Zobrazeno 1 - 10
of 47
pro vyhledávání: '"Meredith E. Jackrel"'
Autor:
Sheng Chen, Anuradhika Puri, Braxton Bell, Joseph Fritsche, Hector H. Palacios, Maurie Balch, Macy L. Sprunger, Matthew K. Howard, Jeremy J. Ryan, Jessica N. Haines, Gary J. Patti, Albert A. Davis, Meredith E. Jackrel
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-18 (2024)
Abstract Parkinson’s disease (PD) is closely linked to α-synuclein (α-syn) misfolding and accumulation in Lewy bodies. The PDZ serine protease HTRA1 degrades fibrillar tau, which is associated with Alzheimer’s disease, and inactivating mutation
Externí odkaz:
https://doaj.org/article/d3a814cfc6b44384be88ec4319bf5430
Autor:
Yeawon Kim, Chuang Li, Chenjian Gu, Yili Fang, Eric Tycksen, Anuradhika Puri, Terri A. Pietka, Jothilingam Sivapackiam, Kendrah Kidd, Sun-Ji Park, Bryce G. Johnson, Stanislav Kmoch, Jeremy S. Duffield, Anthony J. Bleyer, Meredith E. Jackrel, Fumihiko Urano, Vijay Sharma, Maria Lindahl, Ying Maggie Chen
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-22 (2023)
Abstract Misfolded protein aggregates may cause toxic proteinopathy, including autosomal dominant tubulointerstitial kidney disease due to uromodulin mutations (ADTKD-UMOD), a leading hereditary kidney disease. There are no targeted therapies. In our
Externí odkaz:
https://doaj.org/article/72c2d4d2fcd54509bc61bc5046fee857
Autor:
Matthew K. Howard, Karlie R. Miller, Brian S. Sohn, Jeremy J. Ryan, Andy Xu, Meredith E. Jackrel
Publikováno v:
mBio, Vol 14, Iss 4 (2023)
ABSTRACT Phenol-soluble modulins (PSMs) are the primary proteinaceous component of Staphylococcus aureus biofilms. Residence in the protective environment of biofilms allows bacteria to rapidly evolve and acquire antimicrobial resistance, which can l
Externí odkaz:
https://doaj.org/article/61adf2fa236b4edabda0ec692c3ce899
Autor:
Macy L. Sprunger, Meredith E. Jackrel
Publikováno v:
STAR Protocols, Vol 3, Iss 3, Pp 101592- (2022)
Summary: This protocol describes the use of fluorescence recovery after photobleaching (FRAP) to investigate the dynamics of Matrin-3 (MATR3) condensates in live budding yeast. We detail how to generate yeast strains containing MATR3 with an enhanced
Externí odkaz:
https://doaj.org/article/0517063ebf6349a6a788ed761654008c
Publikováno v:
iScience, Vol 25, Iss 3, Pp 103900- (2022)
Summary: Matrin-3 (MATR3) is a DNA- and RNA-binding protein implicated in amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and distal myopathy. Here, we report the development of a yeast model of MATR3 proteotoxicity and aggregatio
Externí odkaz:
https://doaj.org/article/e3d0707b0cd24cf28239b5605c33ad43
Autor:
Macy L. Sprunger, Meredith E. Jackrel
Publikováno v:
Biomolecules, Vol 11, Iss 7, p 1014 (2021)
Aberrant protein folding underpins many neurodegenerative diseases as well as certain myopathies and cancers. Protein misfolding can be driven by the presence of distinctive prion and prion-like regions within certain proteins. These prion and prion-
Externí odkaz:
https://doaj.org/article/1a4b7d9ff13c436284603bd02e9aa88b
Autor:
Amber Tariq, JiaBei Lin, Meredith E. Jackrel, Christina D. Hesketh, Peter J. Carman, Korrie L. Mack, Rachel Weitzman, Craig Gambogi, Oscar A. Hernandez Murillo, Elizabeth A. Sweeny, Esin Gurpinar, Adam L. Yokom, Stephanie N. Gates, Keolamau Yee, Saurabh Sudesh, Jacob Stillman, Alexandra N. Rizo, Daniel R. Southworth, James Shorter
Publikováno v:
Cell Reports, Vol 28, Iss 8, Pp 2080-2095.e6 (2019)
Summary: Hsp104 is an AAA+ protein disaggregase, which can be potentiated via diverse mutations in its autoregulatory middle domain (MD) to mitigate toxic misfolding of TDP-43, FUS, and α-synuclein implicated in fatal neurodegenerative disorders. Pr
Externí odkaz:
https://doaj.org/article/bf589229a4c8478bb067db7496f89daf
Autor:
Meredith E. Jackrel, James Shorter
Publikováno v:
Disease Models & Mechanisms, Vol 7, Iss 10, Pp 1175-1184 (2014)
Protein misfolding is implicated in numerous lethal neurodegenerative disorders, including amyotrophic lateral sclerosis (ALS) and Parkinson disease (PD). There are no therapies that reverse these protein-misfolding events. We aim to apply Hsp104, a
Externí odkaz:
https://doaj.org/article/d10f82b2a49945a898a9b843b81451c7
Autor:
Paresh C. Shrimali, Sheng Chen, Rachel Dreher, Matthew K. Howard, Jeremy Buck, Darren Kim, Jai S. Rudra, Meredith E. Jackrel
De novo designed peptides that self-assemble into cross-β rich fibrillar biomaterials have been pursued as an innovative platform for the development of adjuvant- and inflammation-free vaccines. However, they share structural properties similar to a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f006a714365a6335db6c00af967403f
https://doi.org/10.1101/2022.09.09.507367
https://doi.org/10.1101/2022.09.09.507367
Publikováno v:
Protein Sci
Hsp104, a yeast protein disaggregase, can be potentiated via numerous missense mutations at disparate locations throughout the coiled-coil middle domain (MD). Potentiated Hsp104 variants can counter the toxicity and misfolding of TDP-43, FUS, and α-