User profiles for Anika L. Burrell

Anika L Burrell

PhD Candidate, University of Washington
Verified email at uw.edu
Cited by 391

BRCA1/BARD1 site-specific ubiquitylation of nucleosomal H2A is directed by BARD1

SR Witus, AL Burrell, DP Farrell, J Kang… - Nature structural & …, 2021 - nature.com
Mutations in the E3 ubiquitin ligase RING domains of BRCA1/BARD1 predispose carriers to
breast and ovarian cancers. We present the structure of the BRCA1/BARD1 RING …

IMPDH1 retinal variants control filament architecture to tune allosteric regulation

AL Burrell, C Nie, M Said, JC Simonet… - Nature structural & …, 2022 - nature.com
Inosine-5′-monophosphate dehydrogenase (IMPDH), a key regulatory enzyme in purine
nucleotide biosynthesis, dynamically assembles filaments in response to changes in …

Reconstituted IMPDH polymers accommodate both catalytically active and inactive conformations

SA Anthony, AL Burrell, MC Johnson… - Molecular biology of …, 2017 - Am Soc Cell Biol
Several metabolic enzymes undergo reversible polymerization into macromolecular
assemblies. The function of these assemblies is often unclear, but in some cases they regulate …

IMPDH dysregulation in disease: a mini review

AL Burrell, JM Kollman - Biochemical Society Transactions, 2022 - portlandpress.com
Inosine-5′-monophosphate dehydrogenase (IMPDH) is a highly conserved enzyme in purine
metabolism that is tightly regulated on multiple levels. IMPDH has a critical role in purine …

Freedom of assembly: metabolic enzymes come together

JC Simonet, AL Burrell, JM Kollman… - Molecular Biology of …, 2020 - Am Soc Cell Biol
Many different enzymes in intermediate metabolism dynamically assemble filamentous
polymers in cells, often in response to changes in physiological conditions. Most of the enzyme …

[HTML][HTML] Neurodevelopmental disorder mutations in the purine biosynthetic enzyme IMPDH2 disrupt its allosteric regulation

AG O'Neill, AL Burrell, M Zech, O Elpeleg… - Journal of Biological …, 2023 - ASBMB
Inosine 5′ monophosphate dehydrogenase (IMPDH) is a critical regulatory enzyme in
purine nucleotide biosynthesis that is inhibited by the downstream product GTP. Multiple point …

Light-sensitive phosphorylation regulates retinal IMPDH1 activity and filament assembly

SJ Calise, AG O'Neill, AL Burrell, MS Dickinson… - Journal of Cell …, 2024 - rupress.org
Inosine monophosphate dehydrogenase (IMPDH) is the rate-limiting enzyme in guanosine
triphosphate (GTP) synthesis and assembles into filaments in cells, which desensitizes the …

[HTML][HTML] A highly conserved zebrafish IMPDH retinal isoform produces the majority of guanine and forms dynamic protein filaments in photoreceptor cells

WM Cleghorn, AL Burrell, MM Giarmarco… - Journal of Biological …, 2022 - ASBMB
Inosine monophosphate dehydrogenase (IMPDH) is a key regulatory enzyme in the de
novo synthesis of the purine base guanine. Dominant mutations in human IMPDH1 cause …

[HTML][HTML] Point mutations in IMPDH2 which cause early-onset neurodevelopmental disorders disrupt enzyme regulation and filament structure

AG O'Neill, AL Burrell, M Zech, O Elpeleg, T Harel… - bioRxiv, 2023 - ncbi.nlm.nih.gov
Inosine 5’monophosphate dehydrogenase (IMPDH) is a critical regulatory enzyme in purine
nucleotide biosynthesis that is inhibited by the downstream product GTP. Multiple point …

[HTML][HTML] Light-sensitive phosphorylation regulates enzyme activity and filament assembly of human IMPDH1 retinal splice variants

SJ Calise, AG O'Neill, AL Burrell, MS Dickinson… - bioRxiv, 2023 - ncbi.nlm.nih.gov
Inosine monophosphate dehydrogenase (IMPDH) is the rate-limiting enzyme in de novo
guanosine triphosphate (GTP) synthesis and is controlled by feedback inhibition and allosteric …