메뉴 건너뛰기




Volumn 76, Issue 2-3, 1998, Pages 351-358

RING fingers and B-boxes: Zinc-binding protein-protein interaction domains

Author keywords

B box; NMR; PML; RING

Indexed keywords

BINDING PROTEIN;

EID: 0032463343     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o98-021     Document Type: Review
Times cited : (242)

References (44)
  • 1
    • 0028861418 scopus 로고
    • The PhD finger: Implications for chromatin mediated transcriptional regulation
    • Aasland, R., Gibson, T.J., and Stewart, A.F. 1995. The PhD finger: implications for chromatin mediated transcriptional regulation. Trends Biochem. Sci. 20: 56-59.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 56-59
    • Aasland, R.1    Gibson, T.J.2    Stewart, A.F.3
  • 3
    • 0028883688 scopus 로고
    • A zinc-binding domain is required for targeting the maternal nuclear protein PwA33 to lampbrush chromosome loops
    • Bellini, M., Lacroix, T.C., and Gall, J.G. 1995. A zinc-binding domain is required for targeting the maternal nuclear protein PwA33 to lampbrush chromosome loops. J. Cell Biol. 131: 563-570.
    • (1995) J. Cell Biol. , vol.131 , pp. 563-570
    • Bellini, M.1    Lacroix, T.C.2    Gall, J.G.3
  • 4
    • 0030959658 scopus 로고    scopus 로고
    • The crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel xinc binuclear cluster
    • Bellon, S.F., Rodgers, K.K., Schatz, D.G., Coleman, J.E., and Steitz, T.A. 1997. The crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel xinc binuclear cluster. Nat. Struct. Biol. 4: 586-591.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 586-591
    • Bellon, S.F.1    Rodgers, K.K.2    Schatz, D.G.3    Coleman, J.E.4    Steitz, T.A.5
  • 5
    • 0028277934 scopus 로고
    • The p53 associated protein MDM2, contains a newly characterised zinc-binding domain called the RING finger
    • Boddy, M.N., Freemont, P.S., and Borden, K.L.B. 1994. The p53 associated protein MDM2, contains a newly characterised zinc-binding domain called the RING finger. Trends Biochem. Sci. 19: 198-199.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 198-199
    • Boddy, M.N.1    Freemont, P.S.2    Borden, K.L.B.3
  • 6
    • 0030796314 scopus 로고    scopus 로고
    • Surface residue mutations of the PML RING finger domain alters the formation of nuclear matrix-associated PML bodies
    • Boddy, M.N., Duprez, E., Borden, K.L.B., and Freemont, P.S. 1997. Surface residue mutations of the PML RING finger domain alters the formation of nuclear matrix-associated PML bodies. J. Cell Sci. 110: 2197-2205.
    • (1997) J. Cell Sci. , vol.110 , pp. 2197-2205
    • Boddy, M.N.1    Duprez, E.2    Borden, K.L.B.3    Freemont, P.S.4
  • 7
    • 0029977716 scopus 로고    scopus 로고
    • The RING finger: An example of a sequence structure family
    • Borden, K.L.B., and Freemont P.S. 1996. The RING finger: an example of a sequence structure family. Curr. Opin. Struct. Biol. 6: 395-401.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 395-401
    • Borden, K.L.B.1    Freemont, P.S.2
  • 8
    • 0027422113 scopus 로고
    • Characterisation of a novel cysteine/histidine rich metal binding domain from Xenopus nuclear factor 7
    • Borden, K.L.B., Martin, S., O'Reilly, N., Lally, J.M., Bramham, R.A., Eitkin, L., and Freemont, P.S. 1993. Characterisation of a novel cysteine/histidine rich metal binding domain from Xenopus nuclear factor 7. FEBS Lett. 335: 255-260.
    • (1993) FEBS Lett. , vol.335 , pp. 255-260
    • Borden, K.L.B.1    Martin, S.2    O'Reilly, N.3    Lally, J.M.4    Bramham, R.A.5    Eitkin, L.6    Freemont, P.S.7
  • 9
    • 0028932963 scopus 로고
    • The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein, pml
    • Borden, K.L.B., Boddy, M.N., Lally, J., O'Reilly, N.J., Martin, S., Howe, K., Solomon, E., and Freemont, P.S. 1995a. The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein, pml. EMBO J. 14: 1532-1541.
    • (1995) EMBO J. , vol.14 , pp. 1532-1541
    • Borden, K.L.B.1    Boddy, M.N.2    Lally, J.3    O'Reilly, N.J.4    Martin, S.5    Howe, K.6    Solomon, E.7    Freemont, P.S.8
  • 11
    • 0029918562 scopus 로고    scopus 로고
    • In vivo and in vitro characterisation of the B1 and B2 zinc-binding domains from the acute promylocytic leukemia proto-oncoprotein PML
    • Borden, K.L.B., Lally, J.M., Martin, S.R., O'Reilly, N.J., Solomon, E., and Freemont, P.S. 1996. In vivo and in vitro characterisation of the B1 and B2 zinc-binding domains from the acute promylocytic leukemia proto-oncoprotein PML. Proc. Natl. Acad. Sci. U.S.A. 93: 1601-1606.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1601-1606
    • Borden, K.L.B.1    Lally, J.M.2    Martin, S.R.3    O'Reilly, N.J.4    Solomon, E.5    Freemont, P.S.6
  • 12
    • 0030817386 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein PML has a pro-apoptotic activity mediated through its RING
    • Borden, K.L.B., CampbellDwyer, E.J., and Salvato, M.S. 1997. The promyelocytic leukemia protein PML has a pro-apoptotic activity mediated through its RING. FEBS Lett. 418: 30-34.
    • (1997) FEBS Lett. , vol.418 , pp. 30-34
    • Borden, K.L.B.1    CampbellDwyer, E.J.2    Salvato, M.S.3
  • 13
    • 2642670320 scopus 로고    scopus 로고
    • The promyleocytic leukemia protein nuclear body function: New insights from lymphocytic choriomeningits virus infection
    • Borden, K.L.B., CampbellDwyer, E.J., and Salvato, M.S. 1998. The promyleocytic leukemia protein nuclear body function: new insights from lymphocytic choriomeningits virus infection. J. Virol. 72: 758-766.
    • (1998) J. Virol. , vol.72 , pp. 758-766
    • Borden, K.L.B.1    CampbellDwyer, E.J.2    Salvato, M.S.3
  • 14
    • 0030751654 scopus 로고    scopus 로고
    • Involvement of the rfp tripartite motif in protein protein interactions and subcellular distribution
    • Cao, T., Borden, K.L.B., Freemont, P.S., and Etkin, L.D. 1997. Involvement of the rfp tripartite motif in protein protein interactions and subcellular distribution. J. Cell Sci. 110: 1563-1571.
    • (1997) J. Cell Sci. , vol.110 , pp. 1563-1571
    • Cao, T.1    Borden, K.L.B.2    Freemont, P.S.3    Etkin, L.D.4
  • 16
    • 0030052130 scopus 로고    scopus 로고
    • Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure
    • Doucas, V., Ishov, A.M., Romo, A. Juguilon, J., Weitzman, M., Evans, R.M., and Maul, G.G. 1996. Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure. Genes Dev. 10: 196-207.
    • (1996) Genes Dev. , vol.10 , pp. 196-207
    • Doucas, V.1    Ishov, A.M.2    Romo, A.3    Juguilon, J.4    Weitzman, M.5    Evans, R.M.6    Maul, G.G.7
  • 17
    • 0027239790 scopus 로고
    • The RING finger. A novel protein sequence
    • Freemont, P.S. 1993. The RING finger. A novel protein sequence. Ann. N.Y. Acad. Sci. 684: 174-192.
    • (1993) Ann. N.Y. Acad. Sci. , vol.684 , pp. 174-192
    • Freemont, P.S.1
  • 18
    • 0025977953 scopus 로고
    • A novel cysteine-rich sequence motif
    • Freemont, P.S., Hanson, I.M., and Trowsdale, J. 1991. A novel cysteine-rich sequence motif. Cell, 64: 483-484.
    • (1991) Cell , vol.64 , pp. 483-484
    • Freemont, P.S.1    Hanson, I.M.2    Trowsdale, J.3
  • 19
    • 0027485083 scopus 로고
    • Comparison of conformational characteristics in structurally similar protein pairs
    • Flores, T.P., Orengo, C.A., Moss, D.S., and Thornton, J.M. 1993. Comparison of conformational characteristics in structurally similar protein pairs. Protein Sci. 2: 1811-1826.
    • (1993) Protein Sci. , vol.2 , pp. 1811-1826
    • Flores, T.P.1    Orengo, C.A.2    Moss, D.S.3    Thornton, J.M.4
  • 20
    • 0029646094 scopus 로고
    • The enigma of the LIM domains
    • Gill, G.N. 1995. The enigma of the LIM domains. Structure (London), 3: 1285-1289.
    • (1995) Structure (London) , vol.3 , pp. 1285-1289
    • Gill, G.N.1
  • 21
    • 0026326963 scopus 로고
    • Characterization of a zinc finger gene disrupted by the t(15:17) in acute promyelocytic leukemia
    • Goddard, A.D., Borrow, J., Freemont, P.S., and Solomon, E. 1991. Characterization of a zinc finger gene disrupted by the t(15:17) in acute promyelocytic leukemia. Science (Washington, D.C.), 254: 1371-1373.
    • (1991) Science (Washington, D.C.) , vol.254 , pp. 1371-1373
    • Goddard, A.D.1    Borrow, J.2    Freemont, P.S.3    Solomon, E.4
  • 22
    • 0025727771 scopus 로고
    • Novel zinc finger gene implicated as myc collaborator by retrovirally accelerated lymphomagenesis in E mu-myc transgenic mice
    • Haupt, Y., Alexander, W.S., Barri, G., Klinker, S.P., and Adams, J.M. 1991. Novel zinc finger gene implicated as myc collaborator by retrovirally accelerated lymphomagenesis in E mu-myc transgenic mice. Cell, 65: 753-763.
    • (1991) Cell , vol.65 , pp. 753-763
    • Haupt, Y.1    Alexander, W.S.2    Barri, G.3    Klinker, S.P.4    Adams, J.M.5
  • 23
    • 0029838230 scopus 로고    scopus 로고
    • The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition
    • Ishov, A.M., and Maul, G.G. 1996. The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition. J. Cell Biol. 134: 815-826.
    • (1996) J. Cell Biol. , vol.134 , pp. 815-826
    • Ishov, A.M.1    Maul, G.G.2
  • 24
    • 0026583943 scopus 로고
    • Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): Structural similarities with a new family of oncoproteins
    • Kastner, P., Perez, A., Lutz, Y., Rochette-Egly, C., Gaub, B., Durnad, M., Lanotte, M., Berger, R., and Chambon, P. 1992. Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins. EMBO J. 11: 629-642.
    • (1992) EMBO J. , vol.11 , pp. 629-642
    • Kastner, P.1    Perez, A.2    Lutz, Y.3    Rochette-Egly, C.4    Gaub, B.5    Durnad, M.6    Lanotte, M.7    Berger, R.8    Chambon, P.9
  • 25
    • 0028972538 scopus 로고
    • Disruption of PML-associated nuclear bodies during human cytomegalovirus infection
    • Kelly, C., Van Driel, R., and Wilkinson, G.W.G. 1995. Disruption of PML-associated nuclear bodies during human cytomegalovirus infection. J. Gen. Virol. 76: 2887-2893.
    • (1995) J. Gen. Virol. , vol.76 , pp. 2887-2893
    • Kelly, C.1    Van Driel, R.2    Wilkinson, G.W.G.3
  • 26
    • 0029024780 scopus 로고
    • Molecular characterization of NDP52, a novel protein of the nuclear domain 10, which is redistributed upon virus infection and interferon treatment
    • Korioth, F., Gieffers, C., Maul, G.G., and Frey, J. 1995. Molecular characterization of NDP52, a novel protein of the nuclear domain 10, which is redistributed upon virus infection and interferon treatment. J. Cell Biol. 130: 1-13.
    • (1995) J. Cell Biol. , vol.130 , pp. 1-13
    • Korioth, F.1    Gieffers, C.2    Maul, G.G.3    Frey, J.4
  • 27
    • 0030027449 scopus 로고    scopus 로고
    • Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene PML
    • Le, X.F., Yang P., and Chang, K.S. 1996. Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene PML. J. Biol. Chem. 271: 130-135.
    • (1996) J. Biol. Chem. , vol.271 , pp. 130-135
    • Le, X.F.1    Yang, P.2    Chang, K.S.3
  • 29
    • 0027769358 scopus 로고
    • Modification of discrete nuclear domains induced by herpes simplex virus type-1 immediate early gene 1 product (ICP0)
    • Maul, G.G., Guldner, H.H., and Spivack, J.G. 1993. Modification of discrete nuclear domains induced by herpes simplex virus type-1 immediate early gene 1 product (ICP0). J. Gen. Virol. 74: 2679-2690.
    • (1993) J. Gen. Virol. , vol.74 , pp. 2679-2690
    • Maul, G.G.1    Guldner, H.H.2    Spivack, J.G.3
  • 30
    • 0029583591 scopus 로고
    • Nuclear domain 10 (ND10) associated proteins are present in nuclear bodies and redistribute to hundreds of nuclear sites after stress
    • Maul, G.G., Yu, E., Ishov, A.M., and Epstein, A.L. 1995. Nuclear domain 10 (ND10) associated proteins are present in nuclear bodies and redistribute to hundreds of nuclear sites after stress. J. Cell. Biochem. 59: 499-514.
    • (1995) J. Cell. Biochem. , vol.59 , pp. 499-514
    • Maul, G.G.1    Yu, E.2    Ishov, A.M.3    Epstein, A.L.4
  • 31
    • 0029862620 scopus 로고    scopus 로고
    • Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1
    • Maul, G.G., Ishov, A.M., and Everett, R.D. 1996. Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1. Virology, 217: 67-75.
    • (1996) Virology , vol.217 , pp. 67-75
    • Maul, G.G.1    Ishov, A.M.2    Everett, R.D.3
  • 32
    • 0028095410 scopus 로고
    • A growth suppressor disrupted in acute promyelocytic leukemia
    • Mu, Z.-M., Chin, K.-V., Liu, J.-H., Lozano, G., and Chang, K.-S. 1994. A growth suppressor disrupted in acute promyelocytic leukemia. Mol. Cell. Biol. 14: 6858-6867.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6858-6867
    • Mu, Z.-M.1    Chin, K.-V.2    Liu, J.-H.3    Lozano, G.4    Chang, K.-S.5
  • 33
    • 0025917413 scopus 로고
    • Structure and origin of the acute promyelocytic leukemia myL/RARa cDNA and characterization of its retinoid-binding and transactivation properties
    • Pandolfi, P.P., Grignani, F., Alcalay, M., Mencarelli, A., Biondi, A., LoCoco, F., Grignani, F., and Pellicci, P.G. 1991. Structure and origin of the acute promyelocytic leukemia myL/RARa cDNA and characterization of its retinoid-binding and transactivation properties. Oncogene, 6: 1285-1292.
    • (1991) Oncogene , vol.6 , pp. 1285-1292
    • Pandolfi, P.P.1    Grignani, F.2    Alcalay, M.3    Mencarelli, A.4    Biondi, A.5    LoCoco, F.6    Grignani, F.7    Pellicci, P.G.8
  • 34
    • 0029032354 scopus 로고
    • Adenovirus infection induces rearrangements in the intranuclear distribution of the nuclear body associated PML protein
    • Puvion-Dutilleul, F., Chelbi-Alix, M.K., Koken, M., Quignon, F., Puvion, E., and de The, H. 1995. Adenovirus infection induces rearrangements in the intranuclear distribution of the nuclear body associated PML protein. Exp. Cell Res. 218: 9-16.
    • (1995) Exp. Cell Res. , vol.218 , pp. 9-16
    • Puvion-Dutilleul, F.1    Chelbi-Alix, M.K.2    Koken, M.3    Quignon, F.4    Puvion, E.5    De The, H.6
  • 35
    • 0026004844 scopus 로고
    • A unique bipartite cysteine-histidine motif defines a subfamily of potential zinc-finger proteins
    • Reddy, B.A., and Etkin, L.D. 1991. A unique bipartite cysteine-histidine motif defines a subfamily of potential zinc-finger proteins. Nucleic Acids Res. 19: 6330.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6330
    • Reddy, B.A.1    Etkin, L.D.2
  • 36
    • 0026782376 scopus 로고
    • A novel zinc finger coiled coil domain in a family of nuclear proteins
    • Reddy, B.A., Etkin, L.D., and Freemont, P.S. 1992. A novel zinc finger coiled coil domain in a family of nuclear proteins. Trends Biochem. Sci. 17: 344-345.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 344-345
    • Reddy, B.A.1    Etkin, L.D.2    Freemont, P.S.3
  • 37
    • 0028856787 scopus 로고
    • Presence of a new conserved domain in CART1, a novel member of the tumor necrosis factor receptor associated protein family which is expressed in breast carcinoma
    • Regnier, C.H., Tomasetto, C., Chenard, M.P., Wendling, C., Basset, P., and Rio, M.C. 1995. Presence of a new conserved domain in CART1, a novel member of the tumor necrosis factor receptor associated protein family which is expressed in breast carcinoma. J. Biol. Chem. 270: 25 715-25 721.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25715-25721
    • Regnier, C.H.1    Tomasetto, C.2    Chenard, M.P.3    Wendling, C.4    Basset, P.5    Rio, M.C.6
  • 38
    • 0028857948 scopus 로고
    • The leukemia-associated protein (LAP) domain, a cysteine rich motif, is present in a wide range of proteins including MLL, AF10 and MLLT6 proteins
    • Saha, V., Chaplin, T., Gregorini, A., Ayton, P., and Young, B.D. 1995. The leukemia-associated protein (LAP) domain, a cysteine rich motif, is present in a wide range of proteins including MLL, AF10 and MLLT6 proteins. Proc. Natl. Acad. Sci. U.S.A. 92: 9737-9741.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 9737-9741
    • Saha, V.1    Chaplin, T.2    Gregorini, A.3    Ayton, P.4    Young, B.D.5
  • 41
    • 0029912985 scopus 로고    scopus 로고
    • The Epstein-Barr virus encoded nuclear antigen EBNA-5 accumulates in PML-containing bodies
    • Szekely, L., Pokrovskaja, K., Jiang, W.-A., de The, H., Ringertz, N., and Klein, G. 1996. The Epstein-Barr virus encoded nuclear antigen EBNA-5 accumulates in PML-containing bodies. J. Virol. 70: 2562-2568.
    • (1996) J. Virol. , vol.70 , pp. 2562-2568
    • Szekely, L.1    Pokrovskaja, K.2    Jiang, W.-A.3    De The, H.4    Ringertz, N.5    Klein, G.6
  • 42
    • 0025875679 scopus 로고
    • The PML-RAR alpha fusion mRNA generated by t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR
    • de The, H.C., Lavau, C.A., Marchio, C., Chrornr, L., Degos, L., and Dejean, A. 1991. The PML-RAR alpha fusion mRNA generated by t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell, 66: 675-684.
    • (1991) Cell , vol.66 , pp. 675-684
    • De The, H.C.1    Lavau, C.A.2    Marchio, C.3    Chrornr, L.4    Degos, L.5    Dejean, A.6
  • 43
    • 0025863346 scopus 로고
    • Identification of cooperating oncogenes in E mu-myc transgenic mice by provirus tagging
    • van Lohuizen, M., Verbeek, S., Scheijen, B., Wientjens, E., van der Gulden, H., and Berns, A. 1991. Identification of cooperating oncogenes in E mu-myc transgenic mice by provirus tagging. Cell, 65: 753-763.
    • (1991) Cell , vol.65 , pp. 753-763
    • Van Lohuizen, M.1    Verbeek, S.2    Scheijen, B.3    Wientjens, E.4    Van Der Gulden, H.5    Berns, A.6
  • 44
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML-RARa in acute promyelocytic leukemia cells
    • Weiss, K., Rambaud, S., Lavau, C., Jansen, J., Carvalho, T., Carmo-Foneseca, M., Lamond, A., and Dejean, A. 1994. Retinoic acid regulates aberrant nuclear localization of PML-RARa in acute promyelocytic leukemia cells. Cell, 76: 345-356.
    • (1994) Cell , vol.76 , pp. 345-356
    • Weiss, K.1    Rambaud, S.2    Lavau, C.3    Jansen, J.4    Carvalho, T.5    Carmo-Foneseca, M.6    Lamond, A.7    Dejean, A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.