메뉴 건너뛰기




Volumn 31, Issue 22, 2003, Pages 6392-6408

Comparative analysis of editosome proteins in trypanosomatids

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA; NUCLEASE; NUCLEIC ACID; RIBONUCLEASE; RIBONUCLEASE III; RNA; RNA HELICASE; RNA LIGASE; ZINC FINGER PROTEIN;

EID: 0344668871     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkg870     Document Type: Review
Times cited : (78)

References (130)
  • 1
    • 0025189769 scopus 로고
    • A model for RNA editing in kinetoplastid mitochondria: 'Guide' RNA molecules transcribed from maxicircle DNA provide the edited information
    • Blum, B., Bakalara, N. and Simpson, L. (1990) A model for RNA editing in kinetoplastid mitochondria: 'guide' RNA molecules transcribed from maxicircle DNA provide the edited information. Cell, 60, 189-198.
    • (1990) Cell , vol.60 , pp. 189-198
    • Blum, B.1    Bakalara, N.2    Simpson, L.3
  • 3
    • 0030922796 scopus 로고    scopus 로고
    • The mechanism of U insertion/deletion RNA editing in kinetoplastid mitochondria
    • Alfonso, J.D., Thiemann, O. and Simpson, L. (1997) The mechanism of U insertion/deletion RNA editing in kinetoplastid mitochondria. Nucleic Acids Res., 25, 3751-3759.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3751-3759
    • Alfonso, J.D.1    Thiemann, O.2    Simpson, L.3
  • 4
    • 0033081421 scopus 로고    scopus 로고
    • Mapping contacts between gRNA and mRNA in the trypanosome RNA editing
    • Leung, S.S. and Koslowsky, D.J. (1999) Mapping contacts between gRNA and mRNA in the trypanosome RNA editing. Nucleic Acids Res., 27, 778-787.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 778-787
    • Leung, S.S.1    Koslowsky, D.J.2
  • 5
    • 0030848282 scopus 로고    scopus 로고
    • Disruption of a gene encoding a novel mitochondrial DEAD-box protein in Trypanosoma brucei affects edited mRNAs
    • Missel, A., Souza, A.E., Norskau, G. and Göringer, H.U. (1997) Disruption of a gene encoding a novel mitochondrial DEAD-box protein in Trypanosoma brucei affects edited mRNAs. Mol. Cell. Biol., 17, 4895-4903.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4895-4903
    • Missel, A.1    Souza, A.E.2    Norskau, G.3    Göringer, H.U.4
  • 7
    • 0036364353 scopus 로고    scopus 로고
    • RNA editing: Complexity and complications
    • Stuart, K. and Panigrahi, A.K. (2002) RNA editing: complexity and complications. Mol. Microbiol., 45, 591-596.
    • (2002) Mol. Microbiol. , vol.45 , pp. 591-596
    • Stuart, K.1    Panigrahi, A.K.2
  • 9
    • 0035896357 scopus 로고    scopus 로고
    • An RNA ligase essential for RNA editing and survival of the bloodstream form of Trypanosoma brucei
    • Schnaufer, A., Panigrahi, A.K., Panicucci, B., Igo, R.P., Jr, Wirtz, E., Salavati, R. and Stuart, K.D. (2001) An RNA ligase essential for RNA editing and survival of the bloodstream form of Trypanosoma brucei. Science, 291, 2159-2162.
    • (2001) Science , vol.291 , pp. 2159-2162
    • Schnaufer, A.1    Panigrahi, A.K.2    Panicucci, B.3    Igo Jr., R.P.4    Wirtz, E.5    Salavati, R.6    Stuart, K.D.7
  • 10
    • 0035801635 scopus 로고    scopus 로고
    • Roles for ligases in the RNA editing complex of Trypanosoma brucei: Band IV is needed for U-deletion and RNA repair
    • Huang, C.E., Cruz-Reyes, J., Zhelonkina, A.G., O'Hearn, S., Wirtz, E. and Sollner-Webb, B. (2001) Roles for ligases in the RNA editing complex of Trypanosoma brucei: band IV is needed for U-deletion and RNA repair. EMBO J., 20, 4694-4703.
    • (2001) EMBO J. , vol.20 , pp. 4694-4703
    • Huang, C.E.1    Cruz-Reyes, J.2    Zhelonkina, A.G.3    O'Hearn, S.4    Wirtz, E.5    Sollner-Webb, B.6
  • 11
    • 0036277208 scopus 로고    scopus 로고
    • Distinct functions of two RNA ligases in active Trypanosoma brucei RNA editing complexes
    • Cruz-Reyes, J., Zhelonkina, A.G., Huang, C.E. and Sollner-Webb, B. (2002) Distinct functions of two RNA ligases in active Trypanosoma brucei RNA editing complexes. Mol. Cell. Biol., 22, 4652-4660.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4652-4660
    • Cruz-Reyes, J.1    Zhelonkina, A.G.2    Huang, C.E.3    Sollner-Webb, B.4
  • 12
    • 0035260718 scopus 로고    scopus 로고
    • Identification of candidate mitochondrial RNA editing ligases from Trypanosoma brucei
    • McManus, M.T., Shimamura, M., Grams, J. and Hajduk, S.L. (2001) Identification of candidate mitochondrial RNA editing ligases from Trypanosoma brucei. RNA, 7, 167-175.
    • (2001) RNA , vol.7 , pp. 167-175
    • McManus, M.T.1    Shimamura, M.2    Grams, J.3    Hajduk, S.L.4
  • 13
    • 0038433297 scopus 로고    scopus 로고
    • TbMP57 is a 3′ terminal uridylyl transferase (TUTase) of the Trypanosoma brucei editosome
    • Ernst, N.L., Panicucci, B., Igo, R.P., Jr, Panigrahi, A.K., Salavati, R. and Stuart, K. (2003) TbMP57 is a 3′ terminal uridylyl transferase (TUTase) of the Trypanosoma brucei editosome. Mol. Cell, 11, 1525-1536.
    • (2003) Mol. Cell , vol.11 , pp. 1525-1536
    • Ernst, N.L.1    Panicucci, B.2    Igo Jr., R.P.3    Panigrahi, A.K.4    Salavati, R.5    Stuart, K.6
  • 16
    • 0141922994 scopus 로고    scopus 로고
    • Separate insertion and deletion sub-complexes of the Trypanosoma brucei RNA editing complex
    • Schnaufer, A., Ernst, N., O'Rear, J., Salavati, R. and Stuart, K. (2003) Separate insertion and deletion sub-complexes of the Trypanosoma brucei RNA editing complex. Mol. Cell, 12, 307-319.
    • (2003) Mol. Cell , vol.12 , pp. 307-319
    • Schnaufer, A.1    Ernst, N.2    O'Rear, J.3    Salavati, R.4    Stuart, K.5
  • 18
    • 0030012876 scopus 로고    scopus 로고
    • Mechanism and evolution of RNA editing in kinetoplastida
    • 1307
    • Arts, G.J. and Benne, R. (1996) Mechanism and evolution of RNA editing in kinetoplastida. Biochim. Biophys. Acta, 1307, 39-54.
    • (1996) Biochim. Biophys. Acta , pp. 39-54
    • Arts, G.J.1    Benne, R.2
  • 19
    • 0028209204 scopus 로고
    • Evolution of RNA editing in kinetoplastid protozoa
    • Maslov, D.A., Avila, H.A., Lake, J.A. and Simpson, L. (1994) Evolution of RNA editing in kinetoplastid protozoa. Nature, 368, 345-348.
    • (1994) Nature , vol.368 , pp. 345-348
    • Maslov, D.A.1    Avila, H.A.2    Lake, J.A.3    Simpson, L.4
  • 20
    • 0023647931 scopus 로고
    • Developmentally regulated addition of nucleotides within apocytochrome b transcripts in Trypanosoma brucei
    • Feagin, J.E., Jasmer, D.P. and Stuart, K. (1987) Developmentally regulated addition of nucleotides within apocytochrome b transcripts in Trypanosoma brucei. Cell, 49, 337-345.
    • (1987) Cell , vol.49 , pp. 337-345
    • Feagin, J.E.1    Jasmer, D.P.2    Stuart, K.3
  • 21
    • 0023968427 scopus 로고
    • Developmental aspects of uridine addition within mitochondrial transcripts of Trypanosoma brucei
    • Feagin, J.E. and Stuart, K. (1988) Developmental aspects of uridine addition within mitochondrial transcripts of Trypanosoma brucei. Mol. Cell. Biol., 8, 1259-1265.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 1259-1265
    • Feagin, J.E.1    Stuart, K.2
  • 22
    • 0025108122 scopus 로고
    • The MURF3 gene of T. brucei contains multiple domains of extensive editing and is homologous to a subunit of NADH dehydrogenase
    • Koslowsky, D.J., Bhat, G.J., Perrollaz, A.L., Feagin, J.E. and Stuart, K. (1990) The MURF3 gene of T. brucei contains multiple domains of extensive editing and is homologous to a subunit of NADH dehydrogenase. Cell, 62, 901-911.
    • (1990) Cell , vol.62 , pp. 901-911
    • Koslowsky, D.J.1    Bhat, G.J.2    Perrollaz, A.L.3    Feagin, J.E.4    Stuart, K.5
  • 23
    • 0028180651 scopus 로고
    • Developmental regulation of mitochondrial biogenesis in Trypanosoma brucei
    • Priest, J.W. and Hajduk, S.L. (1994) Developmental regulation of mitochondrial biogenesis in Trypanosoma brucei. J. Bioenerg. Biomembr., 26, 179-192.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 179-192
    • Priest, J.W.1    Hajduk, S.L.2
  • 24
    • 0027078820 scopus 로고
    • Mitochondrial DNA of kinetoplastids
    • Stuart, K. and Feagin, J.E. (1992) Mitochondrial DNA of kinetoplastids. Int. Rev. Cytol., 141, 65-88.
    • (1992) Int. Rev. Cytol. , vol.141 , pp. 65-88
    • Stuart, K.1    Feagin, J.E.2
  • 25
    • 0036020251 scopus 로고    scopus 로고
    • Natural and induced dyskinetoplastid trypanosomatids: How to live without mitochondrial DNA
    • Schnaufer, A., Domingo, G.J. and Stuart, K.D. (2002) Natural and induced dyskinetoplastid trypanosomatids: how to live without mitochondrial DNA. Int. J. Parasitol., 32, 1071-1084.
    • (2002) Int. J. Parasitol. , vol.32 , pp. 1071-1084
    • Schnaufer, A.1    Domingo, G.J.2    Stuart, K.D.3
  • 26
    • 0037288278 scopus 로고    scopus 로고
    • Integrated analysis of transcript profiling and protein sequence data
    • Grate, L.R., Bhattacharyya, C., Jordan, M.I. and Mian, I.S. (2003) Integrated analysis of transcript profiling and protein sequence data. Mech. Ageing Dev., 124, 109-114.
    • (2003) Mech. Ageing Dev. , vol.124 , pp. 109-114
    • Grate, L.R.1    Bhattacharyya, C.2    Jordan, M.I.3    Mian, I.S.4
  • 27
    • 0030836805 scopus 로고    scopus 로고
    • Comparative sequence analysis of ribonucleases HII, III, II, PH and D
    • Mian, I.S. (2002) Comparative sequence analysis of ribonucleases HII, III, II, PH and D. Nucleic Acids Res., 25, 3187-3195.
    • (2002) Nucleic Acids Res. , vol.25 , pp. 3187-3195
    • Mian, I.S.1
  • 28
    • 0013040064 scopus 로고    scopus 로고
    • Analysis of telomerase in Candida albicans: Potential role in telomere end protection
    • Singh, S.M., Steinberg-Neifach, O., Mian, I.S. and Lue, N.F. (2002) Analysis of telomerase in Candida albicans: potential role in telomere end protection. Eukaryot. Cell, 1, 967-977.
    • (2002) Eukaryot. Cell , vol.1 , pp. 967-977
    • Singh, S.M.1    Steinberg-Neifach, O.2    Mian, I.S.3    Lue, N.F.4
  • 29
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi, Y., Segal, M., Normington, K., Gethering, M.-J. and Sambrook, J. (1988) The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature, 332, 462-464.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gethering, M.-J.4    Sambrook, J.5
  • 31
    • 0028181441 scopus 로고
    • Hidden Markov models in computational biology. Applications to protein modeling
    • Krogh, A., Brown, M., Mian, I.S., Sjolander, K. and Haussler, D. (1994) Hidden Markov models in computational biology. Applications to protein modeling. J. Mol. Biol., 235, 1501-1531.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1501-1531
    • Krogh, A.1    Brown, M.2    Mian, I.S.3    Sjolander, K.4    Haussler, D.5
  • 32
    • 0031901903 scopus 로고    scopus 로고
    • Methods and statistics for combining motif match scores
    • Bailey, T.L. and Gribskov, M. (1998) Methods and statistics for combining motif match scores. J. Comput. Biol., 5, 211-221.
    • (1998) J. Comput. Biol. , vol.5 , pp. 211-221
    • Bailey, T.L.1    Gribskov, M.2
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
    • 0028607296 scopus 로고
    • The evolutionary expansion of the trypanosomatid flagellates
    • Vickerman, K. (1994) The evolutionary expansion of the trypanosomatid flagellates. Int. J. Parasitol., 24, 1317-1331.
    • (1994) Int. J. Parasitol. , vol.24 , pp. 1317-1331
    • Vickerman, K.1
  • 35
    • 0035662491 scopus 로고    scopus 로고
    • Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage
    • Blaszczyk, J., Tropea, J.E., Bubunenko, M., Routzahn, K.M., Waugh, D.S., Court, D.L. and Ji, X. (2001) Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage. Structure, 9, 1225-1236.
    • (2001) Structure , vol.9 , pp. 1225-1236
    • Blaszczyk, J.1    Tropea, J.E.2    Bubunenko, M.3    Routzahn, K.M.4    Waugh, D.S.5    Court, D.L.6    Ji, X.7
  • 37
    • 0037805672 scopus 로고    scopus 로고
    • TbMP44 is essential for RNA editing and structural integrity of the editosome in Trypanosoma brucei
    • Wang, B., Ernst, N., Palazzo, S.S., Panigrahi, A.K., Salavati, R. and Stuart, K. (2003) TbMP44 is essential for RNA editing and structural integrity of the editosome in Trypanosoma brucei. Eukaryot. Cell, 2, 578-587.
    • (2003) Eukaryot. Cell , vol.2 , pp. 578-587
    • Wang, B.1    Ernst, N.2    Palazzo, S.S.3    Panigrahi, A.K.4    Salavati, R.5    Stuart, K.6
  • 38
    • 0028961190 scopus 로고
    • Two functionally distinct RNA-binding motifs in the regulatory domain of the protein kinase DAI
    • Green, S.R., Manche, L. and Mathews, M.B. (1995) Two functionally distinct RNA-binding motifs in the regulatory domain of the protein kinase DAI. Mol. Cell. Biol., 15, 358-364.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 358-364
    • Green, S.R.1    Manche, L.2    Mathews, M.B.3
  • 39
    • 0037162703 scopus 로고    scopus 로고
    • Modular recognition of RNA by a human pumilio-homology domain
    • Wang, X., McLachlan, J., Zamore, P.D. and Hall, T.M. (2002) Modular recognition of RNA by a human pumilio-homology domain. Cell, 110, 501-512.
    • (2002) Cell , vol.110 , pp. 501-512
    • Wang, X.1    McLachlan, J.2    Zamore, P.D.3    Hall, T.M.4
  • 40
    • 0034615578 scopus 로고    scopus 로고
    • A novel type of RNase III family proteins in eukaryotes
    • Filippov, V., Solovyev, V., Filippova, M. and Gill, S.S. (2000) A novel type of RNase III family proteins in eukaryotes. Gene, 245, 213-221.
    • (2000) Gene , vol.245 , pp. 213-221
    • Filippov, V.1    Solovyev, V.2    Filippova, M.3    Gill, S.S.4
  • 41
    • 0025033465 scopus 로고
    • The cleavage specificity of RNase III
    • Krinke, L. and Wulff, D.L. (1990) The cleavage specificity of RNase III. Nucleic Acids Res., 18, 4809-4815.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4809-4815
    • Krinke, L.1    Wulff, D.L.2
  • 42
    • 0032932638 scopus 로고    scopus 로고
    • Function, mechanism and regulation of bacterial ribonucleases
    • Nicholson, A.W. (1999) Function, mechanism and regulation of bacterial ribonucleases. FEMS Microbiol. Rev., 23, 371-390.
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 371-390
    • Nicholson, A.W.1
  • 43
    • 0034675929 scopus 로고    scopus 로고
    • Processing of polycistronic guide RNAs associated with RNA editing complexes in Trypanosoma brucei
    • Grams, J., McManus, M.T. and Hajduk, S.L. (2000) Processing of polycistronic guide RNAs associated with RNA editing complexes in Trypanosoma brucei. EMBO J., 19, 5525-5532.
    • (2000) EMBO J. , vol.19 , pp. 5525-5532
    • Grams, J.1    McManus, M.T.2    Hajduk, S.L.3
  • 44
    • 0030933871 scopus 로고    scopus 로고
    • Resolution of the RNA editing gRNA-directed endonuclease from two other endonucleases of Trypanosoma brucei mitochondria
    • Piller, K.J., Rusché, L.N., Cruz-Reyes, J. and Sollner-Webb, B. (1997) Resolution of the RNA editing gRNA-directed endonuclease from two other endonucleases of Trypanosoma brucei mitochondria. RNA, 3, 279-290.
    • (1997) RNA , vol.3 , pp. 279-290
    • Piller, K.J.1    Rusché, L.N.2    Cruz-Reyes, J.3    Sollner-Webb, B.4
  • 45
    • 0344925960 scopus 로고    scopus 로고
    • The specificity of nucleotide removal during RNA editing in Trypanosoma brucei
    • Lawson, S., Igo, R.P., Jr, Salavati, R. and Stuart, K.D. (2000) The specificity of nucleotide removal during RNA editing in Trypanosoma brucei. RNA, 7, 1-10.
    • (2000) RNA , vol.7 , pp. 1-10
    • Lawson, S.1    Igo Jr., R.P.2    Salavati, R.3    Stuart, K.D.4
  • 47
    • 0034664049 scopus 로고    scopus 로고
    • Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP
    • Martin, G., Keller, W. and Doublie, S. (2000) Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP. EMBO J., 19, 4193-4203.
    • (2000) EMBO J. , vol.19 , pp. 4193-4203
    • Martin, G.1    Keller, W.2    Doublie, S.3
  • 48
    • 0030930760 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: Evidence for an induced fit mechanism
    • Sawaya, M.R., Prasad, R., Wilson, S.H., Kraut, J. and Pelletier, H. (1997) Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism. Biochemistry, 36, 11205-11215.
    • (1997) Biochemistry , vol.36 , pp. 11205-11215
    • Sawaya, M.R.1    Prasad, R.2    Wilson, S.H.3    Kraut, J.4    Pelletier, H.5
  • 49
    • 0029994499 scopus 로고    scopus 로고
    • Uridine insertion into preedited mRNA by a mitochondrial extract from Leishmania tarentolae: Stereochemical evidence for the enzyme cascade model
    • Frech, G.C. and Simpson, L. (1996) Uridine insertion into preedited mRNA by a mitochondrial extract from Leishmania tarentolae: stereochemical evidence for the enzyme cascade model. Mol. Cell. Biol., 16, 4584-4589.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4584-4589
    • Frech, G.C.1    Simpson, L.2
  • 50
    • 0034664049 scopus 로고    scopus 로고
    • Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP
    • Martin, G., Keller, W. and Doublie, S. (2000) Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP. EMBO J., 19, 4193-4203.
    • (2000) EMBO J. , vol.19 , pp. 4193-4203
    • Martin, G.1    Keller, W.2    Doublie, S.3
  • 51
    • 0037136552 scopus 로고    scopus 로고
    • A regulatory cytoplasmic poly(A) polymerase in Caenorhabditis elegans
    • Wang, L., Eckmann, C.R., Kadyk, L.C., Wickens, M. and Kimble, J. (2002) A regulatory cytoplasmic poly(A) polymerase in Caenorhabditis elegans. Nature, 419, 312-316.
    • (2002) Nature , vol.419 , pp. 312-316
    • Wang, L.1    Eckmann, C.R.2    Kadyk, L.C.3    Wickens, M.4    Kimble, J.5
  • 53
    • 0033578927 scopus 로고    scopus 로고
    • Recognition of polyadenylate RNA by the poly(A)-binding protein
    • Deo, R.C., Bonanno, J.B., Sonenberg, N. and Burley, S.K. (1999) Recognition of polyadenylate RNA by the poly(A)-binding protein. Cell, 98, 835-845.
    • (1999) Cell , vol.98 , pp. 835-845
    • Deo, R.C.1    Bonanno, J.B.2    Sonenberg, N.3    Burley, S.K.4
  • 54
    • 0021140818 scopus 로고
    • DNA structural variations in the E. coli tyrT promoter
    • Drew, H.R. and Travers, A.A. (1984) DNA structural variations in the E. coli tyrT promoter. Cell, 37, 491-502.
    • (1984) Cell , vol.37 , pp. 491-502
    • Drew, H.R.1    Travers, A.A.2
  • 55
    • 0028446567 scopus 로고
    • DNA recognition by DNase I
    • Suck, D. (1994) DNA recognition by DNase I. J. Mol. Recognit., 7, 65-70.
    • (1994) J. Mol. Recognit. , vol.7 , pp. 65-70
    • Suck, D.1
  • 56
    • 0025342965 scopus 로고
    • Repair of intrinsic DNA lesions
    • Lindahl, T. (1990) Repair of intrinsic DNA lesions. Mutat. Res., 238, 305-311.
    • (1990) Mutat. Res. , vol.238 , pp. 305-311
    • Lindahl, T.1
  • 57
    • 0028837564 scopus 로고
    • What's old is new: An alternative DNA excision repair pathway
    • Doetsch, P.W. (1995) What's old is new: an alternative DNA excision repair pathway. Trends Biochem. Sci., 20, 384-386.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 384-386
    • Doetsch, P.W.1
  • 58
    • 0028923440 scopus 로고
    • Structure and function of the multifunctional DNA-repair enzyme exonuclease III
    • Mol, C.D., Kuo, C.F., Thayer, M.M., Cunningham, R.P. and Tainer, J.A. (1995) Structure and function of the multifunctional DNA-repair enzyme exonuclease III. Nature, 374, 381-386.
    • (1995) Nature , vol.374 , pp. 381-386
    • Mol, C.D.1    Kuo, C.F.2    Thayer, M.M.3    Cunningham, R.P.4    Tainer, J.A.5
  • 59
    • 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. and Chen, D.S. (1991) 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, 11450-11454.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11450-11454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 60
    • 0029347105 scopus 로고
    • Structure and function of apurinic/ apyrimidinic endonucleases
    • Barzilay, G. and Hickson, I.D. (1995) Structure and function of apurinic/ apyrimidinic endonucleases. Bioessays, 17, 713-719.
    • (1995) Bioessays , vol.17 , pp. 713-719
    • Barzilay, G.1    Hickson, I.D.2
  • 62
    • 0023818825 scopus 로고
    • Structure refined to 2Å of a nicked DNA octanucleotide complex with DNase I
    • Suck, D., Lahm, A. and Oefner, C. (1988) Structure refined to 2Å of a nicked DNA octanucleotide complex with DNase I. Nature, 332, 464-468.
    • (1988) Nature , vol.332 , pp. 464-468
    • Suck, D.1    Lahm, A.2    Oefner, C.3
  • 63
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination
    • [corrected]
    • Mol, C.D., Izumi, T., Mitra, S. and Tainer, J.A. (2000) DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected]. Nature, 403, 451-456.
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 64
    • 0035815108 scopus 로고    scopus 로고
    • Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: Implications for the catalytic mechanism
    • Beernink, P.T., Segelke, B.W., Hadi, M.Z., Erzberger, J.P., Wilson, D.M., III and Rupp, B. (2001) Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism. J. Mol. Biol., 307, 1023-1034.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1023-1034
    • Beernink, P.T.1    Segelke, B.W.2    Hadi, M.Z.3    Erzberger, J.P.4    Wilson III, D.M.5    Rupp, B.6
  • 65
    • 0030728449 scopus 로고    scopus 로고
    • The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites
    • Gorman, M.A., Morera, S., Rothwell, D.G., de La Fortelle, E., Mol, C.D., Tainer, J.A., Hickson, I.D. and Freemont, P.S. (1997) The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites. EMBO J., 16, 6548-6558.
    • (1997) EMBO J. , vol.16 , pp. 6548-6558
    • Gorman, M.A.1    Morera, S.2    Rothwell, D.G.3    de La Fortelle, E.4    Mol, C.D.5    Tainer, J.A.6    Hickson, I.D.7    Freemont, P.S.8
  • 66
    • 84961981834 scopus 로고    scopus 로고
    • Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleases
    • Erzberger, J.P., Barsky, D., Scharer, O.D., Colvin, M.E. and Wilson, D.M., III (1998) Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleases. Nucleic Acids Res., 26, 2771-2778.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2771-2778
    • Erzberger, J.P.1    Barsky, D.2    Scharer, O.D.3    Colvin, M.E.4    Wilson III, D.M.5
  • 67
    • 0034213216 scopus 로고    scopus 로고
    • 2+-dependent endonucleases
    • 2+-dependent endonucleases. Trends Biochem. Sci., 25, 272-273.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 272-273
    • Dlakic, M.1
  • 68
    • 0036303482 scopus 로고    scopus 로고
    • Determinants in nuclease specificity of Ape1 and Ape2, human homologues of Escherichia coli exonuclease III
    • Hadi, M.Z., Ginalski, K., Nguyen, L.H. and Wilson, D.M., III (2002) Determinants in nuclease specificity of Ape1 and Ape2, human homologues of Escherichia coli exonuclease III. J. Mol. Biol., 316, 853-866.
    • (2002) J. Mol. Biol. , vol.316 , pp. 853-866
    • Hadi, M.Z.1    Ginalski, K.2    Nguyen, L.H.3    Wilson III, D.M.4
  • 69
    • 0344915163 scopus 로고    scopus 로고
    • Apurinic/ apyrimidinic endonuclease genes from the trypanosomatidae Leishmania major and Trypanosoma cruzi confer resistance to oxidizing agents in DNA repair-deficient Escherichia coli
    • Perez, J., Gallego, C., Bernier-Villamor, V., Camacho, A., Gonzalez-Pacanowska, D. and Ruiz-Perez, L.M. (1999) Apurinic/ apyrimidinic endonuclease genes from the trypanosomatidae Leishmania major and Trypanosoma cruzi confer resistance to oxidizing agents in DNA repair-deficient Escherichia coli. Nucleic Acids Res., 27, 771-777.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 771-777
    • Perez, J.1    Gallego, C.2    Bernier-Villamor, V.3    Camacho, A.4    Gonzalez-Pacanowska, D.5    Ruiz-Perez, L.M.6
  • 70
    • 0034610344 scopus 로고    scopus 로고
    • Novel features of the XRN-family in Arabidopsis: Evidence that AtXRN4, one of several orthologs of nuclear Xrn2p/Rat1p, functions in the cytoplasm
    • Kastenmayer, J.P. and Green, P.J. (2000) Novel features of the XRN-family in Arabidopsis: evidence that AtXRN4, one of several orthologs of nuclear Xrn2p/Rat1p, functions in the cytoplasm. Proc. Natl Acad. Sci. USA, 97, 13985-13990.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13985-13990
    • Kastenmayer, J.P.1    Green, P.J.2
  • 71
    • 0027937138 scopus 로고
    • The activity of the Saccharomyces cerevisiae strand exchange protein 1 intrinsic exonuclease during joint molecule formation
    • Johnson, A.W. and Kolodner, R.D. (1994) The activity of the Saccharomyces cerevisiae strand exchange protein 1 intrinsic exonuclease during joint molecule formation. J. Biol. Chem., 269, 3664-3672.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3664-3672
    • Johnson, A.W.1    Kolodner, R.D.2
  • 72
    • 0028886314 scopus 로고
    • Identification of functional domains in the Sep1 protein (= Kem1, Xrn1), which is required for transition through meiotic prophase in Saccharomyces cerevisiae
    • Bashkirov, V.I., Solinger, J.A. and Heyer, W.D. (1995) Identification of functional domains in the Sep1 protein (= Kem1, Xrn1), which is required for transition through meiotic prophase in Saccharomyces cerevisiae. Chromosoma, 104, 215-222.
    • (1995) Chromosoma , vol.104 , pp. 215-222
    • Bashkirov, V.I.1    Solinger, J.A.2    Heyer, W.D.3
  • 74
    • 0029938467 scopus 로고    scopus 로고
    • Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7
    • Subramanya, H.S., Doherty, A.J., Ashford, S.R. and Wigley, D.B. (1996) Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. Cell, 85, 607-615.
    • (1996) Cell , vol.85 , pp. 607-615
    • Subramanya, H.S.1    Doherty, A.J.2    Ashford, S.R.3    Wigley, D.B.4
  • 75
    • 0036790939 scopus 로고    scopus 로고
    • Bacteriophage T4 RNA ligase 2 (gp24.1) exemplifies a family of RNA ligases found in all phylogenetic domains
    • Ho, C.K. and Shuman, S. (2002) Bacteriophage T4 RNA ligase 2 (gp24.1) exemplifies a family of RNA ligases found in all phylogenetic domains. Proc. Natl Acad. Sci. USA, 99, 12709-12714.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12709-12714
    • Ho, C.K.1    Shuman, S.2
  • 76
    • 0029152217 scopus 로고
    • Mutational analysis of vaccinia DNA ligase defines residues essential for covalent catalysis
    • Shuman, S. and Ru, X.M. (1995) Mutational analysis of vaccinia DNA ligase defines residues essential for covalent catalysis. Virology, 211, 73-83.
    • (1995) Virology , vol.211 , pp. 73-83
    • Shuman, S.1    Ru, X.M.2
  • 77
    • 0038043264 scopus 로고    scopus 로고
    • Structure-function analysis of T4 RNA ligase 2
    • Yin, S., Ho, C.K. and Shuman, S. (2003) Structure-function analysis of T4 RNA ligase 2. J. Biol. Chem., 278, 17601-17608.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17601-17608
    • Yin, S.1    Ho, C.K.2    Shuman, S.3
  • 78
    • 0029938467 scopus 로고    scopus 로고
    • Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7
    • Subramanya, H.S., Doherty, A.J., Ashford, S.R. and Wigley, D.B. (1996) Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. Cell, 85, 607-615.
    • (1996) Cell , vol.85 , pp. 607-615
    • Subramanya, H.S.1    Doherty, A.J.2    Ashford, S.R.3    Wigley, D.B.4
  • 79
    • 0033634655 scopus 로고    scopus 로고
    • Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining
    • Odell, M., Sriskanda, V., Shuman, S. and Nikolov, D.B. (2000) Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining. Mol. Cell, 6, 1183-1193.
    • (2000) Mol. Cell , vol.6 , pp. 1183-1193
    • Odell, M.1    Sriskanda, V.2    Shuman, S.3    Nikolov, D.B.4
  • 80
    • 0033534370 scopus 로고    scopus 로고
    • Functional domains of an ATP-dependent DNA ligase
    • Doherty, A.J. and Wigley, D.B. (1999) Functional domains of an ATP-dependent DNA ligase. J. Mol. Biol., 285, 63-71.
    • (1999) J. Mol. Biol. , vol.285 , pp. 63-71
    • Doherty, A.J.1    Wigley, D.B.2
  • 81
    • 0032531971 scopus 로고    scopus 로고
    • Mutational analysis of Chlorella virus DNA ligase: Catalytic roles of domain I and motif VI
    • Sriskanda, V. and Shuman, S. (1998) Mutational analysis of Chlorella virus DNA ligase: catalytic roles of domain I and motif VI. Nucleic Acids Res., 26, 4618-4625.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4618-4625
    • Sriskanda, V.1    Shuman, S.2
  • 82
    • 0032145356 scopus 로고    scopus 로고
    • Specificity and fidelity of strand joining by Chlorella virus DNA ligase
    • Sriskanda, V. and Shuman, S. (1998) Specificity and fidelity of strand joining by Chlorella virus DNA ligase. Nucleic Acids Res., 26, 3536-3541.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3536-3541
    • Sriskanda, V.1    Shuman, S.2
  • 83
    • 0037417236 scopus 로고    scopus 로고
    • Kinetoplastid RNA editing ligases: Complex association, characterization, and substrate requirements
    • Palazzo, S.S., Panigrahi, A.K., Igo, R.P., Jr, Salavati, R. and Stuart, K. (2003) Kinetoplastid RNA editing ligases: complex association, characterization, and substrate requirements. Mol. Biochem. Parasitol., 127, 161-167.
    • (2003) Mol. Biochem. Parasitol. , vol.127 , pp. 161-167
    • Palazzo, S.S.1    Panigrahi, A.K.2    Igo Jr., R.P.3    Salavati, R.4    Stuart, K.5
  • 84
    • 0033570011 scopus 로고    scopus 로고
    • Mutational analysis of Escherichia coli DNA ligase identifies amino acids required for nick-ligation in vitro and for in vivo complementation of the growth of yeast cells deleted for CDC9 and LIG4
    • Sriskanda, V., Schwer, B., Ho, C.K. and Shuman, S. (1999) Mutational analysis of Escherichia coli DNA ligase identifies amino acids required for nick-ligation in vitro and for in vivo complementation of the growth of yeast cells deleted for CDC9 and LIG4. Nucleic Acids Res., 27, 3953-3963.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3953-3963
    • Sriskanda, V.1    Schwer, B.2    Ho, C.K.3    Shuman, S.4
  • 85
    • 0034635347 scopus 로고    scopus 로고
    • Nick recognition by DNA ligases
    • Doherty, A.J. and Dafforn, T.R. (2000) Nick recognition by DNA ligases. J. Mol. Biol., 296, 43-56.
    • (2000) J. Mol. Biol. , vol.296 , pp. 43-56
    • Doherty, A.J.1    Dafforn, T.R.2
  • 86
    • 0032574817 scopus 로고    scopus 로고
    • Agrobacterium transcriptional regulator Ros is a prokaryotic zinc finger protein that regulates the plant oncogene ipt
    • Chou, A.Y., Archdeacon, J. and Kado, C.I. (1998) Agrobacterium transcriptional regulator Ros is a prokaryotic zinc finger protein that regulates the plant oncogene ipt. Proc. Natl Acad. Sci. USA, 95, 5293-5298.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5293-5298
    • Chou, A.Y.1    Archdeacon, J.2    Kado, C.I.3
  • 87
    • 0033853082 scopus 로고    scopus 로고
    • Zinc fingers: DNA binding and protein-protein interactions
    • Leon, O. and Roth, M. (2000) Zinc fingers: DNA binding and protein-protein interactions. Biol. Res., 33, 21-30.
    • (2000) Biol. Res. , vol.33 , pp. 21-30
    • Leon, O.1    Roth, M.2
  • 88
    • 0035253047 scopus 로고    scopus 로고
    • Zinc finger proteins: New insights into structural and functional diversity
    • Laity, J.H., Lee, B.M. and Wright, P.E. (2001) Zinc finger proteins: new insights into structural and functional diversity. Curr. Opin. Struct. Biol., 11, 39-46.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 39-46
    • Laity, J.H.1    Lee, B.M.2    Wright, P.E.3
  • 89
    • 0032464349 scopus 로고    scopus 로고
    • Analysis of zinc binding sites in protein crystal structures
    • Alberts, I.L., Nadassy, K. and Wodak, S.J. (1998) Analysis of zinc binding sites in protein crystal structures. Protein Sci., 7, 1700-1716.
    • (1998) Protein Sci. , vol.7 , pp. 1700-1716
    • Alberts, I.L.1    Nadassy, K.2    Wodak, S.J.3
  • 91
    • 0028246888 scopus 로고
    • Escherichia coli single-stranded DNA-binding protein: Multiple DNA-binding modes and cooperativities
    • Lohman, T.M. and Ferrari, M.E. (1994) Escherichia coli single-stranded DNA-binding protein: multiple DNA-binding modes and cooperativities. Annu. Rev. Biochem., 63, 527-570.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 527-570
    • Lohman, T.M.1    Ferrari, M.E.2
  • 92
    • 0021920551 scopus 로고
    • Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration
    • Lohman, T.M. and Overman, L.B. (1985) Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration. J. Biol. Chem., 260, 3594-3603.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3594-3603
    • Lohman, T.M.1    Overman, L.B.2
  • 93
    • 34147224324 scopus 로고
    • The single-stranded DNA-binding protein of Escherichia coli
    • Meyer, R.R. and Laine, P.S. (1990) The single-stranded DNA-binding protein of Escherichia coli. Microbiol. Rev., 54, 342-380.
    • (1990) Microbiol. Rev. , vol.54 , pp. 342-380
    • Meyer, R.R.1    Laine, P.S.2
  • 94
    • 0026701665 scopus 로고
    • Characterization of DNA-binding and strand-exchange stimulation properties of y-RPA, a yeast single-strand-DNA-binding protein
    • Alani, E., Thresher, R., Griffith, J.D. and Kolodner, R.D. (1992) Characterization of DNA-binding and strand-exchange stimulation properties of y-RPA, a yeast single-strand-DNA-binding protein. J. Mol. Biol., 227, 54-71.
    • (1992) J. Mol. Biol. , vol.227 , pp. 54-71
    • Alani, E.1    Thresher, R.2    Griffith, J.D.3    Kolodner, R.D.4
  • 96
    • 0035253862 scopus 로고    scopus 로고
    • Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding
    • Bochkareva, E., Belegu, V., Korolev, S. and Bochkarev, A. (2001) Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding. EMBO J., 20, 612-618.
    • (2001) EMBO J. , vol.20 , pp. 612-618
    • Bochkareva, E.1    Belegu, V.2    Korolev, S.3    Bochkarev, A.4
  • 97
    • 0028199707 scopus 로고
    • Single-stranded-DNA-binding proteins from human mitochondria and Escherichia coli have analogous physicochemical properties
    • Curth, U., Urbanke, C., Greipel, J., Gerberding, H., Tiranti, V. and Zeviani, M. (1994) Single-stranded-DNA-binding proteins from human mitochondria and Escherichia coli have analogous physicochemical properties. Eur. J. Biochem., 221, 435-443.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 435-443
    • Curth, U.1    Urbanke, C.2    Greipel, J.3    Gerberding, H.4    Tiranti, V.5    Zeviani, M.6
  • 98
    • 0031753251 scopus 로고    scopus 로고
    • Identification and characterization of the fourth single-stranded-DNA binding domain of replication protein A
    • Brill, S.J. and Bastin-Shanower, S. (1998) Identification and characterization of the fourth single-stranded-DNA binding domain of replication protein A. Mol. Cell. Biol., 18, 7225-7234.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7225-7234
    • Brill, S.J.1    Bastin-Shanower, S.2
  • 99
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin, A.G. (1993) OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J., 12, 861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 100
    • 0030888822 scopus 로고    scopus 로고
    • A mutation in E. coli SSB protein (W54S) alters intra-tetramer negative cooperativity and inter-tetramer positive cooperativity for single-stranded DNA binding
    • Ferrari, M.E., Fang, J. and Lohman, T.M. (1997) A mutation in E. coli SSB protein (W54S) alters intra-tetramer negative cooperativity and inter-tetramer positive cooperativity for single-stranded DNA binding. Biophys. Chem., 64, 235-251.
    • (1997) Biophys. Chem. , vol.64 , pp. 235-251
    • Ferrari, M.E.1    Fang, J.2    Lohman, T.M.3
  • 101
    • 0018186386 scopus 로고
    • Fluorescence and chemical studies on the interaction of Escherichia coli DNA-binding protein with single-stranded DNA
    • Bandyopadhyay, P.K. and Wu, C.W. (1978) Fluorescence and chemical studies on the interaction of Escherichia coli DNA-binding protein with single-stranded DNA. Biochemistry., 17, 4078-4085.
    • (1978) Biochemistry. , vol.17 , pp. 4078-4085
    • Bandyopadhyay, P.K.1    Wu, C.W.2
  • 102
    • 0035859960 scopus 로고    scopus 로고
    • Structure of the gene 2.5 protein, a single-stranded DNA binding protein encoded by bacteriophage T7
    • Hollis, T., Stattel, J.M., Walther, D.S., Richardson, C.C. and Ellenberger, T. (2001) Structure of the gene 2.5 protein, a single-stranded DNA binding protein encoded by bacteriophage T7. Proc. Natl Acad. Sci. USA, 98, 9557-9562.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9557-9562
    • Hollis, T.1    Stattel, J.M.2    Walther, D.S.3    Richardson, C.C.4    Ellenberger, T.5
  • 103
    • 0037470236 scopus 로고    scopus 로고
    • The DNA binding domain of the gene 2.5 single-stranded DNA-binding protein of bacteriophage T7
    • Hyland, E.M., Rezende, L.F. and Richardson, C.C. (2003) The DNA binding domain of the gene 2.5 single-stranded DNA-binding protein of bacteriophage T7. J. Biol. Chem., 278, 7247-7256.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7247-7256
    • Hyland, E.M.1    Rezende, L.F.2    Richardson, C.C.3
  • 104
    • 0032463507 scopus 로고    scopus 로고
    • The role of the 6 lysines and the terminal amine of Escherichia coli single-strand binding protein in its binding of single-stranded DNA
    • Chen, J., Smith, D.L. and Griep, M.A. (1998) The role of the 6 lysines and the terminal amine of Escherichia coli single-strand binding protein in its binding of single-stranded DNA. Protein Sci., 7, 1781-1788.
    • (1998) Protein Sci. , vol.7 , pp. 1781-1788
    • Chen, J.1    Smith, D.L.2    Griep, M.A.3
  • 105
    • 0028029835 scopus 로고
    • Trypanosoma brucei mitochondria contain RNA helicase activity
    • Missel, A. and Göringer, H.U. (1994) Trypanosoma brucei mitochondria contain RNA helicase activity. Nucleic Acids Res., 22, 4050-4056.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4050-4056
    • Missel, A.1    Göringer, H.U.2
  • 106
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A
    • Pause, A. and Sonenberg, N. (1992) Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J., 11, 2643-2654.
    • (1992) EMBO J. , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 107
    • 0033133863 scopus 로고    scopus 로고
    • Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families
    • de la Cruz, J., Kressler, D. and Linder, P. (1999) Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families. Trends Biochem. Sci., 24, 192-198.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 192-198
    • de la Cruz, J.1    Kressler, D.2    Linder, P.3
  • 108
    • 0027428138 scopus 로고
    • Four yeast spliceosomal proteins (PRP5, PRP9, PRP11, and PRP21) interact to promote U2 snRNP binding to pre-mRNA
    • Ruby, S.W., Chang, T.H. and Abelson, J. (1993) Four yeast spliceosomal proteins (PRP5, PRP9, PRP11, and PRP21) interact to promote U2 snRNP binding to pre-mRNA. Genes Dev., 7, 1909-1925.
    • (1993) Genes Dev. , vol.7 , pp. 1909-1925
    • Ruby, S.W.1    Chang, T.H.2    Abelson, J.3
  • 109
    • 0035177309 scopus 로고    scopus 로고
    • Deletion of MUD2, the yeast homolog of U2AF65, can bypass the requirement for sub2, an essential spliceosomal ATPase
    • Kistler, A.L. and Guthrie, C. (2001) Deletion of MUD2, the yeast homolog of U2AF65, can bypass the requirement for sub2, an essential spliceosomal ATPase. Genes Dev., 15, 42-49.
    • (2001) Genes Dev. , vol.15 , pp. 42-49
    • Kistler, A.L.1    Guthrie, C.2
  • 110
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP- and GTP-binding proteins
    • Saraste, M., Sibbald, P.R. and Wittinghofer, A. (1990) The P-loop - a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci., 15, 430-434.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 111
    • 0019949753 scopus 로고
    • Solid-phase sequence analysis of polypeptides eluted from polyacrylamide gels. An aid to interpretation of DNA sequences exemplified by the Escherichia coli unc operon and bacteriophage lambda
    • Walker, J.E., Auffret, A.D., Carne, A., Gurnett, A., Hanisch, P., Hill, D. and Saraste, M. (1982) Solid-phase sequence analysis of polypeptides eluted from polyacrylamide gels. An aid to interpretation of DNA sequences exemplified by the Escherichia coli unc operon and bacteriophage lambda. Eur. J. Biochem., 123, 253-260.
    • (1982) Eur. J. Biochem. , vol.123 , pp. 253-260
    • Walker, J.E.1    Auffret, A.D.2    Carne, A.3    Gurnett, A.4    Hanisch, P.5    Hill, D.6    Saraste, M.7
  • 112
    • 0346497938 scopus 로고
    • ATP-binding site of adenylate kinase: Mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins
    • Fry, D.C., Kuby, S.A. and Mildvan, A.S. (1986) ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins. Proc. Natl Acad. Sci. USA, 83, 907-911.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 907-911
    • Fry, D.C.1    Kuby, S.A.2    Mildvan, A.S.3
  • 114
    • 0029914905 scopus 로고    scopus 로고
    • Active site comparisons highlight structural similarities between myosin and other P-loop proteins
    • Smith, C.A. and Rayment, I. (1996) Active site comparisons highlight structural similarities between myosin and other P-loop proteins. Biophys. J., 70, 1590-1602.
    • (1996) Biophys. J. , vol.70 , pp. 1590-1602
    • Smith, C.A.1    Rayment, I.2
  • 115
    • 0032824138 scopus 로고    scopus 로고
    • Structure-based mutagenesis study of hepatitis C virus NS3 helicase
    • Lin, C. and Kim, J.L. (1999) Structure-based mutagenesis study of hepatitis C virus NS3 helicase. J. Virol., 73, 8798-8807.
    • (1999) J. Virol. , vol.73 , pp. 8798-8807
    • Lin, C.1    Kim, J.L.2
  • 116
    • 0034700086 scopus 로고    scopus 로고
    • Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
    • Caruthers, J.M., Johnson, E.R. and McKay, D.B. (2000) Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. Proc. Natl Acad. Sci. USA, 97, 13080-13085.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13080-13085
    • Caruthers, J.M.1    Johnson, E.R.2    McKay, D.B.3
  • 117
    • 0034857262 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: From generic motors to specific dissociation functions
    • Tanner, N.K. and Linder, P. (2001) DExD/H box RNA helicases: from generic motors to specific dissociation functions. Mol. Cell, 8, 251-262.
    • (2001) Mol. Cell , vol.8 , pp. 251-262
    • Tanner, N.K.1    Linder, P.2
  • 118
    • 0031574096 scopus 로고    scopus 로고
    • Genetic interactions of conserved regions in the DEAD-box protein Prp28p
    • Chang, T.H., Latus, L.J., Liu, Z. and Abbott, J.M. (1997) Genetic interactions of conserved regions in the DEAD-box protein Prp28p. Nucleic Acids Res., 25, 5033-5040.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 5033-5040
    • Chang, T.H.1    Latus, L.J.2    Liu, Z.3    Abbott, J.M.4
  • 119
    • 0027494565 scopus 로고
    • The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis
    • Pause, A., Methot, N. and Sonenberg, N. (1993) The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis. Mol. Cell. Biol., 13, 6789-6798.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6789-6798
    • Pause, A.1    Methot, N.2    Sonenberg, N.3
  • 120
    • 0030050636 scopus 로고    scopus 로고
    • The QRxGRxGRxxxG motif of the vaccinia virus DExH box RNA helicase NPH-II is required for ATP hydrolysis and RNA unwinding but not for RNA binding
    • Gross, C.H. and Shuman, S. (1996) The QRxGRxGRxxxG motif of the vaccinia virus DExH box RNA helicase NPH-II is required for ATP hydrolysis and RNA unwinding but not for RNA binding. J. Virol., 70, 1706-1713.
    • (1996) J. Virol. , vol.70 , pp. 1706-1713
    • Gross, C.H.1    Shuman, S.2
  • 121
    • 0025898593 scopus 로고
    • Translation initiation factor 4A from Saccharomyces cerevisiae: Analysis of residues conserved in the D-E-A-D family of RNA helicases
    • Schmid, S.R. and Linder, P. (1991) Translation initiation factor 4A from Saccharomyces cerevisiae: analysis of residues conserved in the D-E-A-D family of RNA helicases. Mol. Cell. Biol., 11, 3463-3471.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3463-3471
    • Schmid, S.R.1    Linder, P.2
  • 122
    • 0026702582 scopus 로고
    • Active site of (A)BC excinuclease. II. Binding, bending, and catalysis mutants of UvrB reveal a direct role in 3′ and an indirect role in 5′ incision
    • Lin, J.J., Phillips, A.M., Hearst, J.E. and Sancar, A. (1992) Active site of (A)BC excinuclease. II. Binding, bending, and catalysis mutants of UvrB reveal a direct role in 3′ and an indirect role in 5′ incision. J. Biol. Chem., 267, 17693-17700.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17693-17700
    • Lin, J.J.1    Phillips, A.M.2    Hearst, J.E.3    Sancar, A.4
  • 123
    • 0033428970 scopus 로고    scopus 로고
    • Helicase motifs: The engine that powers DNA unwinding
    • Hall, M.C. and Matson, S.W. (1999) Helicase motifs: the engine that powers DNA unwinding. Mol. Microbiol., 34, 867-877.
    • (1999) Mol. Microbiol. , vol.34 , pp. 867-877
    • Hall, M.C.1    Matson, S.W.2
  • 124
    • 0027981641 scopus 로고
    • Interactions between highly conserved U2 small nuclear RNA structures and Prp5p, Prp9p, Prp11p, and Prp21p proteins are required to ensure integrity of the U2 small nuclear ribonucleoprotein in Saccharomyces cerevisiae
    • Wells, S.E. and Ares, M., Jr (1994) Interactions between highly conserved U2 small nuclear RNA structures and Prp5p, Prp9p, Prp11p, and Prp21p proteins are required to ensure integrity of the U2 small nuclear ribonucleoprotein in Saccharomyces cerevisiae. Mol. Cell. Biol., 14, 6337-6349.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6337-6349
    • Wells, S.E.1    Ares Jr., M.2
  • 125
    • 0028925960 scopus 로고
    • Structure and function of the UvrB protein
    • Hsu, D.S., Kim, S.T., Sun, Q. and Sancar, A. (1995) Structure and function of the UvrB protein. J. Biol. Chem., 270, 8319-8327.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8319-8327
    • Hsu, D.S.1    Kim, S.T.2    Sun, Q.3    Sancar, A.4
  • 126
    • 0029892790 scopus 로고    scopus 로고
    • DNA excision repair
    • Sancar, A. (1996) DNA excision repair. Annu. Rev. Biochem., 65, 43-81.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 43-81
    • Sancar, A.1
  • 127
    • 0027227415 scopus 로고
    • Nucleotide excision repair, a tracking mechanism in search of damage
    • Grossman, L. and Thiagalingam, S. (1993) Nucleotide excision repair, a tracking mechanism in search of damage. J. Biol. Chem., 268, 16871-16874.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16871-16874
    • Grossman, L.1    Thiagalingam, S.2
  • 128
    • 0037119975 scopus 로고    scopus 로고
    • Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein
    • Will, C.L., Urlaub, H., Achsel, T., Gentzel, M., Wilm, M. and Luhrmann, R. (2002) Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein. EMBO J., 21, 4978-4988.
    • (2002) EMBO J. , vol.21 , pp. 4978-4988
    • Will, C.L.1    Urlaub, H.2    Achsel, T.3    Gentzel, M.4    Wilm, M.5    Luhrmann, R.6
  • 129
    • 0029789824 scopus 로고    scopus 로고
    • A minimal gene set for cellular life derived by comparison of complete bacterial genomes
    • Mushegian, A.R. and Koonin, E.V. (1996) A minimal gene set for cellular life derived by comparison of complete bacterial genomes. Proc. Natl Acad. Sci. USA., 93, 10268-10273.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10268-10273
    • Mushegian, A.R.1    Koonin, E.V.2
  • 130
    • 0033105094 scopus 로고    scopus 로고
    • Conserved domains in DNA repair proteins and evolution of repair systems
    • Aravind, L., Walker, D.R. and Koonin, E.V. (1999) Conserved domains in DNA repair proteins and evolution of repair systems. Nucleic Acids Res., 27, 1223-1242.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1223-1242
    • Aravind, L.1    Walker, D.R.2    Koonin, E.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.