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Biochemical analysis of FA protein complexes. We are using biochemical assays in Xenopus cell–free extracts together with assays in human cells to identify functionally important proteins and protein complexes in the FA network.

Activation of FA proteins by DNA substrates. The current understanding of the triggers of activation for the FA/BRCA pathway proteins is incomplete. We are testing DNA binding and DNA structure-specific FA protein activation in cell free extracts to identify the FA-specific transactions.

Chemical Modulation of the FA/BRCA Pathway. We designed a rapid, inexpensive and sensitive cell-free assay to screen for small molecules that modulate the FA/BRCA pathway. We are using this assay to identify potential therapeutic targets and to dissect the activity of the FA proteins within the network of proteins that guard genomic stability.

The role of the FA proteins at early stages of hematopoiesis. We identified a novel transcriptional repressor (FAZF, for Fanconi Anemia Zinc Finger) that binds to FANCC, one of the Fanconi proteins. We are interested in the functional consequences of this interaction in normal and dysregulated hematopoiesis.

We use proteins from frog eggs to understand the basics about DNA replication and repair in humans.
Fanconi protein FANCC, engineered with a red fluorescent tag, expressed in human cells

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