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Gregory M. Findlay

Researcher at University of Washington

Publications -  19
Citations -  2203

Gregory M. Findlay is an academic researcher from University of Washington. The author has contributed to research in topics: Genome editing & Cas9. The author has an hindex of 10, co-authored 16 publications receiving 1745 citations. Previous affiliations of Gregory M. Findlay include La Jolla Institute for Allergy and Immunology & Harvard University.

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Whole-organism lineage tracing by combinatorial and cumulative genome editing

TL;DR: It is shown that combinatorial, cumulative genome editing of a compact barcode can be used to record lineage information in multicellular systems and that rich, systematically generated maps of organismal development will advance the understanding of development in both healthy and disease states.
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Accurate classification of BRCA1 variants with saturation genome editing.

TL;DR: Saturation genome editing is used to assay 96.5% of all possible single-nucleotide variants in 13 exons that encode functionally critical domains of BRCA1, and functional effects for nearly 4,000 SNVs are bimodally distributed and almost perfectly concordant with established assessments of pathogenicity.
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Saturation editing of genomic regions by multiplex homology-directed repair

TL;DR: Measurement of the functional consequences of large numbers of mutations with saturation genome editing will potentially facilitate high-resolution functional dissection of both cis-regulatory elements and trans-acting factors, as well as the interpretation of variants of uncertain significance observed in clinical sequencing.
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Dephosphorylation of the nuclear factor of activated T cells (NFAT) transcription factor is regulated by an RNA-protein scaffold complex

TL;DR: Evidence is provided that a complex of lincRNA and protein forms a scaffold for a latent transcription factor and its regulatory kinases, and support an emerging consensus that lincRNAs that bind transcriptional regulators have a similar scaffold function.
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An siRNA screen for NFAT activation identifies septins as coordinators of store-operated Ca2+ entry.

TL;DR: Septin filaments and phosphatidylinositol-4,5-bisphosphate rearrange locally at endoplasmic reticulum–plasma membrane junctions before and during formation ofSTIM1–ORAI1 clusters, facilitating STIM1 targeting to these junctions and promoting the stable recruitment of ORAI1.