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1
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0031944706
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RNA-mediated signaling in transcription
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An extremely well written 'News and Views' article describing the origin of the biological specificity associated with aspects of phage transcriptional antitermination that emerged following the publication of the solution structures of P22 and λ N peptide-boxB RNA complexes. This article highlighted the concept of RNA bipartite recognition, whereby peptide binding to one face of the RNA resulted in a conformational change that positioned the opposite face for recognition by other components of the ribonucleoprotein complex.
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Weiss MA RNA-mediated signaling in transcription. Nat Struct Biol. 5:1998;329-333. An extremely well written 'News and Views' article describing the origin of the biological specificity associated with aspects of phage transcriptional antitermination that emerged following the publication of the solution structures of P22 and λ N peptide-boxB RNA complexes. This article highlighted the concept of RNA bipartite recognition, whereby peptide binding to one face of the RNA resulted in a conformational change that positioned the opposite face for recognition by other components of the ribonucleoprotein complex.
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Nat Struct Biol
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Weiss, M.A.1
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2
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0031568305
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Role REVersal: Understanding how RRE RNA binds its peptide ligand
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An exceptional 'News and Views' article outlining the novel principles and patterns associated with peptide-RNA recognition, based on an insightful analysis of the published solution structures of complexes between the HIV-1 Rev peptide and its wildtype RRE RNA and RNA aptamer target sites. This article put forward the concept of recognition by the RNA tertiary structure of minimalist elements of protein secondary structure.
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Grate D, Wilson C Role REVersal: understanding how RRE RNA binds its peptide ligand. Structure. 5:1997;7-11. An exceptional 'News and Views' article outlining the novel principles and patterns associated with peptide-RNA recognition, based on an insightful analysis of the published solution structures of complexes between the HIV-1 Rev peptide and its wildtype RRE RNA and RNA aptamer target sites. This article put forward the concept of recognition by the RNA tertiary structure of minimalist elements of protein secondary structure.
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Structure
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Grate, D.1
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New features in RNA recognition: A Tat-TAR complex
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0032559232
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Induced folding in RNA-protein recognition: More than a simple handshake
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A minireview addressing issues related to the induced folding pathways in protein-RNA recognition and the contribution of the flexibility that is associated with unfolded and partly folded proteins in the RNA recognition process.
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Frankel AD, Smith CA Induced folding in RNA-protein recognition: more than a simple handshake. Cell. 92:1998;149-151. A minireview addressing issues related to the induced folding pathways in protein-RNA recognition and the contribution of the flexibility that is associated with unfolded and partly folded proteins in the RNA recognition process.
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Frankel, A.D.1
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A minireview outlining recent combinatorial library-based selection approaches for the identification and characterization of novel RNA-binding proteins with customized specificities.
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Laird-Offringa IA, Belasco JG RNA-binding proteins tamed. Nat Struct Biol. 5:1998;665-668. A minireview outlining recent combinatorial library-based selection approaches for the identification and characterization of novel RNA-binding proteins with customized specificities.
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Laird-Offringa, I.A.1
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Frankel AD Using peptides to study RNA-protein recognition. Nagai K, Mattaj IW RNA-Protein Interactions. 1994;221-247 IRL Press, New York.
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Frankel, A.D.1
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K. Nagai, & I.W. Mattaj. New York: IRL Press
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Karn J, Gait MJ, Churcher MJ, Mann DA, Mikaelian I, Pritchard C Control of HIV gene expression by RNA-binding proteins Tat and Rev. Nagai K, Mattaj IW RNA-Protein Interactions. 1994;193-220 IRL Press, New York.
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Karn, J.1
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11
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Puglisi JD, Tan R, Calnan BJ, Frankel AD, Williamson JR Conformation of the Tar RNA-arginine complex by NMR spectroscopy. Science. 257:1992;76-80.
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Puglisi, J.D.1
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Williamson, J.R.5
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12
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0029852357
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Structure of HIV-1 TAR RNA in the absence of ligands reveals a novel conformation of the trinucleotide bulge
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Aboud-ela F, Karn J, Varani G Structure of HIV-1 TAR RNA in the absence of ligands reveals a novel conformation of the trinucleotide bulge. Nucleic Acids Res. 24:1996;3974-3981.
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13
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0032543957
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A 1.3 Å resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation
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An important paper that defines the conformation of the divalent-cation-coordinated three base bulge in the structure of the free HIV-1 TAR RNA in the crystalline state. It established that all three bulge bases loop out of the helix, with concomitant stacking of adjacent junctional base pairs. This study contrasts with the conclusions of earlier solution structural studies on the same system in the absence of divalent cations.
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Ippolito JA, Steitz TA A 1.3 Å resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation. Proc Natl Acad Sci USA. 95:1998;9819-9824. An important paper that defines the conformation of the divalent-cation-coordinated three base bulge in the structure of the free HIV-1 TAR RNA in the crystalline state. It established that all three bulge bases loop out of the helix, with concomitant stacking of adjacent junctional base pairs. This study contrasts with the conclusions of earlier solution structural studies on the same system in the absence of divalent cations.
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Proc Natl Acad Sci USA
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Ippolito, J.A.1
Steitz, T.A.2
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0028864394
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The structure of the human immunodeficiency virus type-1 TAR RNA reveals principles of RNA recognition by Tat protein
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Aboud-ela F, Karn J, Varani G The structure of the human immunodeficiency virus type-1 TAR RNA reveals principles of RNA recognition by Tat protein. J Mol Biol. 253:1995;313-332.
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16
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0030935060
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Dissection of the proposed base triple in human immunodeficiency virus TAR RNA indicates the importance of Hoogsteen interaction
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Tao J, Chen L, Frankel AD Dissection of the proposed base triple in human immunodeficiency virus TAR RNA indicates the importance of Hoogsteen interaction. Biochemistry. 36:1997;3491-3495.
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Tao, J.1
Chen, L.2
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17
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0031552350
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Solution structure of the HIV-2 TAR- argininamide complex
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A noteworthy contribution defining the solution structure of L-argininamide bound to HIV-2 TAR RNA. This paper clarifies issues related to the proposed 'arginine fork' alignment architecture, in which the guanidinium group of an arginine can potentially hydrogen bond simultaneously to a base-pair edge and backbone phosphate(s).
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Brodsky AS, Williamson JR Solution structure of the HIV-2 TAR- argininamide complex. J Mol Biol. 267:1997;624-639. A noteworthy contribution defining the solution structure of L-argininamide bound to HIV-2 TAR RNA. This paper clarifies issues related to the proposed 'arginine fork' alignment architecture, in which the guanidinium group of an arginine can potentially hydrogen bond simultaneously to a base-pair edge and backbone phosphate(s).
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J Mol Biol
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Brodsky, A.S.1
Williamson, J.R.2
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18
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Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex
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Puglisi JD, Chen L, Blanchard S, Frankel AD Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex. Science. 270:1995;1200-1203.
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Science
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Puglisi, J.D.1
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Ye X, Kumar RA, Patel DJ Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex. Chem Biol. 2:1995;827-840.
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Chen L, Frankel AD An RNA-binding peptide from bovine immunodeficiency virus Tat protein recognizes an unusual RNA structure. Biochemistry. 33:1994;2708-2715.
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A peptide interaction in the major groove of RNA resembles protein interactions in the minor groove of RNA
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Chen L, Frankel AD A peptide interaction in the major groove of RNA resembles protein interactions in the minor groove of RNA. Proc Natl Acad Sci USA. 92:1995;5077-5081.
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Selective optimization of the Rev-binding element of HIV-1
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Giver L, Bartel D, Zapp M, Pawul A, Green M, Ellington AD Selective optimization of the Rev-binding element of HIV-1. Nucleic Acids Res. 23:1993;5509-5516.
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Giver, L.1
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24
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0029784592
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α Helix-RNA major groove recognition in an HIV-1 Rev peptide-RRE RNA complex
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Battiste JL, Mao H, Rao NS, Tan R, Muhandiram DR, Kay LE, Frankel AD, Williamson JR α Helix-RNA major groove recognition in an HIV-1 Rev peptide-RRE RNA complex. Science. 273:1996;1547-1551.
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Science
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Battiste, J.L.1
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Muhandiram, D.R.5
Kay, L.E.6
Frankel, A.D.7
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25
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0030475417
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Deep penetration of an α-helix into a widened RNA major groove in the HIV-1 Rev peptide-RNA aptamer complex
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Ye X, Gorin A, Ellington A, Patel DJ Deep penetration of an α-helix into a widened RNA major groove in the HIV-1 Rev peptide-RNA aptamer complex. Nat Struct Biol. 3:1996;1026-1033.
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Nat Struct Biol
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Ye, X.1
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0030272096
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A structural model for the HIV-1 Rev-RRE complex deduced from altered-specificity Rev variants isolated by a rapid genetic strategy
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Jain C, Belasco JE A structural model for the HIV-1 Rev-RRE complex deduced from altered-specificity Rev variants isolated by a rapid genetic strategy. Cell. 87:1996;115-125.
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Co-stabilization of peptide and RNA structure in an HIV Rev peptide-RRE complex
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Tan R, Frankel AD Co-stabilization of peptide and RNA structure in an HIV Rev peptide-RRE complex. Biochemistry. 33:1994;14579-14585.
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Das A Control of transcription termination by RNA-binding proteins. Annu Rev Biochem. 62:1993;893-930.
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Friedman DI, Court DL Transcription antitermination: the λ paradigm updated. Mol Microbiol. 18:1995;191-200.
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Assembly of the N-dependent antitermination complex of phage λ: NusA and RNA bind independently to different unfolded domains of the N protein
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This paper conclusively established that boxB RNA and the elongation factor NusA bind independently to different unfolded segments of the N protein. This result requires that the unstructured N protein fold in a modular manner on complex formation with its binding partners in order to form the active ribonucleoprotein antitermination complex.
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van Gilst MR, von Hippel PH Assembly of the N-dependent antitermination complex of phage λ: NusA and RNA bind independently to different unfolded domains of the N protein. J Mol Biol. 274:1997;160-173. This paper conclusively established that boxB RNA and the elongation factor NusA bind independently to different unfolded segments of the N protein. This result requires that the unstructured N protein fold in a modular manner on complex formation with its binding partners in order to form the active ribonucleoprotein antitermination complex.
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J Mol Biol
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Van Gilst, M.R.1
Von Hippel, P.H.2
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Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage λ N protein
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An independent characterization of the modular folding of the unstructured N protein with components of the transcription antitermination apparatus. The paper also reports on the identification of the domains of the N protein that are involved in boxB RNA, NusA and RNA polymerase recognition.
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Mogridge J, Legault P, Li J, van Oene MD, Kay LE, Greenblatt J Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage λ N protein. Mol Cell. 1:1998;265-275. An independent characterization of the modular folding of the unstructured N protein with components of the transcription antitermination apparatus. The paper also reports on the identification of the domains of the N protein that are involved in boxB RNA, NusA and RNA polymerase recognition.
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Mol Cell
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Mogridge, J.1
Legault, P.2
Li, J.3
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Kay, L.E.5
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33
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0031916834
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Solution structure of P22 transcriptional antitermination N-peptide-boxB RNA complex
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2 and one εNH guanidinium protons of Arg6 and intermolecular NOEs with RNA protons in the binding pocket. The adopted GNRA fold in the complex was achieved by looping out the third residue (a cytosine) of the pentaloop sequence.
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2 and one εNH guanidinium protons of Arg6 and intermolecular NOEs with RNA protons in the binding pocket. The adopted GNRA fold in the complex was achieved by looping out the third residue (a cytosine) of the pentaloop sequence.
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Nat Struct Biol
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Cai, Z.1
Gorin, A.2
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Patel, D.J.8
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34
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0032540286
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NMR structure of the bacteriophage λ N peptide/boxB RNA complex: Recognition of a GNRA fold by an arginine-rich motif
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••] reached similar conclusions regarding the conformation and intermolecular contacts of the bent α-helical peptides and their GNRA-fold-aligned stem-loop RNA targets. The adopted GNRA fold in this complex was achieved by looping out the fourth residue (a guanine) of the pentaloop sequence. The complex was stabilized by the stacking of a tryptophan residue located towards the C terminus of the N peptide with a loop adenine, resulting in the extension of the purine stack within the GNRA fold.
-
••] reached similar conclusions regarding the conformation and intermolecular contacts of the bent α-helical peptides and their GNRA-fold-aligned stem-loop RNA targets. The adopted GNRA fold in this complex was achieved by looping out the fourth residue (a guanine) of the pentaloop sequence. The complex was stabilized by the stacking of a tryptophan residue located towards the C terminus of the N peptide with a loop adenine, resulting in the extension of the purine stack within the GNRA fold.
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Cell
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Legault, P.1
Li, J.2
Mogridge, J.3
Kay, L.E.4
Greenblatt, J.5
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0030931149
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An RNA enhancer in a phage transcriptional antitermination complex functions as a structural switch
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Su, L.1
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0024394611
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Effects of all single base substitutions in the loop of boxB on antitermination of transcription by bacteriophage lambda's N protein
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Doelling JH, Franklin NC Effects of all single base substitutions in the loop of boxB on antitermination of transcription by bacteriophage lambda's N protein. Nucleic Acids Res. 17:1989;5565-5577.
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Clustered arginine residues of bacteriophage λ N protein are essential to antitermination of transcription, but their locale cannot compensate for boxB loop defects
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Franklin NC Clustered arginine residues of bacteriophage λ N protein are essential to antitermination of transcription, but their locale cannot compensate for boxB loop defects. J Mol Biol. 231:1993;343-360.
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J Mol Biol
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Franklin, N.C.1
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0031024660
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Analysis of bacteriophage N protein and peptide binding to boxB RNA using polyacrylamide gel coelectrophoresis (PACE)
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Cilley CD, Williamson JR Analysis of bacteriophage N protein and peptide binding to boxB RNA using polyacrylamide gel coelectrophoresis (PACE). RNA. 3:1997;57-67.
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RNA
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Cilley, C.D.1
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Major groove accessibility of RNA
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Weeks KM, Crothers DM Major groove accessibility of RNA. Science. 261:1993;1574-1577.
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Science
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Weeks, K.M.1
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0027251792
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RNA recognition by an isolated α-helix
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Tan R, Chen L, Buettner JA, Hudson D, Frankel AD RNA recognition by an isolated α-helix. Cell. 73:1993;1031-1040.
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Cell
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42
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Arginine-mediated RNA recognition: The arginine fork
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Calnan BJ, Tidor B, Biancalana S, Hudson D, Frankel AD Arginine-mediated RNA recognition: the arginine fork. Science. 252:1991;1167-1171.
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Science
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Calnan, B.J.1
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Frankel, A.D.5
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43
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0032575334
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Altering the context of an RNA bulge switches the binding specificities of two viral Tat proteins
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An interesting paper describing the design of a novel TAR RNA sequence that is recognized by both BIV and HIV-1 Tat. The study highlights the contributions of segments flanking the binding site for the arginine-rich peptide in the discriminative recognition between BIV and HIV-1 TAR RNA.
-
Smith CA, Crotty S, Harada Y, Frankel AD Altering the context of an RNA bulge switches the binding specificities of two viral Tat proteins. Biochemistry. 37:1998;10808-10814. An interesting paper describing the design of a novel TAR RNA sequence that is recognized by both BIV and HIV-1 Tat. The study highlights the contributions of segments flanking the binding site for the arginine-rich peptide in the discriminative recognition between BIV and HIV-1 TAR RNA.
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(1998)
Biochemistry
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Smith, C.A.1
Crotty, S.2
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Selection of RNA-binding peptides in vivo
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Harada K, Martin SS, Frankel AD Selection of RNA-binding peptides in vivo. Nature. 380:1996;175-179.
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Nature
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Harada, K.1
Martin, S.S.2
Frankel, A.D.3
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45
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0030726778
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Molding of a peptide into an RNA site by in vivo peptide evolution
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A peptide-based combinatorial library and subsequent codon-based mutagenesis approach for the identification of evolved arginine-rich peptides that target the HIV-1 RRE RNA with high affinity and specificity. The current peptide library was restricted to hydrophilic and charged amino acids. This approach establishes a protocol for the evolution of novel peptide folds within the context of a defined RNA binding pocket.
-
Harada K, Martin SS, Tan R, Frankel AD Molding of a peptide into an RNA site by in vivo peptide evolution. Proc Natl Acad Sci USA. 94:1997;11887-11892. A peptide-based combinatorial library and subsequent codon-based mutagenesis approach for the identification of evolved arginine-rich peptides that target the HIV-1 RRE RNA with high affinity and specificity. The current peptide library was restricted to hydrophilic and charged amino acids. This approach establishes a protocol for the evolution of novel peptide folds within the context of a defined RNA binding pocket.
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(1997)
Proc Natl Acad Sci USA
, vol.94
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Harada, K.1
Martin, S.S.2
Tan, R.3
Frankel, A.D.4
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46
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0030761265
-
Subtle atomic group discrimination in the RNA minor groove
-
An important paper describing an RNA-directed phage display library approach for identifying peptide folds that can discriminate between a G•U mismatch and other pairing alignments within a helical RNA stem segment. This approach is based on the spatial and angular discriminative recognition of pairing alignments within the minor groove of the RNA helix.
-
Frugier M, Schimmel P Subtle atomic group discrimination in the RNA minor groove. Proc Natl Acad Sci USA. 94:1997;11291-11294. An important paper describing an RNA-directed phage display library approach for identifying peptide folds that can discriminate between a G•U mismatch and other pairing alignments within a helical RNA stem segment. This approach is based on the spatial and angular discriminative recognition of pairing alignments within the minor groove of the RNA helix.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 11291-11294
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-
Frugier, M.1
Schimmel, P.2
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48
-
-
0032511140
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Dynamic behaviour of the HIV-1 nucleocapsid protein
-
An interesting paper that addresses issues related to the relative alignment of individual zinc fingers in the solution conformation of the free HIV-1 nucleocapsid protein. The paper concludes that the free protein is in dynamic equilibrium between multiple conformational states associated with noninteracting and weakly interacting alignments between zinc finger modules.
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Lee BM, de Guzman RN, Turner BG, Tjandra N, Summers MF Dynamic behaviour of the HIV-1 nucleocapsid protein. J Mol Biol. 279:1998;633-649. An interesting paper that addresses issues related to the relative alignment of individual zinc fingers in the solution conformation of the free HIV-1 nucleocapsid protein. The paper concludes that the free protein is in dynamic equilibrium between multiple conformational states associated with noninteracting and weakly interacting alignments between zinc finger modules.
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(1998)
J Mol Biol
, vol.279
, pp. 633-649
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Lee, B.M.1
De Guzman, R.N.2
Turner, B.G.3
Tjandra, N.4
Summers, M.F.5
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49
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0031820966
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Specific RNA binding proteins constructed from zinc fingers
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An in vitro based selection approach was used to identify novel RNA-binding proteins generated from a tandem zinc finger based combinatorial library containing degenerate α helices. The resulting phage displayed selected tandem zinc fingers bound their 5S rRNA and the HIV-1 Rev RRE RNA targets with nanomolar affinity.
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Friesen WJ, Darby MK Specific RNA binding proteins constructed from zinc fingers. Nat Struct Biol. 5:1998;543-546. An in vitro based selection approach was used to identify novel RNA-binding proteins generated from a tandem zinc finger based combinatorial library containing degenerate α helices. The resulting phage displayed selected tandem zinc fingers bound their 5S rRNA and the HIV-1 Rev RRE RNA targets with nanomolar affinity.
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(1998)
Nat Struct Biol
, vol.5
, pp. 543-546
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Friesen, W.J.1
Darby, M.K.2
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50
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0031213649
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The three dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions
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Valegard K, Murray JB, Stonehouse NJ, van den Worm S, Stockley PG, Liljas L The three dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions. J Mol Biol. 270:1997;724-738.
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(1997)
J Mol Biol
, vol.270
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Valegard, K.1
Murray, J.B.2
Stonehouse, N.J.3
Van Den Worm, S.4
Stockley, P.G.5
Liljas, L.6
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51
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0031951789
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Crystal structure of an RNA aptamer-protein complex at 2.8 Å resolution
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This structure of the MS2 coat protein AB dimer bound to an RNA aptamer and an earlier structure of the complex with wildtype RNA [50] establish a critical role in molecular recognition for the orientation and spatial separation of key specificity-determining adenines positioned in the hairpin loop and bulge of the bound RNAs. These structures reinforce the adaptability of RNA folds to mesh with a fixed protein binding architecture.
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Convery MA, Rowsell S, Stonehouse NJ, Ellington AD, Hirao I, Murray JB, Peabody DS, Phillips SE, Stockley PG Crystal structure of an RNA aptamer-protein complex at 2.8 Å resolution. Nat Struct Biol. 5:1998;133-139. This structure of the MS2 coat protein AB dimer bound to an RNA aptamer and an earlier structure of the complex with wildtype RNA [50] establish a critical role in molecular recognition for the orientation and spatial separation of key specificity-determining adenines positioned in the hairpin loop and bulge of the bound RNAs. These structures reinforce the adaptability of RNA folds to mesh with a fixed protein binding architecture.
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(1998)
Nat Struct Biol
, vol.5
, pp. 133-139
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Convery, M.A.1
Rowsell, S.2
Stonehouse, N.J.3
Ellington, A.D.4
Hirao, I.5
Murray, J.B.6
Peabody, D.S.7
Phillips, S.E.8
Stockley, P.G.9
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52
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0031788059
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Crystal structures of a series of RNA aptamers complexed to the same protein target
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••] to include additional MS2 coat protein-RNA aptamer complexes. These new RNA aptamers, one of which is missing a key bulged adenine, still bind the MS2 coat protein dimer through adaptive transitions in a manner that is similar to the wildtype RNA complex. The robustness of the MS2 coat protein-RNA stem-loop system and its ready crystallizability suggest that it could serve as a scaffold for linking nucleic acid motifs in need of structural characterization.
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••] to include additional MS2 coat protein-RNA aptamer complexes. These new RNA aptamers, one of which is missing a key bulged adenine, still bind the MS2 coat protein dimer through adaptive transitions in a manner that is similar to the wildtype RNA complex. The robustness of the MS2 coat protein-RNA stem-loop system and its ready crystallizability suggest that it could serve as a scaffold for linking nucleic acid motifs in need of structural characterization.
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(1998)
Nat Struct Biol
, vol.5
, pp. 970-975
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Rowsell, S.1
Stonehouse, N.J.2
Convery, M.A.3
Adams, C.J.4
Ellington, A.D.5
Hirao, I.6
Peabody, D.S.7
Phillips, S.E.8
Stockley, P.G.9
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53
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0024392753
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Structure of E. coli glutaminyl tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 Å resolution
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Rould MA, Perona JJ, Soll D, Steitz TA Structure of E. coli glutaminyl tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 Å resolution. Science. 246:1989;1135-1142.
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Science
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Rould, M.A.1
Perona, J.J.2
Soll, D.3
Steitz, T.A.4
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55
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0028004607
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Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
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Oubridge C, Ito N, Evans PR, Teo CH, Nagai K Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature. 372:1994;432-438.
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(1994)
Nature
, vol.372
, pp. 432-438
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Oubridge, C.1
Ito, N.2
Evans, P.R.3
Teo, C.H.4
Nagai, K.5
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56
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0029920331
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Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation
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Allain FH, Gubser CC, Howe PW, Nagai K, Neuhaus D, Varani G Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation. Nature. 380:1996;646-650.
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(1996)
Nature
, vol.380
, pp. 646-650
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Allain, F.H.1
Gubser, C.C.2
Howe, P.W.3
Nagai, K.4
Neuhaus, D.5
Varani, G.6
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57
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0031561062
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HIV-1 TAR RNA recognition by an unnatural biopolymer
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A novel approach describing the preparation of oligocarbamate-based Tat peptides for targeting HIV-1 TAR RNA. The oligocarbamate backbone differs from its peptide counterpart in terms of its lipophilicity, flexibility and hydrogen-bonding potential.
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Wang X, Huq I, Rana TM HIV-1 TAR RNA recognition by an unnatural biopolymer. J Am Chem Soc. 119:1997;6444-6445. A novel approach describing the preparation of oligocarbamate-based Tat peptides for targeting HIV-1 TAR RNA. The oligocarbamate backbone differs from its peptide counterpart in terms of its lipophilicity, flexibility and hydrogen-bonding potential.
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(1997)
J Am Chem Soc
, vol.119
, pp. 6444-6445
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Wang, X.1
Huq, I.2
Rana, T.M.3
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58
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0031280039
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Specific recognition of HIV-1 TAR RNA by a D-Tat peptide
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Protease sensitivity has limited the therapeutic potential of Tat peptides in blocking the HIV-1 Tat protein-TAR RNA interaction. This paper describes the synthesis of Tat peptides based on D-amino acids that are able to site-specifically target HIV-1 TAR RNA.
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Huq I, Wang X, Rana TM Specific recognition of HIV-1 TAR RNA by a D-Tat peptide. Nat Struct Biol. 4:1997;881-882. Protease sensitivity has limited the therapeutic potential of Tat peptides in blocking the HIV-1 Tat protein-TAR RNA interaction. This paper describes the synthesis of Tat peptides based on D-amino acids that are able to site-specifically target HIV-1 TAR RNA.
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(1997)
Nat Struct Biol
, vol.4
, pp. 881-882
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Huq, I.1
Wang, X.2
Rana, T.M.3
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59
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0030976612
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An inhibitor of Tat-TAR RNA interaction that effectively suppresses HIV-1 replication
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A pioneering paper describing a combinatorial approach for selecting a mixed peptoid (N-substituted glycines) and D-peptide-based nine residue oligomer that can target the HIV-1 TAR RNA binding site under in vitro and in vivo conditions.
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Hamy F, Felder ER, Heizmann G, Lazdins J, Aboul-ela F, Varani G, Karn J, Klimkait T An inhibitor of Tat-TAR RNA interaction that effectively suppresses HIV-1 replication. Proc Natl Acad Sci USA. 94:1997;3548-3553. A pioneering paper describing a combinatorial approach for selecting a mixed peptoid (N-substituted glycines) and D-peptide-based nine residue oligomer that can target the HIV-1 TAR RNA binding site under in vitro and in vivo conditions.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 3548-3553
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Hamy, F.1
Felder, E.R.2
Heizmann, G.3
Lazdins, J.4
Aboul-Ela, F.5
Varani, G.6
Karn, J.7
Klimkait, T.8
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