and Bax
    • Heibein JA, Goping IS, Barry M, et al. Granzyme B-mediated cytochrome c release is regulated by the Bcl-2 family members Bid and Bax. J Exp Med 2000;92:1391-1402
    • (2000) J Exp Med , vol.92 , pp. 1391-1402
    • Heibein, J.A.1    Goping, I.S.2    Barry, M.3
  • 66
    • 0034107096 scopus 로고    scopus 로고
    • Granzyme B short-circuits the need for caspase 8 activity during granule-mediated cytotoxic T-lymphocyte killing by directly cleaving bid
    • DOI 10.1128/MCB.20.11.3781-3794.2000
    • Barry M, Heibein JA, Pinkoski MJ, et al. Granzyme B short-circuits the need for caspase 8 activity during granule-mediated cytotoxic T-lymphocyte killing by directly cleaving Bid. Mol Cell Biol 2000;20:3781-3794 (Pubitemid 30314478)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.11 , pp. 3781-3794
    • Barry, M.1    Heibein, J.A.2    Pinkoski, M.J.3    Lee, S.-F.4    Moyer, R.W.5    Green, D.R.6    Bleackley, R.C.7
  • 67
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • Gavrieli Y, Sherman Y, Ben-Sasson SA. Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J Cell Biol 1992;119:493-501.
    • (1992) J Cell Biol , vol.119 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 68
    • 0028903933 scopus 로고
    • Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo
    • Zamzami N, Marchetti P, Castedo M, et al. Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo. J Exp Med 1995;181:1661-1672
    • (1995) J Exp Med , vol.181 , pp. 1661-1672
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.