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U2AF homology motifs: protein recognition in the RRM worldAn extended U2AF(65)-RNA-binding domain recognizes the 3' splice site signalStructural effects of DNA sequence on T.A recognition by hydroxypyrrole/pyrrole pairs in the minor grooveConformational flexibility of B-DNA at 0.74 A resolution: d(CCAGTACTGG)(2)X-ray structures of threonine aldolase complexes: structural basis of substrate recognitionAlternative Conformations at the RNA-binding Surface of the N-terminal U2AF65 RNA Recognition MotifStructure of a DNA Repair Substrate Containing an Alkyl Interstrand Cross-Link at 1.65 Å Resolution † , ‡Structure of the central RNA recognition motif of human TIA-1 at 1.95Å resolutionX-ray Structures of U2 snRNA−Branchpoint Duplexes Containing Conserved Pseudouridines † ‡Structural basis for NADH/NAD+ redox sensing by a Rex family repressorStructure of Phosphorylated SF1 Bound to U2AF65 in an Essential Splicing Factor ComplexU2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs.Staufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRNA decayCancer-relevant Splicing Factor CAPERα Engages the Essential Splicing Factor SF3b155 in a Specific Ternary ComplexStructural basis for G.C recognition in the DNA minor grooveRNA induces conformational changes in the SF1/U2AF65 splicing factor complexLarge favorable enthalpy changes drive specific RNA recognition by RNA recognition motif proteinsStructure-guided U2AF65 variant improves recognition and splicing of a defective pre-mRNA.Purification, crystallization and preliminary X-ray crystallographic analysis of a central domain of human splicing factor 1.U2AF1 mutations alter sequence specificity of pre-mRNA binding and splicingThree RNA recognition motifs participate in RNA recognition and structural organization by the pro-apoptotic factor TIA-1.Major phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65.Multiple U2AF65 binding sites within SF3b155: thermodynamic and spectroscopic characterization of protein-protein interactions among pre-mRNA splicing factors.Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65.Wild-Type U2AF1 Antagonizes the Splicing Program Characteristic of U2AF1-Mutant Tumors and Is Required for Cell Survival.A Broad range of conformations contribute to the solution ensemble of the essential splicing factor U2AF(65).Crystallization and preliminary X-ray analysis of a U2AF65 variant in complex with a polypyrimidine-tract analogue by use of protein engineeringDividing and Conquering the Family of RNA Recognition Motifs: A Representative Case Based on hnRNP L.Solution conformation and thermodynamic characteristics of RNA binding by the splicing factor U2AF65Different requirements of the kinase and UHM domains of KIS for its nuclear localization and binding to splicing factors.SF1 Phosphorylation Enhances Specific Binding to U2AF65 and Reduces Binding to 3'-Splice-Site RNA.Unmasking the U2AF homology motif family: a bona fide protein-protein interaction motif in disguise.Splicing Factor Mutations in Myelodysplasias: Insights from Spliceosome Structures.X-ray structure of a Rex-family repressor/NADH complex insights into the mechanism of redox sensing.Cancer-Associated Mutations Mapped on High-Resolution Structures of the U2AF2 RNA Recognition Motifs.Insights from structures of cancer-relevant pre-mRNA splicing factors.The pre-mRNA splicing and transcription factor Tat-SF1 is a functional partner of the spliceosome SF3b1 subunit via a U2AF homology motif interface
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description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Clara L Kielkopf
@ast
Clara L Kielkopf
@en
Clara L Kielkopf
@es
Clara L Kielkopf
@nl
Clara L Kielkopf
@sl
type
label
Clara L Kielkopf
@ast
Clara L Kielkopf
@en
Clara L Kielkopf
@es
Clara L Kielkopf
@nl
Clara L Kielkopf
@sl
prefLabel
Clara L Kielkopf
@ast
Clara L Kielkopf
@en
Clara L Kielkopf
@es
Clara L Kielkopf
@nl
Clara L Kielkopf
@sl
P106
P21
P31
P496
0000-0002-7648-8271