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pro vyhledávání: '"Alyssa R. Stonebraker"'
Autor:
Adewale Adegbuyiro, Alyssa R. Stonebraker, Faezeh Sedighi, Caleb K. Fan, Breanna Hodges, Peng Li, Stephen J. Valentine, Justin Legleiter
Publikováno v:
Biochemistry. 61:1517-1530
Expansion of a polyglutamine (polyQ) domain within the first exon of the huntingtin (htt) protein is the underlying cause of Huntington's disease, a genetic neurodegenerative disorder. PolyQ expansion triggers htt aggregation into oligomers, fibrils,
Autor:
Alyssa R. Stonebraker, Maryssa Beasley, Sophia Massinople, Michelle Wunder, Peng Li, Stephen J. Valentine, Justin Legleiter
Publikováno v:
Protein Science. 32
Publikováno v:
Biophysical Journal. 122:230a
Autor:
Caleb K. Fan, Justin Legleiter, Sharon E. Groover, Maryssa Beasley, Katelyn Taylor, Adewale Adegbuyiro, Breanna L. Hodges, Chathuranga Siriwardhana, Alyssa R. Stonebraker
Publikováno v:
Colloids Surf B Biointerfaces
Huntington’s disease (HD) is a fatal neurodegenerative disease caused by an extended polyglutamine (polyQ) domain within the first exon of the huntingtin protein (htt). PolyQ expansion directly invokes the formation of a heterogenous mixture of tox
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7502d71cd85bf5c0322a2b25b82721d
https://europepmc.org/articles/PMC8429182/
https://europepmc.org/articles/PMC8429182/
Publikováno v:
Biophysical Journal. 121:78a
Publikováno v:
Analytical biochemistry. 609
Mixed polydiacetylene (PDA) lipid vesicles mimic cell membranes and exhibit a colorimetric response induced by mechanical stress, which can be used to determine the affinity of proteins or molecules for lipid membranes. Due to a simple spectroscopic
Autor:
Faezeh Sedighi, Barry J. Liang, Sharon E. Groover, Maryssa Beasley, Garima Agarwal, Alyssa R. Stonebraker, Iraj Hasan, Justin Legleiter, Kathryn L Kapp
Publikováno v:
Biochemistry
Several diseases, including Alzheimer's disease, Parkinson's disease, and Huntington's disease (HD), are associated with specific proteins aggregating and depositing within tissues and/or cellular compartments. The aggregation of these proteins is ch