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Volumn 15, Issue 5, 2003, Pages 553-559

Nuclear war: The granzyme A-bomb

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CURVED DNA; DEOXYRIBONUCLEASE; ENDONUCLEASE; GRANZYME A; HIGH MOBILITY GROUP B2 PROTEIN; HISTONE; LAMIN; PROTEIN APE 1; PROTEIN BCL 2; SERINE PROTEINASE INHIBITOR; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

EID: 0141629512     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(03)00108-0     Document Type: Review
Times cited : (168)

References (77)
  • 1
    • 0021859627 scopus 로고
    • A novel serine protease expressed by cytotoxic T lymphocytes
    • Pasternack M.S., Eisen H.N. A novel serine protease expressed by cytotoxic T lymphocytes. Nature. 314:1985;743-745.
    • (1985) Nature , vol.314 , pp. 743-745
    • Pasternack, M.S.1    Eisen, H.N.2
  • 2
    • 0022624829 scopus 로고
    • Cloning of a cDNA for a T cell-specific serine protease from a cytotoxic T lymphocyte
    • Gershenfeld H.K., Weissman I.L. Cloning of a cDNA for a T cell-specific serine protease from a cytotoxic T lymphocyte. Science. 232:1986;854.
    • (1986) Science , vol.232 , pp. 854
    • Gershenfeld, H.K.1    Weissman, I.L.2
  • 3
    • 0023927292 scopus 로고
    • Appearance of granule-associated molecules during activation of cytolytic T-lymphocyte precursors by defined stimuli
    • Garcia-Sanz J.A., Velotti F., MacDonald H.R., Masson D., Tschopp J., Nabholz M. Appearance of granule-associated molecules during activation of cytolytic T-lymphocyte precursors by defined stimuli. Immunology. 64:1988;129-134.
    • (1988) Immunology , vol.64 , pp. 129-134
    • Garcia-Sanz, J.A.1    Velotti, F.2    MacDonald, H.R.3    Masson, D.4    Tschopp, J.5    Nabholz, M.6
  • 5
    • 0141741403 scopus 로고    scopus 로고
    • Lytic granules, secretory lysosomes and disease
    • Clark R, Griffiths GM: Lytic granules, secretory lysosomes and disease. Curr Opin Immunol 2003, 15: this issue.
    • (2003) Curr Opin Immunol , Issue.THIS ISSUE , pp. 15
    • Clark, R.1    Griffiths, G.M.2
  • 6
    • 0035412370 scopus 로고    scopus 로고
    • CD8 T cells specific for human immunodeficiency virus, Epstein-Barr virus, and cytomegalovirus lack molecules for homing to lymphoid sites of infection
    • Chen G., Shankar P., Lange C., Valdez H., Skolnik P.R., Wu L., Manjunath N., Lieberman J. CD8 T cells specific for human immunodeficiency virus, Epstein-Barr virus, and cytomegalovirus lack molecules for homing to lymphoid sites of infection. Blood. 98:2001;156-164.
    • (2001) Blood , vol.98 , pp. 156-164
    • Chen, G.1    Shankar, P.2    Lange, C.3    Valdez, H.4    Skolnik, P.R.5    Wu, L.6    Manjunath, N.7    Lieberman, J.8
  • 7
    • 0037221406 scopus 로고    scopus 로고
    • Most antiviral CD8 T cells during chronic viral infection do not express high levels of perforin and are not directly cytotoxic
    • Zhang D., Shankar P., Xu Z., Harnisch B., Chen G., Lange C., Lee S.J., Valdez H., Lederman M.M., Lieberman J. Most antiviral CD8 T cells during chronic viral infection do not express high levels of perforin and are not directly cytotoxic. Blood. 101:2003;226-235.
    • (2003) Blood , vol.101 , pp. 226-235
    • Zhang, D.1    Shankar, P.2    Xu, Z.3    Harnisch, B.4    Chen, G.5    Lange, C.6    Lee, S.J.7    Valdez, H.8    Lederman, M.M.9    Lieberman, J.10
  • 8
    • 0026474805 scopus 로고
    • Purification of three cytotoxic lymphocyte granule serine proteases that induce apoptosis through distinct substrate and target cell interactions
    • Shi L., Kam C.M., Powers J.C., Aebersold R., Greenberg A.H. Purification of three cytotoxic lymphocyte granule serine proteases that induce apoptosis through distinct substrate and target cell interactions. J Exp Med. 176:1992;1521-1529.
    • (1992) J Exp Med , vol.176 , pp. 1521-1529
    • Shi, L.1    Kam, C.M.2    Powers, J.C.3    Aebersold, R.4    Greenberg, A.H.5
  • 9
    • 0026532606 scopus 로고
    • A natural killer cell granule protein that induces DNA fragmentation and apoptosis
    • Shi L., Kraut R.P., Aebersold R., Greenberg A.H. A natural killer cell granule protein that induces DNA fragmentation and apoptosis. J Exp Med. 175:1992;553-566.
    • (1992) J Exp Med , vol.175 , pp. 553-566
    • Shi, L.1    Kraut, R.P.2    Aebersold, R.3    Greenberg, A.H.4
  • 10
    • 0036312429 scopus 로고    scopus 로고
    • The differential contribution of granzyme A and granzyme B in cytotoxic T lymphocyte-mediated apoptosis is determined by the quality of target cells
    • Pardo J., Balkow S., Anel A., Simon M.M. The differential contribution of granzyme A and granzyme B in cytotoxic T lymphocyte-mediated apoptosis is determined by the quality of target cells. Eur J Immunol. 32:2002;1980-1985.
    • (2002) Eur J Immunol , vol.32 , pp. 1980-1985
    • Pardo, J.1    Balkow, S.2    Anel, A.3    Simon, M.M.4
  • 11
    • 0033137079 scopus 로고    scopus 로고
    • Granzyme A loading induces rapid cytolysis and a novel form of DNA damage independently of caspase activation
    • Beresford P.J., Xia Z., Greenberg A.H., Lieberman J. Granzyme A loading induces rapid cytolysis and a novel form of DNA damage independently of caspase activation. Immunity. 10:1999;585-594.
    • (1999) Immunity , vol.10 , pp. 585-594
    • Beresford, P.J.1    Xia, Z.2    Greenberg, A.H.3    Lieberman, J.4
  • 12
    • 0033136315 scopus 로고    scopus 로고
    • Granzyme A initiates an alternative pathway for granule-mediated apoptosis
    • Shresta S., Graubert T.A., Thomas D.A., Raptis S.Z., Ley T.J. Granzyme A initiates an alternative pathway for granule-mediated apoptosis. Immunity. 10:1999;595-605.
    • (1999) Immunity , vol.10 , pp. 595-605
    • Shresta, S.1    Graubert, T.A.2    Thomas, D.A.3    Raptis, S.Z.4    Ley, T.J.5
  • 13
    • 0037318699 scopus 로고    scopus 로고
    • Granzyme A: The road less traveled
    • Pinkoski M.J., Green D.R. Granzyme A: the road less traveled. Nat Immunol. 4:2003;106-108.
    • (2003) Nat Immunol , vol.4 , pp. 106-108
    • Pinkoski, M.J.1    Green, D.R.2
  • 15
    • 0029963625 scopus 로고    scopus 로고
    • Extracellular activities of human granzyme A. Monocyte activation by granzyme A versus alpha-thrombin
    • Sower L.E., Froelich C.J., Allegretto N., Rose P.M., Hanna W.D., Klimpel G.R. Extracellular activities of human granzyme A. Monocyte activation by granzyme A versus alpha-thrombin. J Immunol. 156:1996;2585-2590.
    • (1996) J Immunol , vol.156 , pp. 2585-2590
    • Sower, L.E.1    Froelich, C.J.2    Allegretto, N.3    Rose, P.M.4    Hanna, W.D.5    Klimpel, G.R.6
  • 16
    • 0030578437 scopus 로고    scopus 로고
    • Extracellular activities of human granzymes. I. Granzyme A induces IL6 and IL8 production in fibroblast and epithelial cell lines
    • Sower L.E., Klimpel G.R., Hanna W., Froelich C.J. Extracellular activities of human granzymes. I. Granzyme A induces IL6 and IL8 production in fibroblast and epithelial cell lines. Cell Immunol. 171:1996;159-163.
    • (1996) Cell Immunol , vol.171 , pp. 159-163
    • Sower, L.E.1    Klimpel, G.R.2    Hanna, W.3    Froelich, C.J.4
  • 17
    • 0029871382 scopus 로고    scopus 로고
    • The serine protease granzyme A does not induce platelet aggregation but inhibits responses triggered by thrombin
    • Suidan H.S., Clemetson K.J., Brown-Luedi M., Niclou S.P., Clemetson J.M., Tschopp J., Monard D. The serine protease granzyme A does not induce platelet aggregation but inhibits responses triggered by thrombin. Biochem J. 315:1996;939-945.
    • (1996) Biochem J , vol.315 , pp. 939-945
    • Suidan, H.S.1    Clemetson, K.J.2    Brown-Luedi, M.3    Niclou, S.P.4    Clemetson, J.M.5    Tschopp, J.6    Monard, D.7
  • 18
    • 0028967988 scopus 로고
    • Synergistic roles of granzymes A and B in mediating target cell death by rat basophilic leukemia mast cell tumors also expressing cytolysin/perforin
    • Nakajima H., Park H.L., Henkart P.A. Synergistic roles of granzymes A and B in mediating target cell death by rat basophilic leukemia mast cell tumors also expressing cytolysin/perforin. J Exp Med. 181:1995;1037-1046.
    • (1995) J Exp Med , vol.181 , pp. 1037-1046
    • Nakajima, H.1    Park, H.L.2    Henkart, P.A.3
  • 19
    • 0030044052 scopus 로고    scopus 로고
    • Localization of granzyme B in the nucleus. A putative role in the mechanism of cytotoxic lymphocyte-mediated apoptosis
    • Trapani J.A., Browne K.A., Smyth M.J., Jans D.A. Localization of granzyme B in the nucleus. A putative role in the mechanism of cytotoxic lymphocyte-mediated apoptosis. J Biol Chem. 271:1996;4127-4133.
    • (1996) J Biol Chem , vol.271 , pp. 4127-4133
    • Trapani, J.A.1    Browne, K.A.2    Smyth, M.J.3    Jans, D.A.4
  • 21
    • 0026353348 scopus 로고
    • Granzyme A binding to target cell proteins. Granzyme A binds to and cleaves nucleolin in vitro
    • Pasternack M.S., Bleier K.J., McInerney T.N. Granzyme A binding to target cell proteins. Granzyme A binds to and cleaves nucleolin in vitro. J Biol Chem. 266:1991;14703-14708.
    • (1991) J Biol Chem , vol.266 , pp. 14703-14708
    • Pasternack, M.S.1    Bleier, K.J.2    McInerney, T.N.3
  • 22
    • 0035900714 scopus 로고    scopus 로고
    • Granzyme A activates an endoplasmic reticulum-associated caspase- independent nuclease to induce single-stranded DNA nicks
    • Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L., Jaju M., Lieberman J. Granzyme A activates an endoplasmic reticulum-associated caspase- independent nuclease to induce single-stranded DNA nicks. J Biol Chem. 276:2001;43285-43293.
    • (2001) J Biol Chem , vol.276 , pp. 43285-43293
    • Beresford, P.J.1    Zhang, D.2    Oh, D.Y.3    Fan, Z.4    Greer, E.L.5    Russo, M.L.6    Jaju, M.7    Lieberman, J.8
  • 23
    • 0028258577 scopus 로고
    • Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells
    • Heusel J.W., Wesselschmidt R.L., Shresta S., Russell J.H., Ley T.J. Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells. Cell. 76:1994;977-987.
    • (1994) Cell , vol.76 , pp. 977-987
    • Heusel, J.W.1    Wesselschmidt, R.L.2    Shresta, S.3    Russell, J.H.4    Ley, T.J.5
  • 24
    • 0030014911 scopus 로고    scopus 로고
    • Granzyme A is critical for recovery of mice from infection with the natural cytopathic viral pathogen, ectromelia
    • Mullbacher A., Ebnet K., Blanden R.V., Hla R.T., Stehle T., Museteanu C., Simon M.M. Granzyme A is critical for recovery of mice from infection with the natural cytopathic viral pathogen, ectromelia. Proc Natl Acad Sci USA. 93:1996;5783-5787.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5783-5787
    • Mullbacher, A.1    Ebnet, K.2    Blanden, R.V.3    Hla, R.T.4    Stehle, T.5    Museteanu, C.6    Simon, M.M.7
  • 25
    • 0033598718 scopus 로고    scopus 로고
    • Granzymes are the essential downstream effector molecules for the control of primary virus infections by cytolytic leukocytes
    • Mullbacher A., Waring P., Tha Hla R., Tran T., Chin S., Stehle T., Museteanu C., Simon M.M. Granzymes are the essential downstream effector molecules for the control of primary virus infections by cytolytic leukocytes. Proc Natl Acad Sci USA. 96:1999;13950-13955.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13950-13955
    • Mullbacher, A.1    Waring, P.2    Tha Hla, R.3    Tran, T.4    Chin, S.5    Stehle, T.6    Museteanu, C.7    Simon, M.M.8
  • 26
    • 0033986159 scopus 로고    scopus 로고
    • Granzyme A, a noncytolytic component of CD8(+) cell granules, restricts the spread of herpes simplex virus in the peripheral nervous systems of experimentally infected mice
    • Pereira R.A., Simon M.M., Simmons A. Granzyme A, a noncytolytic component of CD8(+) cell granules, restricts the spread of herpes simplex virus in the peripheral nervous systems of experimentally infected mice. J Virol. 74:2000;1029-1032.
    • (2000) J Virol , vol.74 , pp. 1029-1032
    • Pereira, R.A.1    Simon, M.M.2    Simmons, A.3
  • 28
    • 0029914132 scopus 로고    scopus 로고
    • A cytosolic granzyme B inhibitor related to the viral apoptotic regulator cytokine response modifier A is present in cytotoxic lymphocytes
    • Sun J., Bird C.H., Sutton V., McDonald L., Coughlin P.B., DeJong T.A., Trapani J.A., Bird P.I. A cytosolic granzyme B inhibitor related to the viral apoptotic regulator cytokine response modifier A is present in cytotoxic lymphocytes. J Biol Chem. 271:1996;27802-27809.
    • (1996) J Biol Chem , vol.271 , pp. 27802-27809
    • Sun, J.1    Bird, C.H.2    Sutton, V.3    McDonald, L.4    Coughlin, P.B.5    DeJong, T.A.6    Trapani, J.A.7    Bird, P.I.8
  • 29
    • 0031008162 scopus 로고    scopus 로고
    • A new family of 10 murine ovalbumin serpins includes two homologs of proteinase inhibitor 8 and two homologs of the granzyme B inhibitor (proteinase inhibitor 9)
    • Sun J., Ooms L., Bird C.H., Sutton V.R., Trapani J.A., Bird P.I. A new family of 10 murine ovalbumin serpins includes two homologs of proteinase inhibitor 8 and two homologs of the granzyme B inhibitor (proteinase inhibitor 9). J Biol Chem. 272:1997;15434-15441.
    • (1997) J Biol Chem , vol.272 , pp. 15434-15441
    • Sun, J.1    Ooms, L.2    Bird, C.H.3    Sutton, V.R.4    Trapani, J.A.5    Bird, P.I.6
  • 30
    • 0037687435 scopus 로고    scopus 로고
    • Purification and identification of a binding protein for pancreatic secretory trypsin inhibitor: A novel role of the inhibitor as an anti-granzyme A
    • The authors describe the first identification of a naturally occurring inhibitor of GzmA.
    • Tsuzuki S., Kokado Y., Satomi S., Yamasaki Y., Hirayasu H., Iwanaga T., Fushiki T. Purification and identification of a binding protein for pancreatic secretory trypsin inhibitor: a novel role of the inhibitor as an anti-granzyme A. Biochem J. 372:2003;227-233 The authors describe the first identification of a naturally occurring inhibitor of GzmA.
    • (2003) Biochem J , vol.372 , pp. 227-233
    • Tsuzuki, S.1    Kokado, Y.2    Satomi, S.3    Yamasaki, Y.4    Hirayasu, H.5    Iwanaga, T.6    Fushiki, T.7
  • 31
    • 0034651593 scopus 로고    scopus 로고
    • Extracellular granzyme A, complexed to proteoglycans, is protected against inactivation by protease inhibitors
    • Spaeny-Dekking E.H., Kamp A.M., Froelich C.J., Hack C.E. Extracellular granzyme A, complexed to proteoglycans, is protected against inactivation by protease inhibitors. Blood. 95:2000;1465-1472.
    • (2000) Blood , vol.95 , pp. 1465-1472
    • Spaeny-Dekking, E.H.1    Kamp, A.M.2    Froelich, C.J.3    Hack, C.E.4
  • 33
    • 0035826778 scopus 로고    scopus 로고
    • Granzymes A and B directly cleave lamins and disrupt the nuclear lamina during granule-mediated cytolysis
    • Zhang D., Beresford P.J., Greenberg A.H., Lieberman J. Granzymes A and B directly cleave lamins and disrupt the nuclear lamina during granule-mediated cytolysis. Proc Natl Acad Sci USA. 98:2001;5746-5751.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5746-5751
    • Zhang, D.1    Beresford, P.J.2    Greenberg, A.H.3    Lieberman, J.4
  • 34
    • 0037318731 scopus 로고    scopus 로고
    • Cleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme A
    • The authors show that Ape1 is part of the SET complex; GzmA cleavage of Ape1 prevents the cell from repairing damage and recovering.
    • Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A., Pommier Y., Lieberman J. Cleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme A. Nat Immunol. 4:2003;145-153 The authors show that Ape1 is part of the SET complex; GzmA cleavage of Ape1 prevents the cell from repairing damage and recovering.
    • (2003) Nat Immunol , vol.4 , pp. 145-153
    • Fan, Z.1    Beresford, P.J.2    Zhang, D.3    Xu, Z.4    Novina, C.D.5    Yoshida, A.6    Pommier, Y.7    Lieberman, J.8
  • 35
    • 0037423932 scopus 로고    scopus 로고
    • Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor
    • This paper identifies NM23-H1 as the GzmA-activated DNase and provides the first description of a caspase-independent mechanism of apoptotic DNA damage.
    • Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J. Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell. 112:2003;659-672 This paper identifies NM23-H1 as the GzmA-activated DNase and provides the first description of a caspase-independent mechanism of apoptotic DNA damage.
    • (2003) Cell , vol.112 , pp. 659-672
    • Fan, Z.1    Beresford, P.J.2    Oh, D.Y.3    Zhang, D.4    Lieberman, J.5
  • 36
    • 0030787867 scopus 로고    scopus 로고
    • Recombinant human granzyme A binds to two putative HLA-associated proteins and cleaves one of them
    • Beresford P.J., Kam C.M., Powers J.C., Lieberman J. Recombinant human granzyme A binds to two putative HLA-associated proteins and cleaves one of them. Proc Natl Acad Sci USA. 94:1997;9285-9290.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9285-9290
    • Beresford, P.J.1    Kam, C.M.2    Powers, J.C.3    Lieberman, J.4
  • 37
    • 0036199666 scopus 로고    scopus 로고
    • HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme A
    • Fan Z., Beresford P.J., Zhang D., Lieberman J. HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme A. Mol Cell Biol. 22:2002;2810-2820.
    • (2002) Mol Cell Biol , vol.22 , pp. 2810-2820
    • Fan, Z.1    Beresford, P.J.2    Zhang, D.3    Lieberman, J.4
  • 38
    • 0034597057 scopus 로고    scopus 로고
    • Protein ligands to HuR modulate its interaction with target mRNAs in vivo
    • Brennan C.M., Gallouzi I.E., Steitz J.A. Protein ligands to HuR modulate its interaction with target mRNAs in vivo. J Cell Biol. 151:2000;1-14.
    • (2000) J Cell Biol , vol.151 , pp. 1-14
    • Brennan, C.M.1    Gallouzi, I.E.2    Steitz, J.A.3
  • 39
    • 0034462693 scopus 로고    scopus 로고
    • Functional interaction between nucleosome assembly proteins and p300/CREB-binding protein family coactivators
    • Shikama N., Chan H.M., Krstic-Demonacos M., Smith L., Lee C.W., Cairns W., La Thangue N.B. Functional interaction between nucleosome assembly proteins and p300/CREB-binding protein family coactivators. Mol Cell Biol. 20:2000;8933-8943.
    • (2000) Mol Cell Biol , vol.20 , pp. 8933-8943
    • Shikama, N.1    Chan, H.M.2    Krstic-Demonacos, M.3    Smith, L.4    Lee, C.W.5    Cairns, W.6    La Thangue, N.B.7
  • 40
    • 0034850959 scopus 로고    scopus 로고
    • Protein ligands mediate the CRM1-dependent export of HuR in response to heat shock
    • Gallouzi I.E., Brennan C.M., Steitz J.A. Protein ligands mediate the CRM1-dependent export of HuR in response to heat shock. RNA. 7:2001;1348-1361.
    • (2001) RNA , vol.7 , pp. 1348-1361
    • Gallouzi, I.E.1    Brennan, C.M.2    Steitz, J.A.3
  • 41
    • 0035846894 scopus 로고    scopus 로고
    • Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein
    • Seo S., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D. Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein. Cell. 104:2001;119-130.
    • (2001) Cell , vol.104 , pp. 119-130
    • Seo, S.1    McNamara, P.2    Heo, S.3    Turner, A.4    Lane, W.S.5    Chakravarti, D.6
  • 42
    • 0037134538 scopus 로고    scopus 로고
    • Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex
    • Seo S.B., Macfarlan T., McNamara P., Hong R., Mukai Y., Heo S., Chakravarti D. Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex. J Biol Chem. 277:2002;14005-14010.
    • (2002) J Biol Chem , vol.277 , pp. 14005-14010
    • Seo, S.B.1    Macfarlan, T.2    McNamara, P.3    Hong, R.4    Mukai, Y.5    Heo, S.6    Chakravarti, D.7
  • 43
    • 0037067661 scopus 로고    scopus 로고
    • The oncoprotein Set/TAF-1beta, an inhibitor of histone acetyltransferase, inhibits active demethylation of DNA, integrating DNA methylation and transcriptional silencing
    • Cervoni N., Detich N., Seo S.B., Chakravarti D., Szyf M. The oncoprotein Set/TAF-1beta, an inhibitor of histone acetyltransferase, inhibits active demethylation of DNA, integrating DNA methylation and transcriptional silencing. J Biol Chem. 277:2002;25026-25031.
    • (2002) J Biol Chem , vol.277 , pp. 25026-25031
    • Cervoni, N.1    Detich, N.2    Seo, S.B.3    Chakravarti, D.4    Szyf, M.5
  • 44
    • 0037423949 scopus 로고    scopus 로고
    • SET-ting the stage for life and death
    • Chakravarti D., Hong R. SET-ting the stage for life and death. Cell. 112:2003;589-591.
    • (2003) Cell , vol.112 , pp. 589-591
    • Chakravarti, D.1    Hong, R.2
  • 45
    • 0037428217 scopus 로고    scopus 로고
    • Distinctive roles of PHAP proteins and prothymosin-alpha in a death regulatory pathway
    • This study implicates pp32 in activating the apoptosome in caspase-mediated cell death.
    • Jiang X., Kim H.E., Shu H., Zhao Y., Zhang H., Kofron J., Donnelly J., Burns D., Ng S.C., Rosenberg S.et al. Distinctive roles of PHAP proteins and prothymosin-alpha in a death regulatory pathway. Science. 299:2003;223-226 This study implicates pp32 in activating the apoptosome in caspase-mediated cell death.
    • (2003) Science , vol.299 , pp. 223-226
    • Jiang, X.1    Kim, H.E.2    Shu, H.3    Zhao, Y.4    Zhang, H.5    Kofron, J.6    Donnelly, J.7    Burns, D.8    Ng, S.C.9    Rosenberg, S.10
  • 46
    • 0034160089 scopus 로고    scopus 로고
    • An 'environment to nucleus' signaling system operates in B lymphocytes: Redox status modulates BSAP/Pax-5 activation through Ref-1 nuclear translocation
    • Tell G., Zecca A., Pellizzari L., Spessotto P., Colombatti A., Kelley M.R., Damante G., Pucillo C. An 'environment to nucleus' signaling system operates in B lymphocytes: redox status modulates BSAP/Pax-5 activation through Ref-1 nuclear translocation. Nucleic Acids Res. 28:2000;1099-1105.
    • (2000) Nucleic Acids Res , vol.28 , pp. 1099-1105
    • Tell, G.1    Zecca, A.2    Pellizzari, L.3    Spessotto, P.4    Colombatti, A.5    Kelley, M.R.6    Damante, G.7    Pucillo, C.8
  • 47
    • 0026323008 scopus 로고
    • Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: Definition of a family of DNA repair enzymes
    • Demple B., Herman T., Chen D.S. Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes. Proc Natl Acad Sci USA. 88:1991;11450-11454.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11450-11454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 48
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • Xanthoudakis S., Miao G., Wang F., Pan Y.C., Curran T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J. 11:1992;3323-3335.
    • (1992) EMBO J , vol.11 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.C.4    Curran, T.5
  • 49
    • 0026583944 scopus 로고
    • Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity
    • Xanthoudakis S., Curran T. Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. EMBO J. 11:1992;653-665.
    • (1992) EMBO J , vol.11 , pp. 653-665
    • Xanthoudakis, S.1    Curran, T.2
  • 51
    • 0026693436 scopus 로고
    • Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3′ half to different genes: Characterization of the set gene
    • von Lindern M., van Baal S., Wiegant J., Raap A., Hagemeijer A., Grosveld G. Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3′ half to different genes: characterization of the set gene. Mol Cell Biol. 12:1992;3346-3355.
    • (1992) Mol Cell Biol , vol.12 , pp. 3346-3355
    • Von Lindern, M.1    Van Baal, S.2    Wiegant, J.3    Raap, A.4    Hagemeijer, A.5    Grosveld, G.6
  • 53
    • 0032827034 scopus 로고    scopus 로고
    • Sperm chromatin decondensation by template activating factor I through direct interaction with basic proteins
    • Matsumoto K., Nagata K., Miyaji-Yamaguchi M., Kikuchi A., Tsujimoto M. Sperm chromatin decondensation by template activating factor I through direct interaction with basic proteins. Mol Cell Biol. 19:1999;6940-6952.
    • (1999) Mol Cell Biol , vol.19 , pp. 6940-6952
    • Matsumoto, K.1    Nagata, K.2    Miyaji-Yamaguchi, M.3    Kikuchi, A.4    Tsujimoto, M.5
  • 54
    • 0033407137 scopus 로고    scopus 로고
    • Histone- and chromatin-binding activity of template activating factor-I
    • Matsumoto K., Nagata K., Okuwaki M., Tsujimoto M. Histone- and chromatin-binding activity of template activating factor-I. FEBS Lett. 463:1999;285-288.
    • (1999) FEBS Lett , vol.463 , pp. 285-288
    • Matsumoto, K.1    Nagata, K.2    Okuwaki, M.3    Tsujimoto, M.4
  • 55
    • 0027263966 scopus 로고
    • Template activating factor I, a novel host factor required to stimulate the adenovirus core DNA replication
    • Matsumoto K., Nagata K., Ui M., Hanaoka F. Template activating factor I, a novel host factor required to stimulate the adenovirus core DNA replication. J Biol Chem. 268:1993;10582-10587.
    • (1993) J Biol Chem , vol.268 , pp. 10582-10587
    • Matsumoto, K.1    Nagata, K.2    Ui, M.3    Hanaoka, F.4
  • 56
    • 0028898807 scopus 로고
    • Stimulation of DNA transcription by the replication factor from the adenovirus genome in a chromatin-like structure
    • Matsumoto K., Okuwaki M., Kawase H., Handa H., Hanaoka F., Nagata K. Stimulation of DNA transcription by the replication factor from the adenovirus genome in a chromatin-like structure. J Biol Chem. 270:1995;9645-9650.
    • (1995) J Biol Chem , vol.270 , pp. 9645-9650
    • Matsumoto, K.1    Okuwaki, M.2    Kawase, H.3    Handa, H.4    Hanaoka, F.5    Nagata, K.6
  • 57
    • 0030723205 scopus 로고    scopus 로고
    • HRX leukemic fusion proteins form a heterocomplex with the leukemia-associated protein SET and protein phosphatase 2A
    • Adler H.T., Nallaseth F.S., Walter G., Tkachuk D.C. HRX leukemic fusion proteins form a heterocomplex with the leukemia-associated protein SET and protein phosphatase 2A. J Biol Chem. 272:1997;28407-28414.
    • (1997) J Biol Chem , vol.272 , pp. 28407-28414
    • Adler, H.T.1    Nallaseth, F.S.2    Walter, G.3    Tkachuk, D.C.4
  • 58
    • 0035912064 scopus 로고    scopus 로고
    • Tumor suppression and potentiation by manipulation of pp32 expression
    • Bai J., Brody J.R., Kadkol S.S., Pasternack G.R. Tumor suppression and potentiation by manipulation of pp32 expression. Oncogene. 20:2001;2153-2160.
    • (2001) Oncogene , vol.20 , pp. 2153-2160
    • Bai, J.1    Brody, J.R.2    Kadkol, S.S.3    Pasternack, G.R.4
  • 59
    • 0029665228 scopus 로고    scopus 로고
    • PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A
    • PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A. Biochemistry. 35:1996;6998-7002.
    • (1996) Biochemistry , vol.35 , pp. 6998-7002
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 60
    • 0029889342 scopus 로고    scopus 로고
    • The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A
    • Li M., Makkinje A., Damuni Z. The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A. J Biol Chem. 271:1996;11059-11062.
    • (1996) J Biol Chem , vol.271 , pp. 11059-11062
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 61
    • 0025103372 scopus 로고
    • Polyoma small and middle T antigens and SV40 small t antigen form stable complexes with protein phosphatase 2A
    • Pallas D.C., Shahrik L.K., Martin B.L., Jaspers S., Miller T.B., Brautigan D.L., Roberts T.M. Polyoma small and middle T antigens and SV40 small t antigen form stable complexes with protein phosphatase 2A. Cell. 60:1990;167-176.
    • (1990) Cell , vol.60 , pp. 167-176
    • Pallas, D.C.1    Shahrik, L.K.2    Martin, B.L.3    Jaspers, S.4    Miller, T.B.5    Brautigan, D.L.6    Roberts, T.M.7
  • 63
    • 0037059740 scopus 로고    scopus 로고
    • NM23-H1 and NM23-H2 repress transcriptional activities of nuclease- hypersensitive elements in the platelet-derived growth factor-A promoter
    • Ma D., Xing Z., Liu B., Pedigo N.G., Zimmer S.G., Bai Z., Postel E.H., Kaetzel D.M. NM23-H1 and NM23-H2 repress transcriptional activities of nuclease- hypersensitive elements in the platelet-derived growth factor-A promoter. J Biol Chem. 277:2002;1560-1567.
    • (2002) J Biol Chem , vol.277 , pp. 1560-1567
    • Ma, D.1    Xing, Z.2    Liu, B.3    Pedigo, N.G.4    Zimmer, S.G.5    Bai, Z.6    Postel, E.H.7    Kaetzel, D.M.8
  • 64
    • 0033795962 scopus 로고    scopus 로고
    • Nm23/nucleoside diphosphate kinase in human cancers
    • Hartsough M.T., Steeg P.S. Nm23/nucleoside diphosphate kinase in human cancers. J Bioenerg Biomembr. 32:2000;301-308.
    • (2000) J Bioenerg Biomembr , vol.32 , pp. 301-308
    • Hartsough, M.T.1    Steeg, P.S.2
  • 65
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu X., Zou H., Slaughter C., Wang X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell. 89:1997;175-184.
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 66
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • Sakahira H., Enari M., Nagata S. Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. Nature. 391:1998;96-99.
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 67
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M., Sakahira H., Yokohama H., Okawa K., Iwamatsu A., Nagata S. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature. 391:1998;43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokohama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 68
    • 0033673428 scopus 로고    scopus 로고
    • DFF45/ICAD can be directly processed by granzyme B during the induction of apoptosis
    • Thomas D.A., Du C., Xu M., Wang X., Ley T.J. DFF45/ICAD can be directly processed by granzyme B during the induction of apoptosis. Immunity. 12:2000;621-632.
    • (2000) Immunity , vol.12 , pp. 621-632
    • Thomas, D.A.1    Du, C.2    Xu, M.3    Wang, X.4    Ley, T.J.5
  • 71
    • 0022648101 scopus 로고
    • Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins
    • McKeon F.D., Kirschner M.W., Caput D. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature. 319:1986;463-468.
    • (1986) Nature , vol.319 , pp. 463-468
    • McKeon, F.D.1    Kirschner, M.W.2    Caput, D.3
  • 72
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter M., Nakagawa J., Doree M., Labbe J.C., Nigg E.A. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell. 61:1990;591-602.
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 73
    • 0027989510 scopus 로고
    • Chromatin condensation during apoptosis is accompanied by degradation of lamin A+B, without enhanced activation of cdc2 kinase
    • Oberhammer F.A., Hochegger K., Froschl G., Tiefenbacher R., Pavelka M. Chromatin condensation during apoptosis is accompanied by degradation of lamin A+B, without enhanced activation of cdc2 kinase. J Cell Biol. 126:1994;827-837.
    • (1994) J Cell Biol , vol.126 , pp. 827-837
    • Oberhammer, F.A.1    Hochegger, K.2    Froschl, G.3    Tiefenbacher, R.4    Pavelka, M.5
  • 74
    • 0030465544 scopus 로고    scopus 로고
    • Lamin proteolysis facilitates nuclear events during apoptosis
    • Rao L., Perez D., White E. Lamin proteolysis facilitates nuclear events during apoptosis. J Cell Biol. 135:1996;1441-1455.
    • (1996) J Cell Biol , vol.135 , pp. 1441-1455
    • Rao, L.1    Perez, D.2    White, E.3
  • 77
    • 0038392751 scopus 로고    scopus 로고
    • The oligomeric structure of human granzyme A is a determinant of its extended substrate specificity
    • Bell J.K., Goetz D.H., Mahrus S., Harris J.L., Fletterick R.J., Craik C.S. The oligomeric structure of human granzyme A is a determinant of its extended substrate specificity. Nat Struct Biol. 10:2003;527-534.
    • (2003) Nat Struct Biol , vol.10 , pp. 527-534
    • Bell, J.K.1    Goetz, D.H.2    Mahrus, S.3    Harris, J.L.4    Fletterick, R.J.5    Craik, C.S.6


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