-
1
-
-
0030754921
-
Distribution of both lengths and 5′ terminal nucleotides of mammalian pre-tRNA 3′ trailers reflects properties of 3′ processing endoribonuclease
-
Nashimoto M. Distribution of both lengths and 5′ terminal nucleotides of mammalian pre-tRNA 3′ trailers reflects properties of 3′ processing endoribonuclease. Nucleic Acids Res. 25 (1997) 1148-1155
-
(1997)
Nucleic Acids Res.
, vol.25
, pp. 1148-1155
-
-
Nashimoto, M.1
-
2
-
-
0038750928
-
A candidate prostate cancer susceptibility gene encodes tRNA 3′ processing endoribonuclease
-
Takaku H., Minagawa A., Takagi M., and Nashimoto M. A candidate prostate cancer susceptibility gene encodes tRNA 3′ processing endoribonuclease. Nucleic Acids Res. 31 (2003) 2272-2278
-
(2003)
Nucleic Acids Res.
, vol.31
, pp. 2272-2278
-
-
Takaku, H.1
Minagawa, A.2
Takagi, M.3
Nashimoto, M.4
-
3
-
-
2442616184
-
A novel endonucleolytic mechanism to generate the CCA 3′ termini of tRNA molecules in Thermotoga maritima
-
Minagawa A., Takaku H., Takagi M., and Nashimoto M. A novel endonucleolytic mechanism to generate the CCA 3′ termini of tRNA molecules in Thermotoga maritima. J. Biol. Chem. 279 (2004) 15688-15697
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 15688-15697
-
-
Minagawa, A.1
Takaku, H.2
Takagi, M.3
Nashimoto, M.4
-
4
-
-
20444395097
-
Residues in the conserved His domain of fruit fly tRNase Z that function in catalysis are not involved in substrate recognition or binding
-
Zareen N., Yan H., Hopkinson A., and Levinger L. Residues in the conserved His domain of fruit fly tRNase Z that function in catalysis are not involved in substrate recognition or binding. J. Mol. Biol. 350 (2005) 189-199
-
(2005)
J. Mol. Biol.
, vol.350
, pp. 189-199
-
-
Zareen, N.1
Yan, H.2
Hopkinson, A.3
Levinger, L.4
-
5
-
-
27444439481
-
Analysis of the functional modules of the tRNA 3′ endonuclease (tRNase Z)
-
Späth B., Kirchner S., Vogel A., Schubert S., Meinlschmidt P., Aymanns S., et al. Analysis of the functional modules of the tRNA 3′ endonuclease (tRNase Z). J. Biol. Chem. 280 (2005) 35440-35447
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 35440-35447
-
-
Späth, B.1
Kirchner, S.2
Vogel, A.3
Schubert, S.4
Meinlschmidt, P.5
Aymanns, S.6
-
6
-
-
33646402107
-
Substrate recognition ability differs among various prokaryotic tRNase Zs
-
Minagawa A., Takaku H., Shibata H.S., Ishii R., Takagi M., Yokoyama S., and Nashimoto M. Substrate recognition ability differs among various prokaryotic tRNase Zs. Biochem. Biophys. Res. Commun. 345 (2006) 385-393
-
(2006)
Biochem. Biophys. Res. Commun.
, vol.345
, pp. 385-393
-
-
Minagawa, A.1
Takaku, H.2
Shibata, H.S.3
Ishii, R.4
Takagi, M.5
Yokoyama, S.6
Nashimoto, M.7
-
7
-
-
4243087008
-
The N-terminal half-domain of the long form of tRNase Z is required for the RNase 65 activity
-
Takaku H., Minagawa A., Takagi M., and Nashimoto M. The N-terminal half-domain of the long form of tRNase Z is required for the RNase 65 activity. Nucleic Acids Res. 32 (2004) 4429-4438
-
(2004)
Nucleic Acids Res.
, vol.32
, pp. 4429-4438
-
-
Takaku, H.1
Minagawa, A.2
Takagi, M.3
Nashimoto, M.4
-
8
-
-
17144378531
-
Crystal structure of the tRNA 3′ processing endoribonuclease tRNase Z from Thermotoga maritima
-
Ishii R., Minagawa A., Takaku H., Takagi M., Nashimoto M., and Yokoyama S. Crystal structure of the tRNA 3′ processing endoribonuclease tRNase Z from Thermotoga maritima. J. Biol. Chem. 280 (2005) 14138-14144
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 14138-14144
-
-
Ishii, R.1
Minagawa, A.2
Takaku, H.3
Takagi, M.4
Nashimoto, M.5
Yokoyama, S.6
-
9
-
-
14144251951
-
Structural basis for substrate binding, cleavage and allostery in the tRNA maturase RNase Z
-
de la Sierra-Gallay I.L., Pellegrini O., and Condon C. Structural basis for substrate binding, cleavage and allostery in the tRNA maturase RNase Z. Nature 433 (2005) 657-661
-
(2005)
Nature
, vol.433
, pp. 657-661
-
-
de la Sierra-Gallay, I.L.1
Pellegrini, O.2
Condon, C.3
-
10
-
-
32444437167
-
The crystal structure of the zinc phosphodiesterase from Escherichia coli provides insight into function and cooperativity of tRNase Z-family proteins
-
Kostelecky B., Pohl E., Vogel A., Schilling O., and Meyer-Klaucke W. The crystal structure of the zinc phosphodiesterase from Escherichia coli provides insight into function and cooperativity of tRNase Z-family proteins. J. Bacteriol. 188 (2006) 1607-1614
-
(2006)
J. Bacteriol.
, vol.188
, pp. 1607-1614
-
-
Kostelecky, B.1
Pohl, E.2
Vogel, A.3
Schilling, O.4
Meyer-Klaucke, W.5
-
12
-
-
0033537798
-
Selection of cleavage site by mammalian tRNA 3′ processing endoribonuclease
-
Nashimoto M., Tamura M., and Kaspar R.L. Selection of cleavage site by mammalian tRNA 3′ processing endoribonuclease. J. Mol. Biol. 287 (1999) 727-740
-
(1999)
J. Mol. Biol.
, vol.287
, pp. 727-740
-
-
Nashimoto, M.1
Tamura, M.2
Kaspar, R.L.3
-
13
-
-
0033554375
-
Minimum requirements for substrates of mammalian tRNA 3′ processing endoribonuclease
-
Nashimoto M., Tamura M., and Kaspar R.L. Minimum requirements for substrates of mammalian tRNA 3′ processing endoribonuclease. Biochemistry 38 (1999) 12089-12096
-
(1999)
Biochemistry
, vol.38
, pp. 12089-12096
-
-
Nashimoto, M.1
Tamura, M.2
Kaspar, R.L.3
-
14
-
-
20444425394
-
Exosite modules guide substrate recognition in the ZiPD/ElaC protein family
-
Schilling O., Späth B., Kostelecky B., Marchfelder A., Meyer-Klaucke W., and Vogel A. Exosite modules guide substrate recognition in the ZiPD/ElaC protein family. J. Biol. Chem. 280 (2005) 17857-17862
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 17857-17862
-
-
Schilling, O.1
Späth, B.2
Kostelecky, B.3
Marchfelder, A.4
Meyer-Klaucke, W.5
Vogel, A.6
-
16
-
-
34547634674
-
The structure of the flexible arm of Thermotoga maritima tRNase Z differs from those of homologous enzymes
-
Ishii R., Minagawa A., Takaku H., Takagi M., Nashimoto M., and Yokoyama S. The structure of the flexible arm of Thermotoga maritima tRNase Z differs from those of homologous enzymes. Acta Crystallogr. F 63 (2007) 637-641
-
(2007)
Acta Crystallogr. F
, vol.63
, pp. 637-641
-
-
Ishii, R.1
Minagawa, A.2
Takaku, H.3
Takagi, M.4
Nashimoto, M.5
Yokoyama, S.6
-
17
-
-
0043239333
-
Endonucleolytic processing of CCA-less tRNA precursors by RNase Z in Bacillus subtilis
-
Pellegrini O., Nezzar J., Marchfelder A., Putzer H., and Condon C. Endonucleolytic processing of CCA-less tRNA precursors by RNase Z in Bacillus subtilis. EMBO J. 22 (2003) 4534-4543
-
(2003)
EMBO J.
, vol.22
, pp. 4534-4543
-
-
Pellegrini, O.1
Nezzar, J.2
Marchfelder, A.3
Putzer, H.4
Condon, C.5
-
18
-
-
33646341197
-
Unstructured RNA is a substrate for tRNase Z
-
Shibata H.S., Minagawa A., Takaku H., Takagi M., and Nashimoto M. Unstructured RNA is a substrate for tRNase Z. Biochemistry 45 (2006) 5486-5492
-
(2006)
Biochemistry
, vol.45
, pp. 5486-5492
-
-
Shibata, H.S.1
Minagawa, A.2
Takaku, H.3
Takagi, M.4
Nashimoto, M.5
-
19
-
-
0027340664
-
Arg is essential for in vitro specific cleavage of partially synthesized mouse 18S rRNA
-
Arg is essential for in vitro specific cleavage of partially synthesized mouse 18S rRNA. Nucleic Acids Res. 21 (1993) 4696-4702
-
(1993)
Nucleic Acids Res.
, vol.21
, pp. 4696-4702
-
-
Nashimoto, M.1
-
20
-
-
0029113672
-
Conversion of mammalian tRNA 3′ processing endoribonuclease to four-base-recognizing RNA cutters
-
Nashimoto M. Conversion of mammalian tRNA 3′ processing endoribonuclease to four-base-recognizing RNA cutters. Nucleic Acids Res. 23 (1995) 3642-3647
-
(1995)
Nucleic Acids Res.
, vol.23
, pp. 3642-3647
-
-
Nashimoto, M.1
-
21
-
-
0035812598
-
The inhibitory effect of the autoantigen La on in vitro 3′ processing of mammalian precursor tRNAs
-
Nashimoto M., Nashimoto C., Tamura M., Kaspar R.L., and Ochi K. The inhibitory effect of the autoantigen La on in vitro 3′ processing of mammalian precursor tRNAs. J. Mol. Biol. 312 (2001) 975-984
-
(2001)
J. Mol. Biol.
, vol.312
, pp. 975-984
-
-
Nashimoto, M.1
Nashimoto, C.2
Tamura, M.3
Kaspar, R.L.4
Ochi, K.5
-
22
-
-
0024520745
-
Site-directed mutagenesis by overlap extension using the polymerase chain reaction
-
Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., and Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77 (1989) 51-59
-
(1989)
Gene
, vol.77
, pp. 51-59
-
-
Ho, S.N.1
Hunt, H.D.2
Horton, R.M.3
Pullen, J.K.4
Pease, L.R.5
-
23
-
-
20444450546
-
The T loop structure is dispensable for substrate recognition by tRNase ZL
-
Shibata H.S., Takaku H., Takagi M., and Nashimoto M. The T loop structure is dispensable for substrate recognition by tRNase ZL. J. Biol. Chem. 280 (2005) 22326-22334
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 22326-22334
-
-
Shibata, H.S.1
Takaku, H.2
Takagi, M.3
Nashimoto, M.4
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