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Profil bibliographique

Sarah Barndt

Informations fournies par OpenAlex. Research Africa ne déduit ni nationalité, ni poste, ni coordonnées personnelles.

7Publications signalées
13Citations signalées
2Affiliations récentes

Les institutions déclarées

Les domaines associés

Genetic Neurodegenerative DiseasesDNA Repair MechanismsBlood groups and transfusionErythrocyte Function and PathophysiologyMitochondrial Function and Pathology

Les publications récentes

Accès ouvert 2025 article OpenAlex

DNA extrusion size determines pathway choice during CAG repeat expansion

Mayuri Bhatia, Ashutosh S. Phadte, Anna Lakhina, Anthony R Monte Carlo III et autres

DNA triplet repeat expansion causes several primarly neurological disorders like Huntington's disease, myotonic dystrophy type 1, and fragile-X related disorders. There is general consensus that recognition of extrahelical extrusions or hairpin-loop structures (formed by strand slippage) by the DNA mismatch repair protein …

us (code pays fourni par la source)

3 citations Nucleic Acids Research
Accès ouvert 2025 article OpenAlex

A novel isoform of tensin-1 promotes actin filament assembly for efficient erythroblast enucleation

Arit Ghosh, Megan Coffin, Sarah Barndt, Vincent Schulz et autres

ABSTRACT: Mammalian red blood cells are generated via a terminal erythroid differentiation pathway culminating in cell polarization and enucleation. Actin filament (F-actin) polymerization is critical for enucleation, but the underlying molecular regulatory mechanisms remain poorly understood. We used publicly available RNA sequencing …

us, tw (code pays fourni par la source)

0 citations Blood Advances
Accès ouvert 2025 preprint OpenAlex

DNA extrusion size determines pathway choice during CAG repeat expansion

Mayuri Bhatia, Ashutosh S. Phadte, Anna Lakhina, Anthony R. Monte Carlo et autres

DNA triplet repeat expansion is the mutational cause of neurodegenerative disorders such as Huntington's disease, myotonic dystrophy type 1, and fragile-X related disorders. There is a general consensus that recognition of extrahelical extrusions or hairpin-loop structures (formed by strand slippage) by the …

us (code pays fourni par la source)

2 citations bioRxiv (Cold Spring Harbor Laboratory)
Accès ouvert 2025 article OpenAlex

Structural and molecular basis of PCNA-activated FAN1 nuclease function in DNA repair

Fenglin Li, Ashutosh S. Phadte, Mayuri Bhatia, Sarah Barndt et autres

FAN1 is a DNA dependent nuclease whose proper function is essential for maintaining human health. For example, a genetic variant in FAN1, Arg507 to His hastens onset of Huntington’s disease, a repeat expansion disorder for which there is no cure. How the …

us (code pays fourni par la source)

5 citations Nature Communications
Accès ouvert 2024 preprint OpenAlex

A novel isoform of Tensin1 promotes actin filament assembly for efficient erythroblast enucleation

Arit Ghosh, Megan Coffin, Sarah Barndt, Vincent Schulz et autres

Abstract Mammalian red blood cells are generated via a terminal erythroid differentiation pathway culminating in cell polarization and enucleation. Actin filament polymerization is critical for enucleation, but the molecular regulatory mechanisms remain poorly understood. We utilized publicly available RNA-seq and proteomics datasets …

us, tw (code pays fourni par la source)

1 citation bioRxiv (Cold Spring Harbor Laboratory)
Accès ouvert 2024 preprint OpenAlex

Structural and molecular basis of FAN1 defects in promoting Huntington’s disease

Fei Li, Ashutosh S. Phadte, Mayuri Bhatia, Sarah Barndt et autres

FAN1 is a DNA dependent nuclease whose proper function is essential for maintaining human health. For example, a genetic variant in FAN1, Arg507 to His hastens onset of Huntington's disease, a repeat expansion disorder for which there is no cure. How the …

us (code pays fourni par la source)

2 citations bioRxiv (Cold Spring Harbor Laboratory)

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