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Volumn 427, Issue 19, 2015, Pages 3001-3022

The Signature of the Five-Stranded vRRM Fold Defined by Functional, Structural and Computational Analysis of the hnRNP L Protein

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE TRANSPORTER 2; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN L; POLYPYRIMIDINE TRACT BINDING PROTEIN; RNA;

EID: 84941938743     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2015.05.020     Document Type: Article
Times cited : (24)

References (87)
  • 2
    • 18544377013 scopus 로고    scopus 로고
    • The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression
    • C. Maris, C. Dominguez, and F.H. Allain The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression FEBS J 272 2005 2118 2131
    • (2005) FEBS J , vol.272 , pp. 2118-2131
    • Maris, C.1    Dominguez, C.2    Allain, F.H.3
  • 3
    • 84867595792 scopus 로고    scopus 로고
    • Structural insight into RNA recognition motifs: Versatile molecular Lego building blocks for biological systems
    • Y. Muto, and S. Yokoyama Structural insight into RNA recognition motifs: versatile molecular Lego building blocks for biological systems Wiley Interdiscip Rev RNA 3 2012 229 246
    • (2012) Wiley Interdiscip Rev RNA , vol.3 , pp. 229-246
    • Muto, Y.1    Yokoyama, S.2
  • 4
    • 0025761656 scopus 로고
    • RNA recognition: Towards identifying determinants of specificity
    • D.J. Kenan, C.C. Query, and J.D. Keene RNA recognition: towards identifying determinants of specificity Trends Biochem Sci 16 1991 214 220
    • (1991) Trends Biochem Sci , vol.16 , pp. 214-220
    • Kenan, D.J.1    Query, C.C.2    Keene, J.D.3
  • 6
    • 0029920331 scopus 로고    scopus 로고
    • Specificity of ribonucleoprotein interaction determined by RNA folding during complex formulation
    • F.H. Allain, C.C. Gubser, P.W. Howe, K. Nagai, D. Neuhaus, and G. Varani Specificity of ribonucleoprotein interaction determined by RNA folding during complex formulation Nature 380 1996 646 650
    • (1996) Nature , vol.380 , pp. 646-650
    • Allain, F.H.1    Gubser, C.C.2    Howe, P.W.3    Nagai, K.4    Neuhaus, D.5    Varani, G.6
  • 8
    • 84871807395 scopus 로고    scopus 로고
    • The RRM domain of human fused in sarcoma protein reveals a non-canonical nucleic acid binding site
    • X. Liu, C. Niu, J. Ren, J. Zhang, X. Xie, H. Zhu, and et al. The RRM domain of human fused in sarcoma protein reveals a non-canonical nucleic acid binding site Biochim Biophys Acta 1832 2013 375 385
    • (2013) Biochim Biophys Acta , vol.1832 , pp. 375-385
    • Liu, X.1    Niu, C.2    Ren, J.3    Zhang, J.4    Xie, X.5    Zhu, H.6
  • 9
    • 25444486174 scopus 로고    scopus 로고
    • Structure of PTB bound to RNA: Specific binding and implications for splicing regulation
    • F.C. Oberstrass, S.D. Auweter, M. Erat, Y. Hargous, A. Henning, P. Wenter, and et al. Structure of PTB bound to RNA: specific binding and implications for splicing regulation Science 309 2005 2054 2057
    • (2005) Science , vol.309 , pp. 2054-2057
    • Oberstrass, F.C.1    Auweter, S.D.2    Erat, M.3    Hargous, Y.4    Henning, A.5    Wenter, P.6
  • 10
    • 0024835141 scopus 로고
    • A novel heterogeneous nuclear RNP protein with a unique distribution on nascent transcripts
    • S. Pinol-Roma, M.S. Swanson, J.G. Gall, and G. Dreyfuss A novel heterogeneous nuclear RNP protein with a unique distribution on nascent transcripts J Cell Biol 109 1989 2575 2587
    • (1989) J Cell Biol , vol.109 , pp. 2575-2587
    • Pinol-Roma, S.1    Swanson, M.S.2    Gall, J.G.3    Dreyfuss, G.4
  • 11
    • 0023979999 scopus 로고
    • Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation
    • G. Dreyfuss, M.S. Swanson, and S. Pinol-Roma Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation Trends Biochem Sci 13 1988 86 91
    • (1988) Trends Biochem Sci , vol.13 , pp. 86-91
    • Dreyfuss, G.1    Swanson, M.S.2    Pinol-Roma, S.3
  • 12
    • 0033555522 scopus 로고    scopus 로고
    • Regulation of human vascular endothelial growth factor mRNA stability in hypoxia by heterogeneous nuclear ribonucleoprotein L
    • S.C. Shih, and K.P. Claffey Regulation of human vascular endothelial growth factor mRNA stability in hypoxia by heterogeneous nuclear ribonucleoprotein L J Biol Chem 274 1999 1359 1365
    • (1999) J Biol Chem , vol.274 , pp. 1359-1365
    • Shih, S.C.1    Claffey, K.P.2
  • 13
    • 0037217365 scopus 로고    scopus 로고
    • HnRNP L stimulates splicing of the eNOS gene by binding to variable-length CA repeats
    • J. Hui, K. Stangl, W.S. Lane, and A. Bindereif HnRNP L stimulates splicing of the eNOS gene by binding to variable-length CA repeats Nat Struct Biol 10 2003 33 37
    • (2003) Nat Struct Biol , vol.10 , pp. 33-37
    • Hui, J.1    Stangl, K.2    Lane, W.S.3    Bindereif, A.4
  • 14
    • 0035941211 scopus 로고    scopus 로고
    • Determination of the RNA binding specificity of the heterogeneous nuclear ribonucleoprotein (hnRNP) H/H′/F/2H9 family
    • M. Caputi, and A.M. Zahler Determination of the RNA binding specificity of the heterogeneous nuclear ribonucleoprotein (hnRNP) H/H′/F/2H9 family J Biol Chem 276 2001 43850 43859
    • (2001) J Biol Chem , vol.276 , pp. 43850-43859
    • Caputi, M.1    Zahler, A.M.2
  • 15
    • 58149395090 scopus 로고    scopus 로고
    • Control of the papillomavirus early-to-late switch by differentially expressed SRp20
    • R. Jia, X. Liu, M. Tao, M. Kruhlak, M. Guo, C. Meyers, and et al. Control of the papillomavirus early-to-late switch by differentially expressed SRp20 J Virol 83 2009 167 180
    • (2009) J Virol , vol.83 , pp. 167-180
    • Jia, R.1    Liu, X.2    Tao, M.3    Kruhlak, M.4    Guo, M.5    Meyers, C.6
  • 16
    • 21244469877 scopus 로고    scopus 로고
    • Intronic CA-repeat and CA-rich elements: A new class of regulators of mammalian alternative splicing
    • J. Hui, L.H. Hung, M. Heiner, S. Schreiner, N. Neumuller, G. Reither, and et al. Intronic CA-repeat and CA-rich elements: a new class of regulators of mammalian alternative splicing EMBO J 24 2005 1988 1998
    • (2005) EMBO J , vol.24 , pp. 1988-1998
    • Hui, J.1    Hung, L.H.2    Heiner, M.3    Schreiner, S.4    Neumuller, N.5    Reither, G.6
  • 17
    • 0032478588 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein interacts with HnRNP L
    • B. Hahm, O.H. Cho, J.E. Kim, Y.K. Kim, J.H. Kim, Y.L. Oh, and et al. Polypyrimidine tract-binding protein interacts with HnRNP L FEBS Lett 425 1998 401 406
    • (1998) FEBS Lett , vol.425 , pp. 401-406
    • Hahm, B.1    Cho, O.H.2    Kim, J.E.3    Kim, Y.K.4    Kim, J.H.5    Oh, Y.L.6
  • 18
    • 84876820281 scopus 로고    scopus 로고
    • HnRNP L and hnRNP A1 induce extended U1 snRNA interactions with an exon to repress spliceosome assembly
    • N.T. Chiou, G. Shankarling, and K.W. Lynch HnRNP L and hnRNP A1 induce extended U1 snRNA interactions with an exon to repress spliceosome assembly Mol Cell 49 2013 972 982
    • (2013) Mol Cell , vol.49 , pp. 972-982
    • Chiou, N.T.1    Shankarling, G.2    Lynch, K.W.3
  • 20
    • 0042808438 scopus 로고    scopus 로고
    • Novel functional role of CA repeats and hnRNP L in RNA stability
    • J. Hui, G. Reither, and A. Bindereif Novel functional role of CA repeats and hnRNP L in RNA stability RNA 9 2003 931 936
    • (2003) RNA , vol.9 , pp. 931-936
    • Hui, J.1    Reither, G.2    Bindereif, A.3
  • 21
    • 16244402306 scopus 로고    scopus 로고
    • Rhythmic serotonin N-acetyltransferase mRNA degradation is essential for the maintenance of its circadian oscillation
    • T.D. Kim, J.S. Kim, J.H. Kim, J. Myung, H.D. Chae, K.C. Woo, and et al. Rhythmic serotonin N-acetyltransferase mRNA degradation is essential for the maintenance of its circadian oscillation Mol Cell Biol 25 2005 3232 3246
    • (2005) Mol Cell Biol , vol.25 , pp. 3232-3246
    • Kim, T.D.1    Kim, J.S.2    Kim, J.H.3    Myung, J.4    Chae, H.D.5    Woo, K.C.6
  • 23
    • 84871740038 scopus 로고    scopus 로고
    • HnRNPL and nucleolin bind LINE-1 RNA and function as host factors to modulate retrotransposition
    • S. Peddigari, P.W. Li, J.L. Rabe, and S.L. Martin hnRNPL and nucleolin bind LINE-1 RNA and function as host factors to modulate retrotransposition Nucleic Acids Res 41 2013 575 585
    • (2013) Nucleic Acids Res , vol.41 , pp. 575-585
    • Peddigari, S.1    Li, P.W.2    Rabe, J.L.3    Martin, S.L.4
  • 24
    • 22544468490 scopus 로고    scopus 로고
    • Binding of hnRNP L to the pre-mRNA processing enhancer of the herpes simplex virus thymidine kinase gene enhances both polyadenylation and nucleocytoplasmic export of intronless mRNAs
    • S. Guang, A.M. Felthauser, and J.E. Mertz Binding of hnRNP L to the pre-mRNA processing enhancer of the herpes simplex virus thymidine kinase gene enhances both polyadenylation and nucleocytoplasmic export of intronless mRNAs Mol Cell Biol 25 2005 6303 6313
    • (2005) Mol Cell Biol , vol.25 , pp. 6303-6313
    • Guang, S.1    Felthauser, A.M.2    Mertz, J.E.3
  • 25
    • 0029142841 scopus 로고
    • HnRNP L binds a cis-acting RNA sequence element that enables intron-dependent gene expression
    • X. Liu, and J.E. Mertz HnRNP L binds a cis-acting RNA sequence element that enables intron-dependent gene expression Genes Dev 9 1995 1766 1780
    • (1995) Genes Dev , vol.9 , pp. 1766-1780
    • Liu, X.1    Mertz, J.E.2
  • 26
    • 79953797091 scopus 로고    scopus 로고
    • Repression of VEGFA by CA-rich element-binding microRNAs is modulated by hnRNP L
    • F. Jafarifar, P. Yao, S.M. Eswarappa, and P.L. Fox Repression of VEGFA by CA-rich element-binding microRNAs is modulated by hnRNP L EMBO J 30 2011 1324 1334
    • (2011) EMBO J , vol.30 , pp. 1324-1334
    • Jafarifar, F.1    Yao, P.2    Eswarappa, S.M.3    Fox, P.L.4
  • 27
    • 60149091561 scopus 로고    scopus 로고
    • A stress-responsive RNA switch regulates VEGFA expression
    • P.S. Ray, J. Jia, P. Yao, M. Majumder, M. Hatzoglou, and P.L. Fox A stress-responsive RNA switch regulates VEGFA expression Nature 457 2009 915 919
    • (2009) Nature , vol.457 , pp. 915-919
    • Ray, P.S.1    Jia, J.2    Yao, P.3    Majumder, M.4    Hatzoglou, M.5    Fox, P.L.6
  • 28
    • 38649129366 scopus 로고    scopus 로고
    • Diverse roles of hnRNP L in mammalian mRNA processing: A combined microarray and RNAi analysis
    • L.H. Hung, M. Heiner, J. Hui, S. Schreiner, V. Benes, and A. Bindereif Diverse roles of hnRNP L in mammalian mRNA processing: a combined microarray and RNAi analysis RNA 14 2008 284 296
    • (2008) RNA , vol.14 , pp. 284-296
    • Hung, L.H.1    Heiner, M.2    Hui, J.3    Schreiner, S.4    Benes, V.5    Bindereif, A.6
  • 29
    • 84862002189 scopus 로고    scopus 로고
    • Alternative splicing controlled by heterogeneous nuclear ribonucleoprotein L regulates development, proliferation, and migration of thymic pre-T cells
    • M.C. Gaudreau, F. Heyd, R. Bastien, B. Wilhelm, and T. Moroy Alternative splicing controlled by heterogeneous nuclear ribonucleoprotein L regulates development, proliferation, and migration of thymic pre-T cells J Immunol 188 2012 5377 5388
    • (2012) J Immunol , vol.188 , pp. 5377-5388
    • Gaudreau, M.C.1    Heyd, F.2    Bastien, R.3    Wilhelm, B.4    Moroy, T.5
  • 30
    • 74749089043 scopus 로고    scopus 로고
    • Context-dependent regulatory mechanism of the splicing factor hnRNP L
    • L.B. Motta-Mena, F. Heyd, and K.W. Lynch Context-dependent regulatory mechanism of the splicing factor hnRNP L Mol Cell 37 2010 223 234
    • (2010) Mol Cell , vol.37 , pp. 223-234
    • Motta-Mena, L.B.1    Heyd, F.2    Lynch, K.W.3
  • 31
    • 23844471326 scopus 로고    scopus 로고
    • HnRNP L represses exon splicing via a regulated exonic splicing silencer
    • C.R. Rothrock, A.E. House, and K.W. Lynch HnRNP L represses exon splicing via a regulated exonic splicing silencer EMBO J 24 2005 2792 2802
    • (2005) EMBO J , vol.24 , pp. 2792-2802
    • Rothrock, C.R.1    House, A.E.2    Lynch, K.W.3
  • 32
    • 84863224489 scopus 로고    scopus 로고
    • HnRNP L and L-like cooperate in multiple-exon regulation of CD45 alternative splicing
    • M. Preussner, S. Schreiner, L.H. Hung, M. Porstner, H.M. Jack, V. Benes, and et al. HnRNP L and L-like cooperate in multiple-exon regulation of CD45 alternative splicing Nucleic Acids Res 40 2012 5666 5678
    • (2012) Nucleic Acids Res , vol.40 , pp. 5666-5678
    • Preussner, M.1    Schreiner, S.2    Hung, L.H.3    Porstner, M.4    Jack, H.M.5    Benes, V.6
  • 33
    • 33646777183 scopus 로고    scopus 로고
    • HnRNP L regulates differences in expression of mouse integrin alpha2beta1
    • Y. Cheli, and T.J. Kunicki hnRNP L regulates differences in expression of mouse integrin alpha2beta1 Blood 107 2006 4391 4398
    • (2006) Blood , vol.107 , pp. 4391-4398
    • Cheli, Y.1    Kunicki, T.J.2
  • 34
    • 79955545315 scopus 로고    scopus 로고
    • Mechanistic control of carcinoembryonic antigen-related cell adhesion molecule-1 (CEACAM1) splice isoforms by the heterogeneous nuclear ribonuclear proteins hnRNP L, hnRNP A1, and hnRNP M
    • K.J. Dery, S. Gaur, M. Gencheva, Y. Yen, J.E. Shively, and R.K. Gaur Mechanistic control of carcinoembryonic antigen-related cell adhesion molecule-1 (CEACAM1) splice isoforms by the heterogeneous nuclear ribonuclear proteins hnRNP L, hnRNP A1, and hnRNP M J Biol Chem 286 2011 16039 16051
    • (2011) J Biol Chem , vol.286 , pp. 16039-16051
    • Dery, K.J.1    Gaur, S.2    Gencheva, M.3    Yen, Y.4    Shively, J.E.5    Gaur, R.K.6
  • 35
    • 78049448047 scopus 로고    scopus 로고
    • HnRNP L regulates the tumorigenic capacity of lung cancer xenografts in mice via caspase-9 pre-mRNA processing
    • R.W. Goehe, J.C. Shultz, C. Murudkar, S. Usanovic, N.F. Lamour, D.H. Massey, and et al. hnRNP L regulates the tumorigenic capacity of lung cancer xenografts in mice via caspase-9 pre-mRNA processing J Clin Invest 120 2010 3923 3939
    • (2010) J Clin Invest , vol.120 , pp. 3923-3939
    • Goehe, R.W.1    Shultz, J.C.2    Murudkar, C.3    Usanovic, S.4    Lamour, N.F.5    Massey, D.H.6
  • 36
    • 74549123779 scopus 로고    scopus 로고
    • HnRNP L-mediated regulation of mammalian alternative splicing by interference with splice site recognition
    • M. Heiner, J. Hui, S. Schreiner, L.H. Hung, and A. Bindereif HnRNP L-mediated regulation of mammalian alternative splicing by interference with splice site recognition RNA Biol 7 2010 56 64
    • (2010) RNA Biol , vol.7 , pp. 56-64
    • Heiner, M.1    Hui, J.2    Schreiner, S.3    Hung, L.H.4    Bindereif, A.5
  • 37
    • 29044447700 scopus 로고    scopus 로고
    • Alternative pre-mRNA splicing in the human system: Unexpected role of repetitive sequences as regulatory elements
    • J. Hui, and A. Bindereif Alternative pre-mRNA splicing in the human system: unexpected role of repetitive sequences as regulatory elements Biol Chem 386 2005 1265 1271
    • (2005) Biol Chem , vol.386 , pp. 1265-1271
    • Hui, J.1    Bindereif, A.2
  • 38
    • 67650120109 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein L Is a subunit of human KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity in vivo
    • W. Yuan, J. Xie, C. Long, H. Erdjument-Bromage, X. Ding, Y. Zheng, and et al. Heterogeneous nuclear ribonucleoprotein L Is a subunit of human KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity in vivo J Biol Chem 284 2009 15701 15707
    • (2009) J Biol Chem , vol.284 , pp. 15701-15707
    • Yuan, W.1    Xie, J.2    Long, C.3    Erdjument-Bromage, H.4    Ding, X.5    Zheng, Y.6
  • 39
    • 62849102677 scopus 로고    scopus 로고
    • Auto- and cross-regulation of the hnRNP L proteins by alternative splicing
    • O. Rossbach, L.H. Hung, S. Schreiner, I. Grishina, M. Heiner, J. Hui, and et al. Auto- and cross-regulation of the hnRNP L proteins by alternative splicing Mol Cell Biol 29 2009 1442 1451
    • (2009) Mol Cell Biol , vol.29 , pp. 1442-1451
    • Rossbach, O.1    Hung, L.H.2    Schreiner, S.3    Grishina, I.4    Heiner, M.5    Hui, J.6
  • 40
    • 0030250111 scopus 로고    scopus 로고
    • The roles of heterogeneous nuclear ribonucleoproteins (hnRNP) in RNA metabolism
    • F. Weighardt, G. Biamonti, and S. Riva The roles of heterogeneous nuclear ribonucleoproteins (hnRNP) in RNA metabolism Bioessays 18 1996 747 756
    • (1996) Bioessays , vol.18 , pp. 747-756
    • Weighardt, F.1    Biamonti, G.2    Riva, S.3
  • 41
    • 0029896047 scopus 로고    scopus 로고
    • HnRNP A1 selectively interacts through its Gly-rich domain with different RNA-binding proteins
    • L. Cartegni, M. Maconi, E. Morandi, F. Cobianchi, S. Riva, and G. Biamonti hnRNP A1 selectively interacts through its Gly-rich domain with different RNA-binding proteins J Mol Biol 259 1996 337 348
    • (1996) J Mol Biol , vol.259 , pp. 337-348
    • Cartegni, L.1    Maconi, M.2    Morandi, E.3    Cobianchi, F.4    Riva, S.5    Biamonti, G.6
  • 42
    • 0028326761 scopus 로고
    • New insights into the auxiliary domains of eukaryotic RNA-binding proteins
    • G. Biamonti, and S. Riva New insights into the auxiliary domains of eukaryotic RNA-binding proteins FEBS Lett 340 1994 1 8
    • (1994) FEBS Lett , vol.340 , pp. 1-8
    • Biamonti, G.1    Riva, S.2
  • 43
    • 84881232947 scopus 로고    scopus 로고
    • Crystal structures and RNA-binding properties of the RNA recognition motifs of heterogeneous nuclear ribonucleoprotein L: Insights into its roles in alternative splicing regulation
    • W. Zhang, F. Zeng, Y. Liu, Y. Zhao, H. Lv, L. Niu, and et al. Crystal structures and RNA-binding properties of the RNA recognition motifs of heterogeneous nuclear ribonucleoprotein L: insights into its roles in alternative splicing regulation J Biol Chem 288 2013 22636 22649
    • (2013) J Biol Chem , vol.288 , pp. 22636-22649
    • Zhang, W.1    Zeng, F.2    Liu, Y.3    Zhao, Y.4    Lv, H.5    Niu, L.6
  • 44
    • 0032864043 scopus 로고    scopus 로고
    • Adaptive recognition in RNA complexes with peptides and protein modules
    • D.J. Patel Adaptive recognition in RNA complexes with peptides and protein modules Curr Opin Struct Biol 9 1999 74 87
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 74-87
    • Patel, D.J.1
  • 45
    • 0029784592 scopus 로고    scopus 로고
    • Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex
    • J.L. Battiste, H. Mao, N.S. Rao, R. Tan, D.R. Muhandiram, L.E. Kay, and et al. Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex Science 273 1996 1547 1551
    • (1996) Science , vol.273 , pp. 1547-1551
    • Battiste, J.L.1    Mao, H.2    Rao, N.S.3    Tan, R.4    Muhandiram, D.R.5    Kay, L.E.6
  • 46
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease Biochemistry 28 1989 8972 8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 47
    • 77951582198 scopus 로고    scopus 로고
    • Structural basis of O6-alkylguanine recognition by a bacterial alkyltransferase-like DNA repair protein
    • J.M. Aramini, J.L. Tubbs, S. Kanugula, P. Rossi, A. Ertekin, M. Maglaqui, and et al. Structural basis of O6-alkylguanine recognition by a bacterial alkyltransferase-like DNA repair protein J Biol Chem 285 2010 13736 13741
    • (2010) J Biol Chem , vol.285 , pp. 13736-13741
    • Aramini, J.M.1    Tubbs, J.L.2    Kanugula, S.3    Rossi, P.4    Ertekin, A.5    Maglaqui, M.6
  • 48
    • 30444459024 scopus 로고    scopus 로고
    • Structure of the two most C-terminal RNA recognition motifs of PTB using segmental isotope labeling
    • F. Vitali, A. Henning, F.C. Oberstrass, Y. Hargous, S.D. Auweter, M. Erat, and et al. Structure of the two most C-terminal RNA recognition motifs of PTB using segmental isotope labeling EMBO J 25 2006 150 162
    • (2006) EMBO J , vol.25 , pp. 150-162
    • Vitali, F.1    Henning, A.2    Oberstrass, F.C.3    Hargous, Y.4    Auweter, S.D.5    Erat, M.6
  • 50
    • 84897939104 scopus 로고    scopus 로고
    • Solution and crystal structures of a C-terminal fragment of the neuronal isoform of the polypyrimidine tract binding protein (nPTB)
    • A. Joshi, V. Esteve, A.N. Buckroyd, M. Blatter, F.H.T. Allain, and S. Curry Solution and crystal structures of a C-terminal fragment of the neuronal isoform of the polypyrimidine tract binding protein (nPTB) PeerJ PrePrints 2 2014 e211v211
    • (2014) PeerJ PrePrints , vol.2 , pp. e211v211
    • Joshi, A.1    Esteve, V.2    Buckroyd, A.N.3    Blatter, M.4    Allain, F.H.T.5    Curry, S.6
  • 51
    • 77954384049 scopus 로고    scopus 로고
    • Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs
    • C. Dominguez, J.F. Fisette, B. Chabot, and F.H. Allain Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs Nat Struct Mol Biol 17 2010 853 861
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 853-861
    • Dominguez, C.1    Fisette, J.F.2    Chabot, B.3    Allain, F.H.4
  • 52
    • 33747085899 scopus 로고    scopus 로고
    • NMR structure of the three quasi RNA recognition motifs (qRRMs) of human hnRNP F and interaction studies with Bcl-x G-tract RNA: A novel mode of RNA recognition
    • C. Dominguez, and F.H. Allain NMR structure of the three quasi RNA recognition motifs (qRRMs) of human hnRNP F and interaction studies with Bcl-x G-tract RNA: a novel mode of RNA recognition Nucleic Acids Res 34 2006 3634 3645
    • (2006) Nucleic Acids Res , vol.34 , pp. 3634-3645
    • Dominguez, C.1    Allain, F.H.2
  • 53
    • 23144465987 scopus 로고    scopus 로고
    • SCRATCH: A protein structure and structural feature prediction server
    • J. Cheng, A.Z. Randall, M.J. Sweredoski, and P. Baldi SCRATCH: a protein structure and structural feature prediction server Nucleic Acids Res 33 2005 W72 W76
    • (2005) Nucleic Acids Res , vol.33 , pp. W72-W76
    • Cheng, J.1    Randall, A.Z.2    Sweredoski, M.J.3    Baldi, P.4
  • 54
    • 84897939104 scopus 로고    scopus 로고
    • Solution and crystal structures of a C-terminal fragment of the neuronal isoform of the polypyrimidine tract binding protein (nPTB)
    • A. Joshi, V. Esteve, A.N. Buckroyd, M. Blatter, F.H. Allain, and S. Curry Solution and crystal structures of a C-terminal fragment of the neuronal isoform of the polypyrimidine tract binding protein (nPTB) PeerJ 2 2014 e305
    • (2014) PeerJ , vol.2 , pp. e305
    • Joshi, A.1    Esteve, V.2    Buckroyd, A.N.3    Blatter, M.4    Allain, F.H.5    Curry, S.6
  • 56
    • 0028811668 scopus 로고
    • Heterogeneous nuclear ribonucleoproteins H, H′, and F are members of a ubiquitously expressed subfamily of related but distinct proteins encoded by genes mapping to different chromosomes
    • B. Honore, H.H. Rasmussen, H. Vorum, K. Dejgaard, X. Liu, P. Gromov, and et al. Heterogeneous nuclear ribonucleoproteins H, H′, and F are members of a ubiquitously expressed subfamily of related but distinct proteins encoded by genes mapping to different chromosomes J Biol Chem 270 1995 28780 28789
    • (1995) J Biol Chem , vol.270 , pp. 28780-28789
    • Honore, B.1    Rasmussen, H.H.2    Vorum, H.3    Dejgaard, K.4    Liu, X.5    Gromov, P.6
  • 57
    • 84880676352 scopus 로고    scopus 로고
    • Isolated pseudo-RNA-recognition motifs of SR proteins can regulate splicing using a noncanonical mode of RNA recognition
    • A. Clery, R. Sinha, O. Anczukow, A. Corrionero, A. Moursy, G.M. Daubner, and et al. Isolated pseudo-RNA-recognition motifs of SR proteins can regulate splicing using a noncanonical mode of RNA recognition Proc Natl Acad Sci USA 110 2013 E2802 E2811
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. E2802-E2811
    • Clery, A.1    Sinha, R.2    Anczukow, O.3    Corrionero, A.4    Moursy, A.5    Daubner, G.M.6
  • 58
    • 0032054197 scopus 로고    scopus 로고
    • Molecular genetic analysis of the heterodimeric splicing factor U2AF: The RS domain on either the large or small Drosophila subunit is dispensable in vivo
    • D.Z. Rudner, K.S. Breger, and D.C. Rio Molecular genetic analysis of the heterodimeric splicing factor U2AF: the RS domain on either the large or small Drosophila subunit is dispensable in vivo Genes Dev 12 1998 1010 1021
    • (1998) Genes Dev , vol.12 , pp. 1010-1021
    • Rudner, D.Z.1    Breger, K.S.2    Rio, D.C.3
  • 59
    • 0027753933 scopus 로고
    • Analysis of the RNA-recognition motif and RS and RGG domains: Conservation in metazoan pre-mRNA splicing factors
    • E. Birney, S. Kumar, and A.R. Krainer Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors Nucleic Acids Res 21 1993 5803 5816
    • (1993) Nucleic Acids Res , vol.21 , pp. 5803-5816
    • Birney, E.1    Kumar, S.2    Krainer, A.R.3
  • 60
    • 3042737403 scopus 로고    scopus 로고
    • U2AF homology motifs: Protein recognition in the RRM world
    • C.L. Kielkopf, S. Lucke, and M.R. Green U2AF homology motifs: protein recognition in the RRM world Genes Dev 18 2004 1513 1526
    • (2004) Genes Dev , vol.18 , pp. 1513-1526
    • Kielkopf, C.L.1    Lucke, S.2    Green, M.R.3
  • 61
    • 84874990676 scopus 로고    scopus 로고
    • XRRM: A new class of RRM found in the telomerase la family protein p65
    • M. Singh, C.P. Choi, and J. Feigon xRRM: a new class of RRM found in the telomerase La family protein p65 RNA Biol 10 2013 353 359
    • (2013) RNA Biol , vol.10 , pp. 353-359
    • Singh, M.1    Choi, C.P.2    Feigon, J.3
  • 64
    • 77953261028 scopus 로고    scopus 로고
    • Structure of the Rna15 RRM-RNA complex reveals the molecular basis of GU specificity in transcriptional 3′-end processing factors
    • C. Pancevac, D.C. Goldstone, A. Ramos, and I.A. Taylor Structure of the Rna15 RRM-RNA complex reveals the molecular basis of GU specificity in transcriptional 3′-end processing factors Nucleic Acids Res 38 2010 3119 3132
    • (2010) Nucleic Acids Res , vol.38 , pp. 3119-3132
    • Pancevac, C.1    Goldstone, D.C.2    Ramos, A.3    Taylor, I.A.4
  • 65
    • 77955273066 scopus 로고    scopus 로고
    • Novel protein-protein contacts facilitate mRNA 3′-processing signal recognition by Rna15 and Hrp1
    • T.C. Leeper, X. Qu, C. Lu, C. Moore, and G. Varani Novel protein-protein contacts facilitate mRNA 3′-processing signal recognition by Rna15 and Hrp1 J Mol Biol 401 2010 334 349
    • (2010) J Mol Biol , vol.401 , pp. 334-349
    • Leeper, T.C.1    Qu, X.2    Lu, C.3    Moore, C.4    Varani, G.5
  • 66
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • C. Choudhary, C. Kumar, F. Gnad, M.L. Nielsen, M. Rehman, T.C. Walther, and et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions Science 325 2009 834 840
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6
  • 70
    • 84941935879 scopus 로고    scopus 로고
    • University of California, San Francisco
    • Goddard TD, Kneller DG. University of California, San Francisco; 2007.
    • (2007)
    • Goddard, T.D.1    Kneller, D.G.2
  • 71
    • 68349093958 scopus 로고    scopus 로고
    • TALOS +: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Y. Shen, F. Delaglio, G. Cornilescu, and A. Bax TALOS +: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts J Biomol NMR 44 2009 213 223
    • (2009) J Biomol NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 72
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • T. Herrmann, P. Guntert, and K. Wuthrich Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS J Biomol NMR 24 2002 171 189
    • (2002) J Biomol NMR , vol.24 , pp. 171-189
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 73
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • T. Herrmann, P. Guntert, and K. Wuthrich Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA J Mol Biol 319 2002 209 227
    • (2002) J Mol Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 74
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • P. Guntert Automated NMR structure calculation with CYANA Methods Mol Biol 278 2004 353 378
    • (2004) Methods Mol Biol , vol.278 , pp. 353-378
    • Guntert, P.1
  • 75
    • 0029633186 scopus 로고
    • AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
    • D.A. Pearlman, D.A. Case, J.W. Caldwell, W.S. Ross, T.E. Cheatham Iii, S. DeBolt, and et al. AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules Comput Phys Commun 91 1995 1 41
    • (1995) Comput Phys Commun , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatham, T.E.5    DeBolt, S.6
  • 76
    • 77953513118 scopus 로고    scopus 로고
    • Improved side-chain torsion potentials for the AMBER ff99SB protein force field
    • K. Lindorff-Larsen, S. Piana, K. Palmo, P. Maragakis, J.L. Klepeis, R.O. Dror, and et al. Improved side-chain torsion potentials for the AMBER ff99SB protein force field Proteins 78 2010 1950 1958
    • (2010) Proteins , vol.78 , pp. 1950-1958
    • Lindorff-Larsen, K.1    Piana, S.2    Palmo, K.3    Maragakis, P.4    Klepeis, J.L.5    Dror, R.O.6
  • 77
    • 0033654297 scopus 로고    scopus 로고
    • Generalized born models of macromolecular solvation effects
    • D. Bashford, and D.A. Case Generalized born models of macromolecular solvation effects Annu Rev Phys Chem 51 2000 129 152
    • (2000) Annu Rev Phys Chem , vol.51 , pp. 129-152
    • Bashford, D.1    Case, D.A.2
  • 78
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald: an N·log(N) method for Ewald sums in large systems J Chem Phys 98 1993 10089 10092
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 79
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • J.-P. Ryckaert, G. Ciccotti, and H.J.C. Berendsen Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes J Comput Phys 23 1977 327 341
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 82
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PDBViewer: An environment for comparative protein modeling
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PDBViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 84
    • 84856489442 scopus 로고    scopus 로고
    • HHblits: Lightning-fast iterative protein sequence searching by HMM-HMM alignment
    • M. Remmert, A. Biegert, A. Hauser, and J. Soding HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment Nat Methods 9 2012 173 175
    • (2012) Nat Methods , vol.9 , pp. 173-175
    • Remmert, M.1    Biegert, A.2    Hauser, A.3    Soding, J.4
  • 85
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • J. Soding Protein homology detection by HMM-HMM comparison Bioinformatics 21 2005 951 960
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Soding, J.1
  • 86
    • 0043123216 scopus 로고    scopus 로고
    • GeneSilico protein structure prediction meta-server
    • M.A. Kurowski, and J.M. Bujnicki GeneSilico protein structure prediction meta-server Nucleic Acids Res 31 2003 3305 3307
    • (2003) Nucleic Acids Res , vol.31 , pp. 3305-3307
    • Kurowski, M.A.1    Bujnicki, J.M.2
  • 87
    • 10044222704 scopus 로고    scopus 로고
    • CLANS: A Java application for visualizing protein families based on pairwise similarity
    • T. Frickey, and A. Lupas CLANS: a Java application for visualizing protein families based on pairwise similarity Bioinformatics 20 2004 3702 3704
    • (2004) Bioinformatics , vol.20 , pp. 3702-3704
    • Frickey, T.1    Lupas, A.2


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