about
tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerasesStructural basis of UGUA recognition by the Nudix protein CFI(m)25 and implications for a regulatory role in mRNA 3' processingStructural insights into eukaryotic DNA replicationThe Fpg/Nei family of DNA glycosylases: substrates, structures, and search for damageStructural Characterization of Clostridium acetobutylicum 8-Oxoguanine DNA Glycosylase in Its Apo Form and in Complex with 8-OxodeoxyguanosineThe C-terminal Lysine of Ogg2 DNA Glycosylases is a Major Molecular Determinant for Guanine/8-Oxoguanine DistinctionKinetics of Mismatch Formation opposite Lesions by the Replicative DNA Polymerase from Bacteriophage RB69A Crystallographic Study of the Role of Sequence Context in Thymine Glycol Bypass by a Replicative DNA Polymerase Serendipitously Sheds Light on the Exonuclease ComplexThe Miscoding Potential of 5-Hydroxycytosine Arises Due to Template Instability in the Replicative Polymerase Active SiteStructural Studies of a Bacterial tRNAHIS Guanylyltransferase (Thg1)-Like Protein, with Nucleotide in the Activation and Nucleotidyl Transfer SitesPreparation of selenomethionyl proteins for phase determinationDNA polymerase θ (POLQ), double-strand break repair, and cancerStructural biology of poly(A) site definitionOverproduction, crystallization and preliminary crystallographic analysis of a novel human DNA-repair enzyme that recognizes oxidative DNA damageStructural and biochemical investigation of the role in proofreading of a beta hairpin loop found in the exonuclease domain of a replicative DNA polymerase of the B familyMechanism of suppression of chromosomal instability by DNA polymerase POLQA germline polymorphism of thymine DNA glycosylase induces genomic instability and cellular transformationDestabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylaseAn open and closed case for all polymerases.Fluorescence resonance energy transfer studies of DNA polymerase β: the critical role of fingers domain movements and a novel non-covalent step during nucleotide selection.Remote Mutations Induce Functional Changes in Active Site Residues of Human DNA Polymerase β.Look Ma, no PCNA: how DNA polymerase ε synthesizes long stretches of DNA without a processivity factorLesion bypass activity of DNA polymerase θ (POLQ) is an intrinsic property of the pol domain and depends on unique sequence inserts.Human DNA polymerase θ grasps the primer terminus to mediate DNA repairBase Excision Repair in the Mitochondria.8-oxoguanine DNA glycosylases: one lesion, three subfamiliesPhosphorylation Sites Identified in the NEIL1 DNA Glycosylase Are Potential Targets for the JNK1 Kinase.Neil3, the final frontier for the DNA glycosylases that recognize oxidative damage.Determinants of substrate specificity in RNA-dependent nucleotidyl transferasesStructural basis for the dual coding potential of 8-oxoguanosine by a high-fidelity DNA polymerase.Expression and Structural Analyses of Human DNA Polymerase θ (POLQ).Purification, crystallization and preliminary X-ray diffraction of a disulfide cross-linked complex between bovine poly(A) polymerase and a chemically modified 15-mer oligo(A) RNA.Nucleotide insertion opposite a cis-syn thymine dimer by a replicative DNA polymerase from bacteriophage T7.The NEIL1 G83D germline DNA glycosylase variant induces genomic instability and cellular transformation.Defective Nucleotide Release by DNA Polymerase β Mutator Variant E288K Is the Basis of Its Low Fidelity.The A-Rule and Deletion Formation During Abasic and Oxidized Abasic Site Bypass by DNA Polymerase θ.Cryocooling of Macromolecular Crystals: Optimization MethodsCrystallization and preliminary crystallographic analysis of the signal recognition particle SRPphi14-9 fusion proteinCrystallization and preliminary X-ray analysis of the 9 kDa protein of the mouse signal recognition particle and the selenomethionyl-SRP9The mechanism of action of T7 DNA polymerase
P50
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P50
description
researcher ORCID: 0000-0002-6294-5304
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Sylvie Doublié
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Sylvie Doublié
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P106
P1153
6603840078
P21
P31
P496
0000-0002-6294-5304