Articolele autorului Alexandra Deaconescu
Link la profilul stiintific al lui Alexandra Deaconescu

Molecular basis for age-dependent microtubule acetylation by tubulin acetyltransferase.
Nucleotide excision repair (NER) machinery recruitment by the transcription-repair coupling factor involves unmasking of a conserved intramolecular interface

Transcription-coupled DNA repair targets DNA lesions that block progression of elongating RNA polymerases. In bacteria, the transcription-repair coupling factor (TRCF; also known as Mfd) SF2 ATPase recognizes RNA polymerase stalled at a site of DNA damage, removes the enzyme from the DNA, and recruits the Uvr(A)BC nucleotide excision repair machinery via UvrA binding. Previous studies of TRCF revealed a molecular architecture incompatible with UvrA

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Tubulin tyrosine ligase structure reveals adaptation of an ancient fold to bind and modify tubulin.
Adenomatous polyposis coli protein nucleates actin assembly and synergizes with the formin mDia1
The bacterial transcription-repair coupling factor
Structural studies of the TRCF ATPase – coupling transcription and DNA repair in bacteria with a dsDNA-tracking motor
Structural Basis for Bacterial Transcription-Coupled DNA Repair
Crystallization and preliminary structure determination of Escherichia coli Mfd, the transcription-repair coupling factor
X-ray Structure of Saccharomyces cerevisiae Homologous Mitochondrial Matrix Factor Hmf1