메뉴 건너뛰기




Volumn 289, Issue 1, 2014, Pages 89-99

Evaluation of the BH3-only protein Puma as a direct Bak activator

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL ACTIVATION; LIPOSOMES; OLIGOMERIZATION; OLIGOMERS;

EID: 84891698320     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.505701     Document Type: Article
Times cited : (63)

References (79)
  • 1
    • 0019225636 scopus 로고
    • Cell death. The significance of apoptosis
    • Wyllie, A. H., Kerr, J. F., and Currie, A. R. (1980) Cell death. The significance of apoptosis. Int. Rev. Cytol. 68, 251-306
    • (1980) Int. Rev. Cytol. , vol.68 , pp. 251-306
    • Wyllie, A.H.1    Kerr, J.F.2    Currie, A.R.3
  • 2
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson, C. B. (1995) Apoptosis in the pathogenesis and treatment of disease. Science 267, 1456-1462
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 3
    • 0029807603 scopus 로고    scopus 로고
    • Selective induction of apoptosis in hep 3B cells by topoisomerase I inhibitors: Evidence for a protease-dependent pathway that does not activate cysteine protease P32
    • Adjei, P. N., Kaufmann, S. H., Leung, W. Y., Mao, F., and Gores, G. J. (1996) Selective induction of apoptosis in Hep 3B cells by topoisomerase I inhibitors. Evidence for a protease-dependent pathway that does not activate CPP32. J Clin. Invest. 98, 2588-2596 (Pubitemid 26415080)
    • (1996) Journal of Clinical Investigation , vol.98 , Issue.11 , pp. 2588-2596
    • Adjei, P.N.1    Kaufmann, S.H.2    Leung, W.-Y.3    Mao, F.4    Gores, G.J.5
  • 4
    • 22544444514 scopus 로고    scopus 로고
    • Caspase-independent cell death. Nat
    • Kroemer, G., and Martin, S. J. (2005) Caspase-independent cell death. Nat. Med. 11, 725-730
    • (2005) Med. , vol.11 , pp. 725-730
    • Kroemer, G.1    Martin, S.J.2
  • 5
    • 54949152716 scopus 로고    scopus 로고
    • Caspase-independent cell death. Leaving the set without the final cut
    • Tait, S. W., and Green, D. R. (2008) Caspase-independent cell death. Leaving the set without the final cut. Oncogene 27, 6452-6461
    • (2008) Oncogene , vol.27 , pp. 6452-6461
    • Tait, S.W.1    Green, D.R.2
  • 6
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • DOI 10.1146/annurev.biochem.68.1.383
    • Earnshaw, W. C., Martins, L. M., and Kaufmann, S. H. (1999) Mammalian caspases. Structure, Activation, Substrates, and functions during apoptosis. Annu. Rev. Biochem. 68, 383-424 (Pubitemid 29449198)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 7
    • 0035213498 scopus 로고    scopus 로고
    • Caspases. Cellular demolition experts
    • Creagh, E. M., and Martin, S. J. (2001) Caspases. Cellular demolition experts. Biochem. Soc. Trans. 29, 696-702
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 696-702
    • Creagh, E.M.1    Martin, S.J.2
  • 8
    • 0034630161 scopus 로고    scopus 로고
    • The CD95 (APO-1/Fas) and the TRAIL (APO-2L) apoptosis systems
    • DOI 10.1006/excr.2000.4840
    • Walczak, H., and Krammer, P. H. (2000) The CD95 (APO-1/Fas) and the TRAIL (APO-2L) apoptosis systems. Exp. Cell Res. 256, 58-66 (Pubitemid 30211167)
    • (2000) Experimental Cell Research , vol.256 , Issue.1 , pp. 58-66
    • Walczak, H.1    Krammer, P.H.2
  • 9
    • 2342453921 scopus 로고    scopus 로고
    • Death receptors inchemotherapy and cancer
    • Debatin, K. M., and Krammer, P. H. (2004) Death receptors inchemotherapy and cancer. Oncogene 23, 2950-2966
    • (2004) Oncogene , vol.23 , pp. 2950-2966
    • Debatin, K.M.1    Krammer, P.H.2
  • 10
    • 47749089820 scopus 로고    scopus 로고
    • Regulation of TNFR1 and CD95 signalling by receptor compartmentalization
    • DOI 10.1038/nrm2430, PII NRM2430
    • Schütze, S., Tchikov, V., and Schneider-Brachert, W. (2008) Regulation of TNFR1 and CD95 signalling by receptor compartmentalization. Nat. Rev. Mol. Cell Biol. 9, 655-662 (Pubitemid 352032925)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.8 , pp. 655-662
    • Schutze, S.1    Tchikov, V.2    Schneider-Brachert, W.3
  • 11
    • 52649109068 scopus 로고    scopus 로고
    • The TRAIL apoptotic pathway in cancer onset, progression, and therapy
    • Johnstone, R. W., Frew, A. J., and Smyth, M. J. (2008) The TRAIL apoptotic pathway in cancer onset, progression, and therapy. Nat. Rev. Cancer 8, 782-798
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 782-798
    • Johnstone, R.W.1    Frew, A.J.2    Smyth, M.J.3
  • 13
    • 77951681958 scopus 로고    scopus 로고
    • Cytotoxic and noncytotoxic roles of the CTL/NK protease granzyme B
    • Afonina, I. S., Cullen, S. P., and Martin, S. J. (2010) Cytotoxic and noncytotoxic roles of the CTL/NK protease granzyme B. Immunol. Rev. 235, 105-116
    • (2010) Immunol. Rev. , vol.235 , pp. 105-116
    • Afonina, I.S.1    Cullen, S.P.2    Martin, S.J.3
  • 15
    • 3943071150 scopus 로고    scopus 로고
    • Cytochrome C-mediated apoptosis
    • DOI 10.1146/annurev.biochem.73.011303.073706
    • Jiang, X., and Wang, X. (2004) Cytochrome c-mediated apoptosis. Annu. Rev. Biochem. 73, 87-106 (Pubitemid 39050364)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 87-106
    • Jiang, X.1    Wang, X.2
  • 16
    • 39749182234 scopus 로고    scopus 로고
    • Apoptosis: Controlled demolition at the cellular level
    • DOI 10.1038/nrm2312, PII NRM2312
    • Taylor, R. C., Cullen, S. P., and Martin, S. J. (2008) Apoptosis. Controlled demolition at the cellular level. Nat Rev. Mol. Cell Biol. 9, 231-241 (Pubitemid 351301823)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.3 , pp. 231-241
    • Taylor, R.C.1    Cullen, S.P.2    Martin, S.J.3
  • 17
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death. Outer membrane permeabilization and beyond
    • Tait, S. W., and Green, D. R. (2010) Mitochondria and cell death. Outer membrane permeabilization and beyond. Nat. Rev. Mol. Cell Biol. 11, 621-632
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 18
    • 84860389354 scopus 로고    scopus 로고
    • Deciphering the rules of programmed cell death to improve therapy of cancer and other diseases
    • Strasser, A., Cory, S., and Adams, J. M. (2011) Deciphering the rules of programmed cell death to improve therapy of cancer and other diseases. EMBOJ. 30, 3667-3683
    • (2011) EMBOJ. , vol.30 , pp. 3667-3683
    • Strasser, A.1    Cory, S.2    Adams, J.M.3
  • 19
    • 38549145044 scopus 로고    scopus 로고
    • Diagnosing and exploiting cancer's addiction to blocks in apoptosis
    • DOI 10.1038/nrc2297, PII NRC2297
    • Letai, A. G. (2008) Diagnosing and exploiting cancer's addiction to blocks in apoptosis. Nat Rev. Cancer 8, 121-132 (Pubitemid 351161322)
    • (2008) Nature Reviews Cancer , vol.8 , Issue.2 , pp. 121-132
    • Letai, A.G.1
  • 21
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • DOI 10.1016/S1535-6108(02)00127-7
    • Letai, A., Bassik, M. C., Walensky, L. D., Sorcinelli, M. D., Weiler, S., and Korsmeyer, S. J. (2002) Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell 2, 183-192 (Pubitemid 41043974)
    • (2002) Cancer Cell , vol.2 , Issue.3 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 22
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • DOI 10.1016/S0092-8674(02)01036-X
    • Kuwana, T., Mackey, M. R., Perkins, G., Ellisman, M. H., Latterich, M., Schneiter, R., Green, D. R., and Newmeyer, D. D. (2002) Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 111, 331-342 (Pubitemid 35341388)
    • (2002) Cell , vol.111 , Issue.3 , pp. 331-342
    • Kuwana, T.1    Mackey, M.R.2    Perkins, G.3    Ellisman, M.H.4    Latterich, M.5    Schneiter, R.6    Green, D.R.7    Newmeyer, D.D.8
  • 23
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • DOI 10.1016/j.molcel.2005.02.003
    • Kuwana, T., Bouchier-Hayes, L., Chipuk, J. E., Bonzon, C., Sullivan, B. A., Green, D. R., and Newmeyer, D. D. (2005) BH3 Domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. Mol. Cell 17, 525-535 (Pubitemid 40269117)
    • (2005) Molecular Cell , vol.17 , Issue.4 , pp. 525-535
    • Kuwana, T.1    Bouchier-Hayes, L.2    Chipuk, J.E.3    Bonzon, C.4    Sullivan, B.A.5    Green, D.R.6    Newmeyer, D.D.7
  • 24
    • 0032863163 scopus 로고    scopus 로고
    • All along the watchtower: On the regulation of apoptosis regulators
    • Fadeel, B., Zhivotovsky, B., and Orrenius, S. (1999) All along the watchtower. On the regulation of apoptosis regulators. FASEB J. 13, 1647-1657 (Pubitemid 29473328)
    • (1999) FASEB Journal , vol.13 , Issue.13 , pp. 1647-1657
    • Fadeel, B.1    Zhivotovsky, B.2    Orrenius, S.3
  • 25
    • 41149152733 scopus 로고    scopus 로고
    • How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
    • Chipuk, J. E., and Green, D. R. (2008) How do BCL-2 proteins induce mitochondrial outer membrane permeabilization? Trends Cell Biol. 18, 157-164
    • (2008) Trends Cell Biol. , vol.18 , pp. 157-164
    • Chipuk, J.E.1    Green, D.R.2
  • 27
    • 0035265823 scopus 로고    scopus 로고
    • PUMA induces the rapid apoptosis of colorectal cancer cells
    • DOI 10.1016/S1097-2765(01)00213-1
    • Yu, J., Zhang, L., Hwang, P. M., Kinzler, K. W., and Vogelstein, B. (2001) PUMA induces the rapid apoptosis of colorectal cancer cells. Mol. Cell 7, 673-682 (Pubitemid 32706358)
    • (2001) Molecular Cell , vol.7 , Issue.3 , pp. 673-682
    • Yu, J.1    Zhang, L.2    Hwang, P.M.3    Kinzler, K.W.4    Vogelstein, B.5
  • 28
    • 0035265686 scopus 로고    scopus 로고
    • PUMA, a novel proapoptotic gene, is induced by p53
    • DOI 10.1016/S1097-2765(01)00214-3
    • Nakano, K., and Vousden, K. H. (2001) PUMA, a novel proapoptotic gene, is induced by p53. Mol. Cell 7, 683-694 (Pubitemid 32706359)
    • (2001) Molecular Cell , vol.7 , Issue.3 , pp. 683-694
    • Nakano, K.1    Vousden, K.H.2
  • 29
    • 0242410719 scopus 로고    scopus 로고
    • P53 and drug-induced apoptotic responses mediated by bh3-only proteins puma and noxa
    • DOI 10.1126/science.1090072
    • Villunger, A., Michalak, E. M., Coultas, L., Müllauer, F., Böck, G., Ausserlechner, M. J., Adams, J. M., and Strasser, A. (2003) p53- and drug-induced apoptotic responses mediated by BH3-only proteins puma and noxa. Science 302, 1036-1038 (Pubitemid 37386194)
    • (2003) Science , vol.302 , Issue.5647 , pp. 1036-1038
    • Villunger, A.1    Michalak, E.M.2    Coultas, L.3    Mullauer, F.4    Bock, G.5    Ausserlechner, M.J.6    Adams, J.M.7    Strasser, A.8
  • 32
    • 28844472952 scopus 로고    scopus 로고
    • BH3-only proteins Puma and Bim are rate-limiting for γ-radiation- and glucocorticoid-induced apoptosis of lymphoid cells in vivo
    • DOI 10.1182/blood-2005-04-1595
    • Erlacher, M., Michalak, E. M., Kelly, P. N., Labi, V., Niederegger, H., Coultas, L., Adams, J. M., Strasser, A., and Villunger, A. (2005) BH3-only proteins Puma and Bim are rate-limiting for 7-radiation- and glucocorticoidinduced apoptosis of lymphoid cells in vivo. Blood 106, 4131-4138 (Pubitemid 41775918)
    • (2005) Blood , vol.106 , Issue.13 , pp. 4131-4138
    • Erlacher, M.1    Michalak, E.M.2    Kelly, P.N.3    Labi, V.4    Niederegger, H.5    Coultas, L.6    Adams, J.M.7    Strasser, A.8    Villunger, A.9
  • 33
    • 33845913794 scopus 로고    scopus 로고
    • Puma cooperates with Bim, the rate-limiting BH3-only protein in cell death during lymphocyte development, in apoptosis induction
    • DOI 10.1084/jem.20061552
    • Erlacher, M., Labi, V., Manzl, C., Böck, G., Tzankov, A., Häcker, G., Michalak, E., Strasser, A., and Villunger, A. (2006) Puma cooperates with Bim, the rate-limiting BH3-only protein in cell death during lymphocyte development, in apoptosis induction. J. Exp. Med. 203, 2939-2951 (Pubitemid 46026171)
    • (2006) Journal of Experimental Medicine , vol.203 , Issue.13 , pp. 2939-2951
    • Erlacher, M.1    Labi, V.2    Manzl, C.3    Bock, G.4    Tzankov, A.5    Hacker, G.6    Michalak, E.7    Strasser, A.8    Villunger, A.9
  • 34
    • 44049095767 scopus 로고    scopus 로고
    • In several cell types tumour suppressor p53 induces apoptosis largely via Puma but Noxa can contribute
    • DOI 10.1038/cdd.2008.16, PII CDD200816
    • Michalak, E. M., Villunger, A., Adams, J. M., and Strasser, A. (2008) In several cell types tumour suppressor p53 induces apoptosis largely via Puma but Noxa can contribute. Cell Death Differ 15, 1019-1029 (Pubitemid 351712606)
    • (2008) Cell Death and Differentiation , vol.15 , Issue.6 , pp. 1019-1029
    • Michalak, E.M.1    Villunger, A.2    Adams, J.M.3    Strasser, A.4
  • 35
    • 44349122954 scopus 로고    scopus 로고
    • PUMA regulates intestinal progenitor cell radiosensitivity and gastrointestinal syndrome
    • DOI 10.1016/j.stem.2008.03.009, PII S1934590908001227
    • Qiu, W., Carson-Walter, E. B., Liu, H., Epperly, M., Greenberger, J. S., Zambetti, G. P., Zhang, L., and Yu, J. (2008) PUMA regulates intestinal progenitor cell radiosensitivity and gastrointestinal syndrome. Cell Stem Cell 2, 576-583 (Pubitemid 351729214)
    • (2008) Cell Stem Cell , vol.2 , Issue.6 , pp. 576-583
    • Qiu, W.1    Carson-Walter, E.B.2    Liu, H.3    Epperly, M.4    Greenberger, J.S.5    Zambetti, G.P.6    Zhang, L.7    Yu, J.8
  • 37
    • 77951753647 scopus 로고    scopus 로고
    • Deletion of Puma protects hematopoietic stem cells and confers long-term survival in response to high-dose 7-irradiation
    • Yu, H., Shen, H., Yuan, Y., Xu Feng, R., Hu, X., Garrison, S. P., Zhang, L., Yu, J., Zambetti, G. P., and Cheng, T. (2010) Deletion of Puma protects hematopoietic stem cells and confers long-term survival in response to high-dose 7-irradiation. Blood 115, 3472-3480
    • (2010) Blood , vol.115 , pp. 3472-3480
    • Yu, H.1    Shen, H.2    Yuan, Y.3    Xu Feng, R.4    Hu, X.5    Garrison, S.P.6    Zhang, L.7    Yu, J.8    Zambetti, G.P.9    Cheng, T.10
  • 40
    • 36048986227 scopus 로고    scopus 로고
    • The BH3-only protein Puma plays an essential role in cytokine deprivation-induced apoptosis of mast cells
    • DOI 10.1182/blood-2007-02-073957
    • Ekoff, M., Kaufmann, T., Engström, M., Motoyama, N., Villunger, A., Jönsson, J. I., Strasser, A., and Nilsson, G. (2007) The BH3-only protein Puma plays an essential role in cytokine deprivation induced apoptosis of mast cells. Blood 110, 3209-3217 (Pubitemid 350106313)
    • (2007) Blood , vol.110 , Issue.9 , pp. 3209-3217
    • Ekoff, M.1    Kaufmann, T.2    Engstrom, M.3    Motoyama, N.4    Villunger, A.5    Jonsson, J.-I.6    Strasser, A.7    Nilsson, G.8
  • 47
    • 68249161304 scopus 로고    scopus 로고
    • The proapoptotic BH3-only, Bcl-2 family member, Puma is critical for acute ethanol-induced neuronal apoptosis
    • Ghosh, A. P., Walls, K. C., Klocke, B. J., Toms, R., Strasser, A., and Roth, K. A. (2009) The proapoptotic BH3-only, Bcl-2 family member, Puma is critical for acute ethanol-induced neuronal apoptosis. J. Neuropathol. Exp. Neurol. 68, 747-756
    • (2009) J. Neuropathol. Exp. Neurol. , vol.68 , pp. 747-756
    • Ghosh, A.P.1    Walls, K.C.2    Klocke, B.J.3    Toms, R.4    Strasser, A.5    Roth, K.A.6
  • 48
  • 49
    • 42949179577 scopus 로고    scopus 로고
    • BH3-only protein Puma contributes to death of antigen-specific T cells during shutdown of an immune response to acute viral infection
    • DOI 10.1073/pnas.0706913105
    • Fischer, S. F., Belz, G. T., and Strasser, A. (2008) BH3-only protein Puma contributes to death of antigen-specific T cells during shutdown of an immune response to acute viral infection. Proc. Natl. Acad. Sci. U. S. A. 105, 3035-3040 (Pubitemid 351723663)
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , Issue.8 , pp. 3035-3040
    • Fischer, S.F.1    Belz, G.T.2    Strasser, A.3
  • 51
    • 84866491766 scopus 로고    scopus 로고
    • The BH3-only proteins Bim and Puma cooperate to impose deletional tolerance of organ-specific antigens
    • Gray, D. H., Kupresanin, F., Berzins, S. P., Herold, M. J., O'Reilly, L. A., Bouillet, P., and Strasser, A. (2012) The BH3-only proteins Bim and Puma cooperate to impose deletional tolerance of organ-specific antigens. Immunity 37, 451-462
    • (2012) Immunity , vol.37 , pp. 451-462
    • Gray, D.H.1    Kupresanin, F.2    Berzins, S.P.3    Herold, M.J.4    O'Reilly, L.A.5    Bouillet, P.6    Strasser, A.7
  • 54
    • 69749112731 scopus 로고    scopus 로고
    • PUMA cooperates with direct activator proteins to promote mitochondrial outer membrane permeabilization and apoptosis
    • Chipuk, J. E., and Green, D. R. (2009) PUMA cooperates with direct activator proteins to promote mitochondrial outer membrane permeabilization and apoptosis. Cell Cycle 8, 2692-2696
    • (2009) Cell Cycle , vol.8 , pp. 2692-2696
    • Chipuk, J.E.1    Green, D.R.2
  • 57
    • 70449091753 scopus 로고    scopus 로고
    • Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis
    • Kim, H., Tu, H. C., Ren, D., Takeuchi, O., Jeffers, J. R., Zambetti, G. P., Hsieh, J. J., and Cheng, E. H. (2009) Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis. Mol. Cell 36, 487-499
    • (2009) Mol. Cell , vol.36 , pp. 487-499
    • Kim, H.1    Tu, H.C.2    Ren, D.3    Takeuchi, O.4    Jeffers, J.R.5    Zambetti, G.P.6    Hsieh, J.J.7    Cheng, E.H.8
  • 59
    • 67650444323 scopus 로고    scopus 로고
    • PUMA promotes Bax translocation by both directly interacting with Bax and by competitive binding to Bcl-X L during UV-induced apoptosis
    • Zhang, Y., Xing, D., and Liu, L. (2009) PUMA promotes Bax translocation by both directly interacting with Bax and by competitive binding to Bcl-X L during UV-induced apoptosis. Mol. Biol. Cell 20, 3077-3087
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3077-3087
    • Zhang, Y.1    Xing, D.2    Liu, L.3
  • 60
    • 84874050737 scopus 로고    scopus 로고
    • Direct interaction of Bax and Bak proteins with Bcl-2 homology domain 3 (BH3)-only proteins in living cells revealed by fluorescence complementation
    • Vela, L., Gonzalo, O., Naval, J., and Marzo, I. (2013) Direct interaction of Bax and Bak proteins with Bcl-2 homology domain 3 (BH3)-only proteins in living cells revealed by fluorescence complementation. J. Biol. Chem. 288, 4935-4946
    • (2013) J. Biol. Chem. , vol.288 , pp. 4935-4946
    • Vela, L.1    Gonzalo, O.2    Naval, J.3    Marzo, I.4
  • 62
    • 79960235245 scopus 로고    scopus 로고
    • Transient binding of an activator BH3 domain to the Bak BH3-binding groove initiates Bak oligomerization
    • Dai, H., Smith, A., Meng, X. W., Schneider, P. A., Pang, Y.-P., and Kaufmann, S. H. (2011) Transient binding of an activator BH3 domain to the Bak BH3-binding groove initiates Bak oligomerization. J. Cell Biol. 194, 39-48
    • (2011) J. Cell Biol. , vol.194 , pp. 39-48
    • Dai, H.1    Smith, A.2    Meng, X.W.3    Schneider, P.A.4    Pang, Y.-P.5    Kaufmann, S.H.6
  • 64
    • 8444238235 scopus 로고    scopus 로고
    • S-peptide epitope tagging for protein purification, expression monitoring, and localization in mammalian cells
    • Hackbarth, J. S., Lee, S.-H., Meng, X. W., Vroman, B. T., Kaufmann, S. H., and Karnitz, L. M. (2004) S-peptide epitope tagging for protein purification, expression monitoring and localization in mammalian cells. Bio-Techniques 37, 835-839 (Pubitemid 39488463)
    • (2004) BioTechniques , vol.37 , Issue.5 , pp. 835-839
    • Hackbarth, J.S.1    Lee, S.-H.2    Meng, X.W.3    Vroman, B.T.4    Kaufmann, S.H.5    Karnitz, L.M.6
  • 65
    • 33751544565 scopus 로고    scopus 로고
    • The X-Ray Structure of a BAK Homodimer Reveals an Inhibitory Zinc Binding Site
    • DOI 10.1016/j.molcel.2006.10.014, PII S1097276506007039
    • Moldoveanu, T., Liu, Q., Tocilj, A., Watson, M., Shore, G., and Gehring, K. (2006) The X-ray structure of a BAK homodimer revealsan inhibitory zinc binding site. Mol. Cell 24, 677-688 (Pubitemid 44839210)
    • (2006) Molecular Cell , vol.24 , Issue.5 , pp. 677-688
    • Moldoveanu, T.1    Liu, Q.2    Tocilj, A.3    Watson, M.4    Shore, G.5    Gehring, K.6
  • 66
    • 77956523192 scopus 로고    scopus 로고
    • Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for the existence of BH3-BH3 contact interface in BAK homo-oligomers
    • Oh, K. J., Singh, P., Lee, K., Foss, K., Lee, S., Park, M., Lee, S., Aluvila, S., Park, M., Singh, P., Kim, R. S., Symersky, J., and Walters, D. E. (2010) Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for the existence of BH3-BH3 contact interface in BAK homo-oligomers. J. Biol. Chem. 285, 28924-28937
    • (2010) J. Biol. Chem. , vol.285 , pp. 28924-28937
    • Oh, K.J.1    Singh, P.2    Lee, K.3    Foss, K.4    Lee, S.5    Park, M.6    Lee, S.7    Aluvila, S.8    Park, M.9    Singh, P.10    Kim, R.S.11    Symersky, J.12    Walters, D.E.13
  • 70
    • 84859753178 scopus 로고    scopus 로고
    • Bak conformational changes induced by ligand binding. Insight into BH3 domain binding and Bak homo-oligomerization
    • Pang, Y. P., Dai, H., Smith, A., Meng, X. W., Schneider, P. A., and Kaufmann, S. H. (2012) Bak conformational changes induced by ligand binding. Insight into BH3 domain binding and Bak homo-oligomerization. Sci. Rep. 2, 257
    • (2012) Sci. Rep. , vol.2 , pp. 257
    • Pang, Y.P.1    Dai, H.2    Smith, A.3    Meng, X.W.4    Schneider, P.A.5    Kaufmann, S.H.6
  • 72
    • 68949086461 scopus 로고    scopus 로고
    • Evaluating the performance of the ff99SB force field based on NMR scalar coupling data
    • Wickstrom, L., Okur, A., and Simmerling, C. (2009) Evaluating the performance of the ff99SB force field based on NMR scalar coupling data. Biophys. J. 97, 853-856
    • (2009) Biophys. J. , vol.97 , pp. 853-856
    • Wickstrom, L.1    Okur, A.2    Simmerling, C.3
  • 74
    • 33846823909 scopus 로고
    • Particle Mesh Ewald. An N log (N) method for Ewald sums in large systems
    • Darden, T. A., York, D. M., and Pedersen, L. G. (1993) Particle Mesh Ewald. An N log (N) method for Ewald sums in large systems. J. Chem. Phys. 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.A.1    York, D.M.2    Pedersen, L.G.3
  • 76
    • 43049105074 scopus 로고    scopus 로고
    • To Trigger Apoptosis, Bak Exposes Its BH3 Domain and Homodimerizes via BH3:Groove Interactions
    • DOI 10.1016/j.molcel.2008.04.005, PII S1097276508002657
    • Dewson, G., Kratina, T., Sim, H. W., Puthalakath, H., Adams, J. M., Colman, P. M., and Kluck, R. M. (2008) To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3. Groove interactions. Mol. Cell 30, 369-380 (Pubitemid 351626944)
    • (2008) Molecular Cell , vol.30 , Issue.3 , pp. 369-380
    • Dewson, G.1    Kratina, T.2    Sim, H.W.3    Puthalakath, H.4    Adams, J.M.5    Colman, P.M.6    Kluck, R.M.7
  • 77
    • 65549109031 scopus 로고    scopus 로고
    • Configurational entropy in protein-peptide binding. Computational study of Tsg101 ubiquitin E2 variant domain with an HIV-derived PTAP nonapeptide
    • Killian, B. J., Kravitz, J. Y., Somani, S., Dasgupta, P., Pang, Y. P., and Gilson, M. K. (2009) Configurational entropy in protein-peptide binding. Computational study of Tsg101 ubiquitin E2 variant domain with an HIV-derived PTAP nonapeptide. J. Mol. Biol. 389, 315-335
    • (2009) J. Mol. Biol. , vol.389 , pp. 315-335
    • Killian, B.J.1    Kravitz, J.Y.2    Somani, S.3    Dasgupta, P.4    Pang, Y.P.5    Gilson, M.K.6
  • 78
    • 67650510705 scopus 로고    scopus 로고
    • Context-dependent Bcl-2/Bak interactions regulate lymphoid cell apoptosis
    • Dai, H., Meng, X. W., Lee, S.-H., Schneider, P. A., and Kaufmann, S. H. (2009) Context-dependent Bcl-2/Bak interactions regulate lymphoid cell apoptosis. J. Biol. Chem. 284, 18311-18322
    • (2009) J. Biol. Chem. , vol.284 , pp. 18311-18322
    • Dai, H.1    Meng, X.W.2    Lee, S.-H.3    Schneider, P.A.4    Kaufmann, S.H.5
  • 79
    • 80855128781 scopus 로고    scopus 로고
    • Cytotoxicity offarnesyltransferase inhibitors in lymphoid cells mediated by MAPK pathway inhibition and Bim upregulation
    • Ding, H., Hackbarth, J., Schneider, P. A., Peterson, K. L., Meng, X. W., Dai, H., Witzig, T. E., and Kaufmann, S. H. (2011) Cytotoxicity offarnesyltransferase inhibitors in lymphoid cells mediated by MAPK pathway inhibition and Bim upregulation. Blood 118, 4872-4881
    • (2011) Blood , vol.118 , pp. 4872-4881
    • Ding, H.1    Hackbarth, J.2    Schneider, P.A.3    Peterson, K.L.4    Meng, X.W.5    Dai, H.6    Witzig, T.E.7    Kaufmann, S.H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.