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Volumn 21, Issue 7, 2013, Pages 1074-1084

Single-stranded DNA-binding proteins: Multiple domains for multiple functions

Author keywords

[No Author keywords available]

Indexed keywords

HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D; SINGLE STRANDED DNA; SINGLE STRANDED DNA BINDING PROTEIN;

EID: 84879816054     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.05.013     Document Type: Review
Times cited : (96)

References (128)
  • 1
    • 0029897964 scopus 로고    scopus 로고
    • Origins of binding specificity of the A1 heterogeneous nuclear ribonucleoprotein
    • N. Abdul-Manan, S.M. O'Malley, and K.R. Williams Origins of binding specificity of the A1 heterogeneous nuclear ribonucleoprotein Biochemistry 35 1996 3545 3554
    • (1996) Biochemistry , vol.35 , pp. 3545-3554
    • Abdul-Manan, N.1    O'Malley, S.M.2    Williams, K.R.3
  • 2
    • 80052248612 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe protection of telomeres 1 utilizes alternate binding modes to accommodate different telomeric sequences
    • S.E. Altschuler, T.H. Dickey, and D.S. Wuttke Schizosaccharomyces pombe protection of telomeres 1 utilizes alternate binding modes to accommodate different telomeric sequences Biochemistry 50 2011 7503 7513
    • (2011) Biochemistry , vol.50 , pp. 7503-7513
    • Altschuler, S.E.1    Dickey, T.H.2    Wuttke, D.S.3
  • 3
    • 0036798283 scopus 로고    scopus 로고
    • Delineation of the high-affinity single-stranded telomeric DNA-binding domain of Saccharomyces cerevisiae Cdc13
    • E.M. Anderson, W.A. Halsey, and D.S. Wuttke Delineation of the high-affinity single-stranded telomeric DNA-binding domain of Saccharomyces cerevisiae Cdc13 Nucleic Acids Res. 30 2002 4305 4313
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4305-4313
    • Anderson, E.M.1    Halsey, W.A.2    Wuttke, D.S.3
  • 4
    • 84862208973 scopus 로고    scopus 로고
    • Plasmodium falciparum SSB tetramer wraps single-stranded DNA with similar topology but opposite polarity to E. coli SSB
    • E. Antony, E.A. Weiland, S. Korolev, and T.M. Lohman Plasmodium falciparum SSB tetramer wraps single-stranded DNA with similar topology but opposite polarity to E. coli SSB J. Mol. Biol. 420 2012 269 283
    • (2012) J. Mol. Biol. , vol.420 , pp. 269-283
    • Antony, E.1    Weiland, E.A.2    Korolev, S.3    Lohman, T.M.4
  • 5
    • 0034663204 scopus 로고    scopus 로고
    • A nuclear matrix-associated factor, SAF-B, interacts with specific isoforms of AUF1/hnRNP D
    • Y. Arao, R. Kuriyama, F. Kayama, and S. Kato A nuclear matrix-associated factor, SAF-B, interacts with specific isoforms of AUF1/hnRNP D Arch. Biochem. Biophys. 380 2000 228 236
    • (2000) Arch. Biochem. Biophys. , vol.380 , pp. 228-236
    • Arao, Y.1    Kuriyama, R.2    Kayama, F.3    Kato, S.4
  • 6
    • 21744454842 scopus 로고    scopus 로고
    • X-ray crystallographic and NMR studies of the third KH domain of hnRNP K in complex with single-stranded nucleic acids
    • P.H. Backe, A.C. Messias, R.B.G. Ravelli, M. Sattler, and S. Cusack X-ray crystallographic and NMR studies of the third KH domain of hnRNP K in complex with single-stranded nucleic acids Structure 13 2005 1055 1067
    • (2005) Structure , vol.13 , pp. 1055-1067
    • Backe, P.H.1    Messias, A.C.2    Ravelli, R.B.G.3    Sattler, M.4    Cusack, S.5
  • 8
    • 38649116679 scopus 로고    scopus 로고
    • Mechanism of IS200/IS605 family DNA transposases: Activation and transposon-directed target site selection
    • O. Barabas, D.R. Ronning, C. Guynet, A.B. Hickman, B. Ton-Hoang, M. Chandler, and F. Dyda Mechanism of IS200/IS605 family DNA transposases: activation and transposon-directed target site selection Cell 132 2008 208 220
    • (2008) Cell , vol.132 , pp. 208-220
    • Barabas, O.1    Ronning, D.R.2    Guynet, C.3    Hickman, A.B.4    Ton-Hoang, B.5    Chandler, M.6    Dyda, F.7
  • 9
    • 84873059804 scopus 로고    scopus 로고
    • Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: How the relative orientation between RRMs influences the nucleic acid binding topology
    • P. Barraud, and F.H.-T. Allain Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology J. Biomol. NMR 55 2013 119 138
    • (2013) J. Biomol. NMR , vol.55 , pp. 119-138
    • Barraud, P.1    Allain, F.H.-T.2
  • 11
    • 0035844082 scopus 로고    scopus 로고
    • Pot1, the putative telomere end-binding protein in fission yeast and humans
    • P. Baumann, and T.R. Cech Pot1, the putative telomere end-binding protein in fission yeast and humans Science 292 2001 1171 1175
    • (2001) Science , vol.292 , pp. 1171-1175
    • Baumann, P.1    Cech, T.R.2
  • 12
    • 84884819817 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A1 in health and neurodegenerative disease: From structural insights to post-transcriptional regulatory roles
    • 10.1016/j.mcn.2012.12.002 Published online December 14, 2012
    • U. Bekenstein, and H. Soreq Heterogeneous nuclear ribonucleoprotein A1 in health and neurodegenerative disease: from structural insights to post-transcriptional regulatory roles Mol. Cell. Neurosci. 2012 10.1016/j.mcn.2012.12.002 Published online December 14, 2012
    • (2012) Mol. Cell. Neurosci.
    • Bekenstein, U.1    Soreq, H.2
  • 14
    • 0036786446 scopus 로고    scopus 로고
    • Characterization of binding-induced changes in dynamics suggests a model for sequence-nonspecific binding of ssDNA by replication protein A
    • S. Bhattacharya, M.-V. Botuyan, F. Hsu, X. Shan, A.I. Arunkumar, C.H. Arrowsmith, A.M. Edwards, and W.J. Chazin Characterization of binding-induced changes in dynamics suggests a model for sequence-nonspecific binding of ssDNA by replication protein A Protein Sci. 11 2002 2316 2325
    • (2002) Protein Sci. , vol.11 , pp. 2316-2325
    • Bhattacharya, S.1    Botuyan, M.-V.2    Hsu, F.3    Shan, X.4    Arunkumar, A.I.5    Arrowsmith, C.H.6    Edwards, A.M.7    Chazin, W.J.8
  • 15
    • 0031030449 scopus 로고    scopus 로고
    • Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
    • A. Bochkarev, R.A. Pfuetzner, A.M. Edwards, and L. Frappier Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA Nature 385 1997 176 181
    • (1997) Nature , vol.385 , pp. 176-181
    • Bochkarev, A.1    Pfuetzner, R.A.2    Edwards, A.M.3    Frappier, L.4
  • 16
    • 0037007223 scopus 로고    scopus 로고
    • Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA
    • E.E. Bochkareva, S.S. Korolev, S.P.S. Lees-Miller, and A.A. Bochkarev Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA EMBO J. 21 2002 1855 1863
    • (2002) EMBO J. , vol.21 , pp. 1855-1863
    • Bochkareva, E.E.1    Korolev, S.S.2    Lees-Miller, S.P.S.3    Bochkarev, A.A.4
  • 17
    • 33646850212 scopus 로고    scopus 로고
    • Unveiling the molecular mechanism of a conjugative relaxase: The structure of TrwC complexed with a 27-mer DNA comprising the recognition hairpin and the cleavage site
    • R. Boer, S. Russi, A. Guasch, M. Lucas, A.G. Blanco, R. Pérez-Luque, M. Coll, and F. de la Cruz Unveiling the molecular mechanism of a conjugative relaxase: the structure of TrwC complexed with a 27-mer DNA comprising the recognition hairpin and the cleavage site J. Mol. Biol. 358 2006 857 869
    • (2006) J. Mol. Biol. , vol.358 , pp. 857-869
    • Boer, R.1    Russi, S.2    Guasch, A.3    Lucas, M.4    Blanco, A.G.5    Pérez-Luque, R.6    Coll, M.7    De La Cruz, F.8
  • 18
    • 2942623743 scopus 로고    scopus 로고
    • HnRNP K: One protein multiple processes
    • K. Bomsztyk, O. Denisenko, and J. Ostrowski hnRNP K: one protein multiple processes Bioessays 26 2004 629 638
    • (2004) Bioessays , vol.26 , pp. 629-638
    • Bomsztyk, K.1    Denisenko, O.2    Ostrowski, J.3
  • 19
    • 0036646504 scopus 로고    scopus 로고
    • Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: Solution structure of a complex between hnRNP K KH3 and single-stranded DNA
    • D.T. Braddock, J.L. Baber, D. Levens, and G.M. Clore Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: solution structure of a complex between hnRNP K KH3 and single-stranded DNA EMBO J. 21 2002 3476 3485
    • (2002) EMBO J. , vol.21 , pp. 3476-3485
    • Braddock, D.T.1    Baber, J.L.2    Levens, D.3    Clore, G.M.4
  • 20
    • 0037186549 scopus 로고    scopus 로고
    • Structure and dynamics of KH domains from FBP bound to single-stranded DNA
    • D.T. Braddock, J.M. Louis, J.L. Baber, D. Levens, and G.M. Clore Structure and dynamics of KH domains from FBP bound to single-stranded DNA Nature 415 2002 1051 1056
    • (2002) Nature , vol.415 , pp. 1051-1056
    • Braddock, D.T.1    Louis, J.M.2    Baber, J.L.3    Levens, D.4    Clore, G.M.5
  • 22
    • 0028215301 scopus 로고
    • RNA binding specificity of hnRNP A1: Significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicing
    • C.G. Burd, and G. Dreyfuss RNA binding specificity of hnRNP A1: significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicing EMBO J. 13 1994 1197 1204
    • (1994) EMBO J. , vol.13 , pp. 1197-1204
    • Burd, C.G.1    Dreyfuss, G.2
  • 24
    • 77955933529 scopus 로고    scopus 로고
    • Crystal structures of DNA-Whirly complexes and their role in Arabidopsis organelle genome repair
    • L. Cappadocia, A. Maréchal, J.-S. Parent, E. Lepage, J. Sygusch, and N. Brisson Crystal structures of DNA-Whirly complexes and their role in Arabidopsis organelle genome repair Plant Cell 22 2010 1849 1867
    • (2010) Plant Cell , vol.22 , pp. 1849-1867
    • Cappadocia, L.1    Maréchal, A.2    Parent, J.-S.3    Lepage, E.4    Sygusch, J.5    Brisson, N.6
  • 25
    • 84855293895 scopus 로고    scopus 로고
    • A conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damage
    • L. Cappadocia, J.-S. Parent, E. Zampini, E. Lepage, J. Sygusch, and N. Brisson A conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damage Nucleic Acids Res. 40 2012 258 269
    • (2012) Nucleic Acids Res. , vol.40 , pp. 258-269
    • Cappadocia, L.1    Parent, J.-S.2    Zampini, E.3    Lepage, E.4    Sygusch, J.5    Brisson, N.6
  • 26
    • 64649099756 scopus 로고    scopus 로고
    • Single-stranded DNA-binding protein complex from Helicobacter pylori suggests an ssDNA-binding surface
    • K.-W. Chan, Y.-J. Lee, C.-H. Wang, H. Huang, and Y.-J. Sun Single-stranded DNA-binding protein complex from Helicobacter pylori suggests an ssDNA-binding surface J. Mol. Biol. 388 2009 508 519
    • (2009) J. Mol. Biol. , vol.388 , pp. 508-519
    • Chan, K.-W.1    Lee, Y.-J.2    Wang, C.-H.3    Huang, H.4    Sun, Y.-J.5
  • 27
    • 44349162159 scopus 로고    scopus 로고
    • Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
    • Z. Chen, H. Yang, and N.P. Pavletich Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures Nature 453 2008 489 494
    • (2008) Nature , vol.453 , pp. 489-494
    • Chen, Z.1    Yang, H.2    Pavletich, N.P.3
  • 29
    • 0035861983 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of Oxytricha nova telomere end-binding protein α subunit both uncomplexed and complexed with telomeric ssDNA
    • S. Classen, J.A. Ruggles, and S.C. Schultz Crystal structure of the N-terminal domain of Oxytricha nova telomere end-binding protein α subunit both uncomplexed and complexed with telomeric ssDNA J. Mol. Biol. 314 2001 1113 1125
    • (2001) J. Mol. Biol. , vol.314 , pp. 1113-1125
    • Classen, S.1    Ruggles, J.A.2    Schultz, S.C.3
  • 30
    • 0041989705 scopus 로고    scopus 로고
    • Sequence-specific and 3′-end selective single-strand DNA binding by the Oxytricha nova telomere end binding protein α subunit
    • S. Classen, D. Lyons, T.R. Cech, and S.C. Schultz Sequence-specific and 3′-end selective single-strand DNA binding by the Oxytricha nova telomere end binding protein α subunit Biochemistry 42 2003 9269 9277
    • (2003) Biochemistry , vol.42 , pp. 9269-9277
    • Classen, S.1    Lyons, D.2    Cech, T.R.3    Schultz, S.C.4
  • 34
    • 65549101461 scopus 로고    scopus 로고
    • DNA binding induces active site conformational change in the human TREX2 3′-exonuclease
    • U. de Silva, F.W. Perrino, and T. Hollis DNA binding induces active site conformational change in the human TREX2 3′-exonuclease Nucleic Acids Res. 37 2009 2411 2417
    • (2009) Nucleic Acids Res. , vol.37 , pp. 2411-2417
    • De Silva, U.1    Perrino, F.W.2    Hollis, T.3
  • 35
    • 13744250057 scopus 로고    scopus 로고
    • Whirly transcription factors: Defense gene regulation and beyond
    • D. Desveaux, A. Maréchal, and N. Brisson Whirly transcription factors: defense gene regulation and beyond Trends Plant Sci. 10 2005 95 102
    • (2005) Trends Plant Sci. , vol.10 , pp. 95-102
    • Desveaux, D.1    Maréchal, A.2    Brisson, N.3
  • 36
    • 84872134476 scopus 로고    scopus 로고
    • Nonspecific recognition is achieved in Pot1pC through the use of multiple binding modes
    • T.H. Dickey, M.A. McKercher, and D.S. Wuttke Nonspecific recognition is achieved in Pot1pC through the use of multiple binding modes Structure 21 2013 121 132
    • (2013) Structure , vol.21 , pp. 121-132
    • Dickey, T.H.1    McKercher, M.A.2    Wuttke, D.S.3
  • 37
    • 0033134777 scopus 로고    scopus 로고
    • Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA
    • J. Ding, M.K. Hayashi, Y. Zhang, L. Manche, A.R. Krainer, and R.M. Xu Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA Genes Dev. 13 1999 1102 1115
    • (1999) Genes Dev. , vol.13 , pp. 1102-1115
    • Ding, J.1    Hayashi, M.K.2    Zhang, Y.3    Manche, L.4    Krainer, A.R.5    Xu, R.M.6
  • 38
    • 33644687877 scopus 로고    scopus 로고
    • Crystal structure of the first KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.7 Å
    • Z. Du, J.K. Lee, R. Tjhen, S. Li, H. Pan, R.M. Stroud, and T.L. James Crystal structure of the first KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.7 Å J. Biol. Chem. 280 2005 38823 38830
    • (2005) J. Biol. Chem. , vol.280 , pp. 38823-38830
    • Du, Z.1    Lee, J.K.2    Tjhen, R.3    Li, S.4    Pan, H.5    Stroud, R.M.6    James, T.L.7
  • 39
    • 34250887075 scopus 로고    scopus 로고
    • X-ray crystallographic and NMR studies of protein-protein and protein-nucleic acid interactions involving the KH domains from human poly(C)-binding protein-2
    • Z. Du, J.K. Lee, S. Fenn, R. Tjhen, R.M. Stroud, and T.L. James X-ray crystallographic and NMR studies of protein-protein and protein-nucleic acid interactions involving the KH domains from human poly(C)-binding protein-2 RNA 13 2007 1043 1051
    • (2007) RNA , vol.13 , pp. 1043-1051
    • Du, Z.1    Lee, J.K.2    Fenn, S.3    Tjhen, R.4    Stroud, R.M.5    James, T.L.6
  • 40
    • 57649120777 scopus 로고    scopus 로고
    • Structure of a construct of a human poly(C)-binding protein containing the first and second KH domains reveals insights into its regulatory mechanisms
    • Z. Du, S. Fenn, R. Tjhen, and T.L. James Structure of a construct of a human poly(C)-binding protein containing the first and second KH domains reveals insights into its regulatory mechanisms J. Biol. Chem. 283 2008 28757 28766
    • (2008) J. Biol. Chem. , vol.283 , pp. 28757-28766
    • Du, Z.1    Fenn, S.2    Tjhen, R.3    James, T.L.4
  • 41
    • 80054029342 scopus 로고    scopus 로고
    • DNA stretching by bacterial initiators promotes replication origin opening
    • K.E. Duderstadt, K. Chuang, and J.M. Berger DNA stretching by bacterial initiators promotes replication origin opening Nature 478 2011 209 213
    • (2011) Nature , vol.478 , pp. 209-213
    • Duderstadt, K.E.1    Chuang, K.2    Berger, J.M.3
  • 42
    • 0028206551 scopus 로고
    • A sequence-specific, single-strand binding protein activates the far upstream element of c-myc and defines a new DNA-binding motif
    • R. Duncan, L. Bazar, G. Michelotti, T. Tomonaga, H. Krutzsch, M. Avigan, and D. Levens A sequence-specific, single-strand binding protein activates the far upstream element of c-myc and defines a new DNA-binding motif Genes Dev. 8 1994 465 480
    • (1994) Genes Dev. , vol.8 , pp. 465-480
    • Duncan, R.1    Bazar, L.2    Michelotti, G.3    Tomonaga, T.4    Krutzsch, H.5    Avigan, M.6    Levens, D.7
  • 43
    • 1342327713 scopus 로고    scopus 로고
    • Recognition of DNA substrates by T4 bacteriophage polynucleotide kinase
    • J.H. Eastberg, J. Pelletier, and B.L. Stoddard Recognition of DNA substrates by T4 bacteriophage polynucleotide kinase Nucleic Acids Res. 32 2004 653 660
    • (2004) Nucleic Acids Res. , vol.32 , pp. 653-660
    • Eastberg, J.H.1    Pelletier, J.2    Stoddard, B.L.3
  • 44
    • 31044455231 scopus 로고    scopus 로고
    • Identification of the determinants for the specific recognition of single-strand telomeric DNA by Cdc13
    • A.M. Eldridge, W.A. Halsey, and D.S. Wuttke Identification of the determinants for the specific recognition of single-strand telomeric DNA by Cdc13 Biochemistry 45 2006 871 879
    • (2006) Biochemistry , vol.45 , pp. 871-879
    • Eldridge, A.M.1    Halsey, W.A.2    Wuttke, D.S.3
  • 45
    • 21444433242 scopus 로고    scopus 로고
    • Structure of hnRNP D complexed with single-stranded telomere DNA and unfolding of the quadruplex by heterogeneous nuclear ribonucleoprotein D
    • Y. Enokizono, Y. Konishi, K. Nagata, K. Ouhashi, S. Uesugi, F. Ishikawa, and M. Katahira Structure of hnRNP D complexed with single-stranded telomere DNA and unfolding of the quadruplex by heterogeneous nuclear ribonucleoprotein D J. Biol. Chem. 280 2005 18862 18870
    • (2005) J. Biol. Chem. , vol.280 , pp. 18862-18870
    • Enokizono, Y.1    Konishi, Y.2    Nagata, K.3    Ouhashi, K.4    Uesugi, S.5    Ishikawa, F.6    Katahira, M.7
  • 46
    • 84867693856 scopus 로고    scopus 로고
    • Structure and conformational change of a replication protein A heterotrimer bound to ssDNA
    • J. Fan, and N.P. Pavletich Structure and conformational change of a replication protein A heterotrimer bound to ssDNA Genes Dev. 26 2012 2337 2347
    • (2012) Genes Dev. , vol.26 , pp. 2337-2347
    • Fan, J.1    Pavletich, N.P.2
  • 47
    • 33749134033 scopus 로고    scopus 로고
    • A dynamic model for replication protein A (RPA) function in DNA processing pathways
    • E. Fanning, V. Klimovich, and A.R. Nager A dynamic model for replication protein A (RPA) function in DNA processing pathways Nucleic Acids Res. 34 2006 4126 4137
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4126-4137
    • Fanning, E.1    Klimovich, V.2    Nager, A.R.3
  • 48
    • 34250319300 scopus 로고    scopus 로고
    • Crystal structure of the third KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.6 Å resolution
    • S. Fenn, Z. Du, J.K. Lee, R. Tjhen, R.M. Stroud, and T.L. James Crystal structure of the third KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.6 Å resolution Nucleic Acids Res. 35 2007 2651 2660
    • (2007) Nucleic Acids Res. , vol.35 , pp. 2651-2660
    • Fenn, S.1    Du, Z.2    Lee, J.K.3    Tjhen, R.4    Stroud, R.M.5    James, T.L.6
  • 49
  • 53
    • 84862702956 scopus 로고    scopus 로고
    • Structure and cellular dynamics of Deinococcus radiodurans single-stranded DNA (ssDNA)-binding protein (SSB)-DNA complexes
    • N.P. George, K.V. Ngo, S. Chitteni-Pattu, C.A. Norais, J.R. Battista, M.M. Cox, and J.L. Keck Structure and cellular dynamics of Deinococcus radiodurans single-stranded DNA (ssDNA)-binding protein (SSB)-DNA complexes J. Biol. Chem. 287 2012 22123 22132
    • (2012) J. Biol. Chem. , vol.287 , pp. 22123-22132
    • George, N.P.1    Ngo, K.V.2    Chitteni-Pattu, S.3    Norais, C.A.4    Battista, J.R.5    Cox, M.M.6    Keck, J.L.7
  • 54
    • 0023037564 scopus 로고
    • Telomere proteins: Specific recognition and protection of the natural termini of Oxytricha macronuclear DNA
    • D.E. Gottschling, and V.A. Zakian Telomere proteins: specific recognition and protection of the natural termini of Oxytricha macronuclear DNA Cell 47 1986 195 205
    • (1986) Cell , vol.47 , pp. 195-205
    • Gottschling, D.E.1    Zakian, V.A.2
  • 55
    • 73249115808 scopus 로고    scopus 로고
    • X-ray structure of Pur-α reveals a Whirly-like fold and an unusual nucleic-acid binding surface
    • A. Graebsch, S. Roche, and D. Niessing X-ray structure of Pur-α reveals a Whirly-like fold and an unusual nucleic-acid binding surface Proc. Natl. Acad. Sci. USA 106 2009 18521 18526
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 18521-18526
    • Graebsch, A.1    Roche, S.2    Niessing, D.3
  • 56
    • 0028012282 scopus 로고
    • The major cold shock protein of Bacillus subtilis CspB binds with high affinity to the ATTGG- and CCAAT sequences in single stranded oligonucleotides
    • P. Graumann, and M.A. Marahiel The major cold shock protein of Bacillus subtilis CspB binds with high affinity to the ATTGG- and CCAAT sequences in single stranded oligonucleotides FEBS Lett. 338 1994 157 160
    • (1994) FEBS Lett. , vol.338 , pp. 157-160
    • Graumann, P.1    Marahiel, M.A.2
  • 57
    • 79960066235 scopus 로고    scopus 로고
    • Unraveling the mechanism of BRCA2 in homologous recombination
    • W.K. Holloman Unraveling the mechanism of BRCA2 in homologous recombination Nat. Struct. Mol. Biol. 18 2011 748 754
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 748-754
    • Holloman, W.K.1
  • 59
    • 80053464451 scopus 로고    scopus 로고
    • Structural anatomy of telomere OB proteins
    • M.P. Horvath Structural anatomy of telomere OB proteins Crit. Rev. Biochem. Mol. Biol. 46 2011 409 435
    • (2011) Crit. Rev. Biochem. Mol. Biol. , vol.46 , pp. 409-435
    • Horvath, M.P.1
  • 60
    • 0032431057 scopus 로고    scopus 로고
    • Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA
    • M.P. Horvath, V.L. Schweiker, J.M. Bevilacqua, J.A. Ruggles, and S.C. Schultz Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA Cell 95 1998 963 974
    • (1998) Cell , vol.95 , pp. 963-974
    • Horvath, M.P.1    Schweiker, V.L.2    Bevilacqua, J.M.3    Ruggles, J.A.4    Schultz, S.C.5
  • 61
    • 84866772900 scopus 로고    scopus 로고
    • Crystal structure and DNA-binding mode of Klebsiella pneumoniae primosomal PriB protein
    • Y.-H. Huang, Y.-H. Lo, W. Huang, and C.-Y. Huang Crystal structure and DNA-binding mode of Klebsiella pneumoniae primosomal PriB protein Genes Cells 17 2012 837 849
    • (2012) Genes Cells , vol.17 , pp. 837-849
    • Huang, Y.-H.1    Lo, Y.-H.2    Huang, W.3    Huang, C.-Y.4
  • 62
    • 84868552929 scopus 로고    scopus 로고
    • POT1-TPP1 regulates telomeric overhang structural dynamics
    • H. Hwang, N. Buncher, P.L. Opresko, and S. Myong POT1-TPP1 regulates telomeric overhang structural dynamics Structure 20 2012 1872 1880
    • (2012) Structure , vol.20 , pp. 1872-1880
    • Hwang, H.1    Buncher, N.2    Opresko, P.L.3    Myong, S.4
  • 63
    • 0027263365 scopus 로고
    • Nuclear proteins that bind the pre-mRNA 3′ splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n
    • F. Ishikawa, M.J. Matunis, G. Dreyfuss, and T.R. Cech Nuclear proteins that bind the pre-mRNA 3′ splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n Mol. Cell. Biol. 13 1993 4301 4310
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4301-4310
    • Ishikawa, F.1    Matunis, M.J.2    Dreyfuss, G.3    Cech, T.R.4
  • 64
    • 84867538324 scopus 로고    scopus 로고
    • The hexameric helicase DnaB adopts a nonplanar conformation during translocation
    • O. Itsathitphaisarn, R.A. Wing, W.K. Eliason, J. Wang, and T.A. Steitz The hexameric helicase DnaB adopts a nonplanar conformation during translocation Cell 151 2012 267 277
    • (2012) Cell , vol.151 , pp. 267-277
    • Itsathitphaisarn, O.1    Wing, R.A.2    Eliason, W.K.3    Wang, J.4    Steitz, T.A.5
  • 65
    • 84868191171 scopus 로고    scopus 로고
    • Structural basis for 5′-end-specific recognition of single-stranded DNA by the R3H domain from human Sμbp-2
    • K. Jaudzems, X. Jia, H. Yagi, D. Zhulenkovs, B. Graham, G. Otting, and E. Liepinsh Structural basis for 5′-end-specific recognition of single-stranded DNA by the R3H domain from human Sμbp-2 J. Mol. Biol. 424 2012 42 53
    • (2012) J. Mol. Biol. , vol.424 , pp. 42-53
    • Jaudzems, K.1    Jia, X.2    Yagi, H.3    Zhulenkovs, D.4    Graham, B.5    Otting, G.6    Liepinsh, E.7
  • 67
    • 23944467312 scopus 로고    scopus 로고
    • Poly(C) binding protein family is a transcription factor in μ-opioid receptor gene expression
    • S.-S. Kim, K.K. Pandey, H.S. Choi, S.-Y. Kim, P.-Y. Law, L.-N. Wei, and H.H. Loh Poly(C) binding protein family is a transcription factor in μ-opioid receptor gene expression Mol. Pharmacol. 68 2005 729 736
    • (2005) Mol. Pharmacol. , vol.68 , pp. 729-736
    • Kim, S.-S.1    Pandey, K.K.2    Choi, H.S.3    Kim, S.-Y.4    Law, P.-Y.5    Wei, L.-N.6    Loh, H.H.7
  • 69
    • 0037058877 scopus 로고    scopus 로고
    • Cooperative binding of single-stranded telomeric DNA by the Pot1 protein of Schizosaccharomyces pombe
    • M. Lei, P. Baumann, and T.R. Cech Cooperative binding of single-stranded telomeric DNA by the Pot1 protein of Schizosaccharomyces pombe Biochemistry 41 2002 14560 14568
    • (2002) Biochemistry , vol.41 , pp. 14560-14568
    • Lei, M.1    Baumann, P.2    Cech, T.R.3
  • 70
    • 0345304903 scopus 로고    scopus 로고
    • DNA self-recognition in the structure of Pot1 bound to telomeric single-stranded DNA
    • M. Lei, E.R. Podell, P. Baumann, and T.R. Cech DNA self-recognition in the structure of Pot1 bound to telomeric single-stranded DNA Nature 426 2003 198 203
    • (2003) Nature , vol.426 , pp. 198-203
    • Lei, M.1    Podell, E.R.2    Baumann, P.3    Cech, T.R.4
  • 71
    • 12844265975 scopus 로고    scopus 로고
    • Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection
    • M. Lei, E.R. Podell, and T.R. Cech Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection Nat. Struct. Mol. Biol. 11 2004 1223 1229
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1223-1229
    • Lei, M.1    Podell, E.R.2    Cech, T.R.3
  • 72
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: Recent updates to the protein domain annotation resource
    • I. Letunic, T. Doerks, and P. Bork SMART 7: recent updates to the protein domain annotation resource Nucleic Acids Res. 40 Database issue 2012 D302 D305
    • (2012) Nucleic Acids Res. , vol.40
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 73
    • 84855763327 scopus 로고    scopus 로고
    • Telomerase and telomere-associated proteins: Structural insights into mechanism and evolution
    • K.A. Lewis, and D.S. Wuttke Telomerase and telomere-associated proteins: structural insights into mechanism and evolution Structure 20 2012 28 39
    • (2012) Structure , vol.20 , pp. 28-39
    • Lewis, K.A.1    Wuttke, D.S.2
  • 74
    • 0033860563 scopus 로고    scopus 로고
    • The FBP interacting repressor targets TFIIH to inhibit activated transcription
    • J. Liu, L. He, I. Collins, H. Ge, D. Libutti, J. Li, J.M. Egly, and D. Levens The FBP interacting repressor targets TFIIH to inhibit activated transcription Mol. Cell 5 2000 331 341
    • (2000) Mol. Cell , vol.5 , pp. 331-341
    • Liu, J.1    He, L.2    Collins, I.3    Ge, H.4    Libutti, D.5    Li, J.6    Egly, J.M.7    Levens, D.8
  • 75
    • 33646779199 scopus 로고    scopus 로고
    • The FUSE/FBP/FIR/TFIIH system is a molecular machine programming a pulse of c-myc expression
    • J. Liu, F. Kouzine, Z. Nie, H.-J. Chung, Z. Elisha-Feil, A. Weber, K. Zhao, and D. Levens The FUSE/FBP/FIR/TFIIH system is a molecular machine programming a pulse of c-myc expression EMBO J. 25 2006 2119 2130
    • (2006) EMBO J. , vol.25 , pp. 2119-2130
    • Liu, J.1    Kouzine, F.2    Nie, Z.3    Chung, H.-J.4    Elisha-Feil, Z.5    Weber, A.6    Zhao, K.7    Levens, D.8
  • 76
    • 34249316905 scopus 로고    scopus 로고
    • RNA-binding proteins: Modular design for efficient function
    • B.M. Lunde, C. Moore, and G. Varani RNA-binding proteins: modular design for efficient function Nat. Rev. Mol. Cell Biol. 8 2007 479 490
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 479-490
    • Lunde, B.M.1    Moore, C.2    Varani, G.3
  • 77
    • 0028897341 scopus 로고
    • The transcriptional regulatory protein, YB-1, promotes single-stranded regions in the DRA promoter
    • G.H. MacDonald, Y. Itoh-Lindstrom, and J.P. Ting The transcriptional regulatory protein, YB-1, promotes single-stranded regions in the DRA promoter J. Biol. Chem. 270 1995 3527 3533
    • (1995) J. Biol. Chem. , vol.270 , pp. 3527-3533
    • Macdonald, G.H.1    Itoh-Lindstrom, Y.2    Ting, J.P.3
  • 78
    • 84862633452 scopus 로고    scopus 로고
    • Dynamics in multi-domain protein recognition of RNA
    • C.D. Mackereth, and M. Sattler Dynamics in multi-domain protein recognition of RNA Curr. Opin. Struct. Biol. 22 2012 287 296
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 287-296
    • Mackereth, C.D.1    Sattler, M.2
  • 79
    • 0036223676 scopus 로고    scopus 로고
    • The poly(C)-binding proteins: A multiplicity of functions and a search for mechanisms
    • A.V. Makeyev, and S.A. Liebhaber The poly(C)-binding proteins: a multiplicity of functions and a search for mechanisms RNA 8 2002 265 278
    • (2002) RNA , vol.8 , pp. 265-278
    • Makeyev, A.V.1    Liebhaber, S.A.2
  • 80
    • 33745645838 scopus 로고    scopus 로고
    • T-rich DNA single strands bind to a preformed site on the bacterial cold shock protein Bs-CspB
    • K.E.A. Max, M. Zeeb, R. Bienert, J. Balbach, and U. Heinemann T-rich DNA single strands bind to a preformed site on the bacterial cold shock protein Bs-CspB J. Mol. Biol. 360 2006 702 714
    • (2006) J. Mol. Biol. , vol.360 , pp. 702-714
    • Max, K.E.A.1    Zeeb, M.2    Bienert, R.3    Balbach, J.4    Heinemann, U.5
  • 81
    • 33846991935 scopus 로고    scopus 로고
    • Common mode of DNA binding to cold shock domains. Crystal structure of hexathymidine bound to the domain-swapped form of a major cold shock protein from Bacillus caldolyticus
    • K.E.A. Max, M. Zeeb, R. Bienert, J. Balbach, and U. Heinemann Common mode of DNA binding to cold shock domains. Crystal structure of hexathymidine bound to the domain-swapped form of a major cold shock protein from Bacillus caldolyticus FEBS J. 274 2007 1265 1279
    • (2007) FEBS J. , vol.274 , pp. 1265-1279
    • Max, K.E.A.1    Zeeb, M.2    Bienert, R.3    Balbach, J.4    Heinemann, U.5
  • 83
    • 0027059029 scopus 로고
    • HnRNP A2/B1 binds specifically to single stranded vertebrate telomeric repeat TTAGGGn
    • S.J. McKay, and H. Cooke hnRNP A2/B1 binds specifically to single stranded vertebrate telomeric repeat TTAGGGn Nucleic Acids Res. 20 1992 6461 6464
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6461-6464
    • McKay, S.J.1    Cooke, H.2
  • 84
    • 84868147781 scopus 로고    scopus 로고
    • The processing of repetitive extragenic palindromes: The structure of a repetitive extragenic palindrome bound to its associated nuclease
    • S.A.J. Messing, B. Ton-Hoang, A.B. Hickman, A.J. McCubbin, G.F. Peaslee, R. Ghirlando, M. Chandler, and F. Dyda The processing of repetitive extragenic palindromes: the structure of a repetitive extragenic palindrome bound to its associated nuclease Nucleic Acids Res. 40 2012 9964 9979
    • (2012) Nucleic Acids Res. , vol.40 , pp. 9964-9979
    • Messing, S.A.J.1    Ton-Hoang, B.2    Hickman, A.B.3    McCubbin, A.J.4    Peaslee, G.F.5    Ghirlando, R.6    Chandler, M.7    Dyda, F.8
  • 86
    • 77952771824 scopus 로고    scopus 로고
    • Multiple mechanisms for elongation processivity within the reconstituted Tetrahymena telomerase holoenzyme
    • B. Min, and K. Collins Multiple mechanisms for elongation processivity within the reconstituted Tetrahymena telomerase holoenzyme J. Biol. Chem. 285 2010 16434 16443
    • (2010) J. Biol. Chem. , vol.285 , pp. 16434-16443
    • Min, B.1    Collins, K.2
  • 90
    • 71449106849 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 (HIV-1) induces the cytoplasmic retention of heterogeneous nuclear ribonucleoprotein A1 by disrupting nuclear import: Implications for HIV-1 gene expression
    • A. Monette, L. Ajamian, M. López-Lastra, and A.J. Mouland Human immunodeficiency virus type 1 (HIV-1) induces the cytoplasmic retention of heterogeneous nuclear ribonucleoprotein A1 by disrupting nuclear import: implications for HIV-1 gene expression J. Biol. Chem. 284 2009 31350 31362
    • (2009) J. Biol. Chem. , vol.284 , pp. 31350-31362
    • Monette, A.1    Ajamian, L.2    López-Lastra, M.3    Mouland, A.J.4
  • 91
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • A.G. Murzin OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences EMBO J. 12 1993 861 867
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 92
    • 4444283116 scopus 로고    scopus 로고
    • Human UP1 as a model for understanding purine recognition in the family of proteins containing the RNA recognition motif (RRM)
    • J.C. Myers, and Y. Shamoo Human UP1 as a model for understanding purine recognition in the family of proteins containing the RNA recognition motif (RRM) J. Mol. Biol. 342 2004 743 756
    • (2004) J. Mol. Biol. , vol.342 , pp. 743-756
    • Myers, J.C.1    Shamoo, Y.2
  • 93
    • 0142242183 scopus 로고    scopus 로고
    • Structure-based incorporation of 6-methyl-8-(2-deoxy-β- ribofuranosyl)isoxanthopteridine into the human telomeric repeat DNA as a probe for UP1 binding and destabilization of G-tetrad structures
    • J.C. Myers, S.A. Moore, and Y. Shamoo Structure-based incorporation of 6-methyl-8-(2-deoxy-β-ribofuranosyl)isoxanthopteridine into the human telomeric repeat DNA as a probe for UP1 binding and destabilization of G-tetrad structures J. Biol. Chem. 278 2003 42300 42306
    • (2003) J. Biol. Chem. , vol.278 , pp. 42300-42306
    • Myers, J.C.1    Moore, S.A.2    Shamoo, Y.3
  • 94
    • 76249110370 scopus 로고    scopus 로고
    • How telomeric protein POT1 avoids RNA to achieve specificity for single-stranded DNA
    • J. Nandakumar, E.R. Podell, and T.R. Cech How telomeric protein POT1 avoids RNA to achieve specificity for single-stranded DNA Proc. Natl. Acad. Sci. USA 107 2010 651 656
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 651-656
    • Nandakumar, J.1    Podell, E.R.2    Cech, T.R.3
  • 95
    • 27144451010 scopus 로고    scopus 로고
    • Telomere end-binding proteins control the formation of G-quadruplex DNA structures in vivo
    • K. Paeschke, T. Simonsson, J. Postberg, D. Rhodes, and H.J. Lipps Telomere end-binding proteins control the formation of G-quadruplex DNA structures in vivo Nat. Struct. Mol. Biol. 12 2005 847 854
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 847-854
    • Paeschke, K.1    Simonsson, T.2    Postberg, J.3    Rhodes, D.4    Lipps, H.J.5
  • 96
    • 0032806445 scopus 로고    scopus 로고
    • PUF60: A novel U2AF65-related splicing activity
    • P.S. Page-McCaw, K. Amonlirdviman, and P.A. Sharp PUF60: a novel U2AF65-related splicing activity RNA 5 1999 1548 1560
    • (1999) RNA , vol.5 , pp. 1548-1560
    • Page-Mccaw, P.S.1    Amonlirdviman, K.2    Sharp, P.A.3
  • 97
    • 0036176232 scopus 로고    scopus 로고
    • Dimeric structure of the Oxytricha nova telomere end-binding protein α-subunit bound to ssDNA
    • O.B. Peersen, J.A. Ruggles, and S.C. Schultz Dimeric structure of the Oxytricha nova telomere end-binding protein α-subunit bound to ssDNA Nat. Struct. Biol. 9 2002 182 187
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 182-187
    • Peersen, O.B.1    Ruggles, J.A.2    Schultz, S.C.3
  • 98
    • 84863842721 scopus 로고    scopus 로고
    • MRNA decay factor AUF1 maintains normal aging, telomere maintenance, and suppression of senescence by activation of telomerase transcription
    • A.R. Pont, N. Sadri, S.J. Hsiao, S. Smith, and R.J. Schneider mRNA decay factor AUF1 maintains normal aging, telomere maintenance, and suppression of senescence by activation of telomerase transcription Mol. Cell 47 2012 5 15
    • (2012) Mol. Cell , vol.47 , pp. 5-15
    • Pont, A.R.1    Sadri, N.2    Hsiao, S.J.3    Smith, S.4    Schneider, R.J.5
  • 100
    • 2542596992 scopus 로고    scopus 로고
    • Roles of AUF1 isoforms, HuR and BRF1 in ARE-dependent mRNA turnover studied by RNA interference
    • I. Raineri, D. Wegmueller, B. Gross, U. Certa, and C. Moroni Roles of AUF1 isoforms, HuR and BRF1 in ARE-dependent mRNA turnover studied by RNA interference Nucleic Acids Res. 32 2004 1279 1288
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1279-1288
    • Raineri, I.1    Wegmueller, D.2    Gross, B.3    Certa, U.4    Moroni, C.5
  • 101
    • 84055217954 scopus 로고    scopus 로고
    • RNA single strands bind to a conserved surface of the major cold shock protein in crystals and solution
    • R. Sachs, K.E.A. Max, U. Heinemann, and J. Balbach RNA single strands bind to a conserved surface of the major cold shock protein in crystals and solution RNA 18 2012 65 76
    • (2012) RNA , vol.18 , pp. 65-76
    • Sachs, R.1    Max, K.E.A.2    Heinemann, U.3    Balbach, J.4
  • 102
    • 0041689753 scopus 로고    scopus 로고
    • Selective degradation of AU-rich mRNAs promoted by the p37 AUF1 protein isoform
    • B. Sarkar, Q. Xi, C. He, and R.J. Schneider Selective degradation of AU-rich mRNAs promoted by the p37 AUF1 protein isoform Mol. Cell. Biol. 23 2003 6685 6693
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6685-6693
    • Sarkar, B.1    Xi, Q.2    He, C.3    Schneider, R.J.4
  • 103
  • 104
    • 77958096076 scopus 로고    scopus 로고
    • Determining the specificity of protein-DNA interactions
    • G.D. Stormo, and Y. Zhao Determining the specificity of protein-DNA interactions Nat. Rev. Genet. 11 2010 751 760
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 751-760
    • Stormo, G.D.1    Zhao, Y.2
  • 106
    • 85027917185 scopus 로고    scopus 로고
    • Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase α
    • J. Sun, Y. Yang, K. Wan, N. Mao, T.-Y. Yu, Y.-C. Lin, D.C. DeZwaan, B.C. Freeman, J.-J. Lin, N.F. Lue, and M. Lei Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase α Cell Res. 21 2011 258 274
    • (2011) Cell Res. , vol.21 , pp. 258-274
    • Sun, J.1    Yang, Y.2    Wan, K.3    Mao, N.4    Yu, T.-Y.5    Lin, Y.-C.6    Dezwaan, D.C.7    Freeman, B.C.8    Lin, J.-J.9    Lue, N.F.10    Lei, M.11
  • 107
    • 0027182876 scopus 로고
    • Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter, in vitro
    • M. Takimoto, T. Tomonaga, M. Matunis, M. Avigan, H. Krutzsch, G. Dreyfuss, and D. Levens Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter, in vitro J. Biol. Chem. 268 1993 18249 18258
    • (1993) J. Biol. Chem. , vol.268 , pp. 18249-18258
    • Takimoto, M.1    Tomonaga, T.2    Matunis, M.3    Avigan, M.4    Krutzsch, H.5    Dreyfuss, G.6    Levens, D.7
  • 108
    • 0042035638 scopus 로고    scopus 로고
    • Nucleotide shuffling and ssDNA recognition in Oxytricha nova telomere end-binding protein complexes
    • D.L. Theobald, and S.C. Schultz Nucleotide shuffling and ssDNA recognition in Oxytricha nova telomere end-binding protein complexes EMBO J. 22 2003 4314 4324
    • (2003) EMBO J. , vol.22 , pp. 4314-4324
    • Theobald, D.L.1    Schultz, S.C.2
  • 110
    • 0028905957 scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K is a DNA-binding transactivator
    • T. Tomonaga, and D. Levens Heterogeneous nuclear ribonucleoprotein K is a DNA-binding transactivator J. Biol. Chem. 270 1995 4875 4881
    • (1995) J. Biol. Chem. , vol.270 , pp. 4875-4881
    • Tomonaga, T.1    Levens, D.2
  • 111
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the Universal Protein Resource (UniProt)
    • UniProt Consortium
    • UniProt Consortium Reorganizing the protein space at the Universal Protein Resource (UniProt) Nucleic Acids Res. 40 Database issue 2012 D71 D75
    • (2012) Nucleic Acids Res. , vol.40
  • 112
    • 43549124851 scopus 로고    scopus 로고
    • Structure and function of KH domains
    • R. Valverde, L. Edwards, and L. Regan Structure and function of KH domains FEBS J. 275 2008 2712 2726
    • (2008) FEBS J. , vol.275 , pp. 2712-2726
    • Valverde, R.1    Edwards, L.2    Regan, L.3
  • 113
    • 0007570010 scopus 로고    scopus 로고
    • The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation
    • W. van der Houven van Oordt, M.T. Diaz-Meco, J. Lozano, A.R. Krainer, J. Moscat, and J.F. Cáceres The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation J. Cell Biol. 149 2000 307 316
    • (2000) J. Cell Biol. , vol.149 , pp. 307-316
    • Van Der Houven Van Oordt, W.1    Diaz-Meco, M.T.2    Lozano, J.3    Krainer, A.R.4    Moscat, J.5    Cáceres, J.F.6
  • 114
    • 33846691378 scopus 로고    scopus 로고
    • The POT1-TPP1 telomere complex is a telomerase processivity factor
    • F. Wang, E.R. Podell, A.J. Zaug, Y. Yang, P. Baciu, T.R. Cech, and M. Lei The POT1-TPP1 telomere complex is a telomerase processivity factor Nature 445 2007 506 510
    • (2007) Nature , vol.445 , pp. 506-510
    • Wang, F.1    Podell, E.R.2    Zaug, A.J.3    Yang, Y.4    Baciu, P.5    Cech, T.R.6    Lei, M.7
  • 115
    • 84877826875 scopus 로고    scopus 로고
    • Post-transcriptional control of gene expression by AUF1: Mechanisms, physiological targets, and regulation
    • E.J.F. White, G. Brewer, and G.M. Wilson Post-transcriptional control of gene expression by AUF1: mechanisms, physiological targets, and regulation Biochim. Biophys. Acta 1829 2013 680 688
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 680-688
    • White, E.J.F.1    Brewer, G.2    Wilson, G.M.3
  • 117
    • 33846692105 scopus 로고    scopus 로고
    • TPP1 is a homologue of ciliate TEBP-β and interacts with POT1 to recruit telomerase
    • H. Xin, D. Liu, M. Wan, A. Safari, H. Kim, W. Sun, M.S. O'Connor, and Z. Songyang TPP1 is a homologue of ciliate TEBP-β and interacts with POT1 to recruit telomerase Nature 445 2007 559 562
    • (2007) Nature , vol.445 , pp. 559-562
    • Xin, H.1    Liu, D.2    Wan, M.3    Safari, A.4    Kim, H.5    Sun, W.6    O'Connor, M.S.7    Songyang, Z.8
  • 118
    • 84862157578 scopus 로고    scopus 로고
    • Genetic recombination in Bacillus subtilis: A division of labor between two single-strand DNA-binding proteins
    • T. Yadav, B. Carrasco, A.R. Myers, N.P. George, J.L. Keck, and J.C. Alonso Genetic recombination in Bacillus subtilis: a division of labor between two single-strand DNA-binding proteins Nucleic Acids Res. 40 2012 5546 5559
    • (2012) Nucleic Acids Res. , vol.40 , pp. 5546-5559
    • Yadav, T.1    Carrasco, B.2    Myers, A.R.3    George, N.P.4    Keck, J.L.5    Alonso, J.C.6
  • 122
    • 33750008214 scopus 로고    scopus 로고
    • Recognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution
    • M. Zeeb, K.E.A. Max, U. Weininger, C. Löw, H. Sticht, and J. Balbach Recognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution Nucleic Acids Res. 34 2006 4561 4571
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4561-4571
    • Zeeb, M.1    Max, K.E.A.2    Weininger, U.3    Löw, C.4    Sticht, H.5    Balbach, J.6
  • 123
    • 84862907900 scopus 로고    scopus 로고
    • Structural basis for Tetrahymena telomerase processivity factor Teb1 binding to single-stranded telomeric-repeat DNA
    • Z. Zeng, B. Min, J. Huang, K. Hong, Y. Yang, K. Collins, and M. Lei Structural basis for Tetrahymena telomerase processivity factor Teb1 binding to single-stranded telomeric-repeat DNA Proc. Natl. Acad. Sci. USA 108 2011 20357 20361
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20357-20361
    • Zeng, Z.1    Min, B.2    Huang, J.3    Hong, K.4    Yang, Y.5    Collins, K.6    Lei, M.7
  • 124
    • 84879421217 scopus 로고    scopus 로고
    • Far upstream element binding protein 1: A commander of transcription, translation and beyond
    • 10.1038/onc.2012.350 Published online August 27, 2012
    • J. Zhang, and Q.M. Chen Far upstream element binding protein 1: a commander of transcription, translation and beyond Oncogene 2012 10.1038/onc.2012.350 Published online August 27, 2012
    • (2012) Oncogene
    • Zhang, J.1    Chen, Q.M.2
  • 126
    • 0035909804 scopus 로고    scopus 로고
    • The affinity-enhancing roles of flexible linkers in two-domain DNA-binding proteins
    • H.X. Zhou The affinity-enhancing roles of flexible linkers in two-domain DNA-binding proteins Biochemistry 40 2001 15069 15073
    • (2001) Biochemistry , vol.40 , pp. 15069-15073
    • Zhou, H.X.1
  • 127
    • 79960804204 scopus 로고    scopus 로고
    • SSB functions as a sliding platform that migrates on DNA via reptation
    • R. Zhou, A.G. Kozlov, R. Roy, J. Zhang, S. Korolev, T.M. Lohman, and T. Ha SSB functions as a sliding platform that migrates on DNA via reptation Cell 146 2011 222 232
    • (2011) Cell , vol.146 , pp. 222-232
    • Zhou, R.1    Kozlov, A.G.2    Roy, R.3    Zhang, J.4    Korolev, S.5    Lohman, T.M.6    Ha, T.7
  • 128
    • 78649865439 scopus 로고    scopus 로고
    • Alternatively expressed domains of AU-rich element RNA-binding protein 1 (AUF1) regulate RNA-binding affinity, RNA-induced protein oligomerization, and the local conformation of bound RNA ligands
    • B.E. Zucconi, J.D. Ballin, B.Y. Brewer, C.R. Ross, J. Huang, E.A. Toth, and G.M. Wilson Alternatively expressed domains of AU-rich element RNA-binding protein 1 (AUF1) regulate RNA-binding affinity, RNA-induced protein oligomerization, and the local conformation of bound RNA ligands J. Biol. Chem. 285 2010 39127 39139
    • (2010) J. Biol. Chem. , vol.285 , pp. 39127-39139
    • Zucconi, B.E.1    Ballin, J.D.2    Brewer, B.Y.3    Ross, C.R.4    Huang, J.5    Toth, E.A.6    Wilson, G.M.7


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