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U2AF homology motifs: protein recognition in the RRM world

Genes & development, 2004-07, Vol.18 (13), p.1513-1526

2004

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Structural Basis for Polypyrimidine Tract Recognition by the Essential Pre-mRNA Splicing Factor U2AF65

Molecular cell, 2006-07, Vol.23 (1), p.49-59

2006

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Structure-guided U2AF⁶⁵ variant improves recognition and splicing of a defective pre-mRNA

Proceedings of the National Academy of Sciences - PNAS, 2014-12, Vol.111 (49), p.17420-17425

2014

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Different Requirements of the Kinase and UHM Domains of KIS for Its Nuclear Localization and Binding to Splicing Factors

Journal of molecular biology, 2008-09, Vol.381 (3), p.748-762

2008

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An extended U2AF(65)-RNA-binding domain recognizes the 3' splice site signal

Nature communications, 2016-03, Vol.7, p.10950-10950

2016

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Structure of Phosphorylated SF1 Bound to U2AF65 in an Essential Splicing Factor Complex

Structure (London), 2013-02, Vol.21 (2), p.197-208

2013

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Solution Conformation and Thermodynamic Characteristics of RNA Binding by the Splicing Factor U2AF65

The Journal of biological chemistry, 2008-11, Vol.283 (48), p.33641-33649

2008

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A Broad range of conformations contribute to the solution ensemble of the essential splicing factor U2AF(65)

Biochemistry (Easton), 2012-07, Vol.51 (26), p.5223-5225

2012

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U2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs

Nucleic acids research, 2013-04, Vol.41 (6), p.3859-3873

2013

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RNA Induces Conformational Changes in the SF1/U2AF⁶⁵ Splicing Factor Complex

Journal of molecular biology, 2011-02, Vol.405 (5), p.1128-1138

2011

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Multiple U2AF65 binding sites within SF3b155: thermodynamic and spectroscopic characterization of protein-protein interactions among pre-mRNA splicing factors

Journal of molecular biology, 2006-02, Vol.356 (3), p.664-683

2006

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Alternative conformations at the RNA-binding surface of the N-terminal U2AF(65) RNA recognition motif

Journal of molecular biology, 2007-02, Vol.366 (3), p.703-710

2007

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U2AF1 mutations alter sequence specificity of pre-mRNA binding and splicing

Leukemia, 2015-04, Vol.29 (4), p.909-917

2015

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Major phosphorylation of SF1 on adjacent Ser‐Pro motifs enhances interaction with U2AF65

The FEBS journal, 2006-02, Vol.273 (3), p.577-587

2006

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Crystallization and preliminary X-ray analysis of a U2AF65 variant in complex with a polypyrimidine-tract analogue by use of protein engineering

Acta crystallographica. Section F, Structural biology and crystallization communications, 2006-05, Vol.62 (5), p.457-459

2006

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U2AF homology motifs: protein recognition in the RRM world

Structural Basis for Polypyrimidine Tract Recognition by the Essential Pre-mRNA Splicing Factor U2AF65

Structure-guided U2AF⁶⁵ variant improves recognition and splicing of a defective pre-mRNA

Different Requirements of the Kinase and UHM Domains of KIS for Its Nuclear Localization and Binding to Splicing Factors

An extended U2AF(65)-RNA-binding domain recognizes the 3' splice site signal

Structure of Phosphorylated SF1 Bound to U2AF65 in an Essential Splicing Factor Complex

Solution Conformation and Thermodynamic Characteristics of RNA Binding by the Splicing Factor U2AF65

A Broad range of conformations contribute to the solution ensemble of the essential splicing factor U2AF(65)

U2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs

RNA Induces Conformational Changes in the SF1/U2AF⁶⁵ Splicing Factor Complex

Multiple U2AF65 binding sites within SF3b155: thermodynamic and spectroscopic characterization of protein-protein interactions among pre-mRNA splicing factors

Alternative conformations at the RNA-binding surface of the N-terminal U2AF(65) RNA recognition motif

U2AF1 mutations alter sequence specificity of pre-mRNA binding and splicing

Major phosphorylation of SF1 on adjacent Ser‐Pro motifs enhances interaction with U2AF65

Crystallization and preliminary X-ray analysis of a U2AF65 variant in complex with a polypyrimidine-tract analogue by use of protein engineering

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