Výsledky vyhledávání - "Marion E. Weir"

Akademický článek

Host-Driven Phosphorylation Appears to Regulate the Budding Activity of the Lassa Virus Matrix Protein

Autor: Christopher M. Ziegler, Philip Eisenhauer, Inessa Manuelyan, Marion E. Weir, Emily A. Bruce, Bryan A. Ballif, Jason Botten

Publikováno v: Pathogens, Vol 7, Iss 4, p 97 (2018)

Lassa mammarenavirus (LASV) is an enveloped RNA virus that can cause Lassa fever, an acute hemorrhagic fever syndrome associated with significant morbidity and high rates of fatality in endemic regions of western Africa. The arenavirus matrix protein

Externí odkaz: https://doaj.org/article/a829504f55f148738954cb215e21d667

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Akademický článek

Fyn Regulates Binding Partners of Cyclic-AMP Dependent Protein Kinase A

Autor: Anna M. Schmoker, Samuel A. Barritt, Marion E. Weir, Jacqueline E. Mann, Tyler C. Hogan, Bryan A. Ballif, Paula B. Deming

Publikováno v: Proteomes, Vol 6, Iss 4, p 37 (2018)

The cAMP-dependent protein kinase A (PKA) is a serine/threonine kinase involved in many fundamental cellular processes, including migration and proliferation. Recently, we found that the Src family kinase Fyn phosphorylates the catalytic subunit of P

Externí odkaz: https://doaj.org/article/7d6b03d3fa484afca32d52efd6d993a5

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Akademický článek

NEDD4 family ubiquitin ligases associate with LCMV Z's PPXY domain and are required for virus budding, but not via direct ubiquitination of Z.

Autor: Christopher M Ziegler, Loan Dang, Philip Eisenhauer, Jamie A Kelly, Benjamin R King, Joseph P Klaus, Inessa Manuelyan, Ethan B Mattice, David J Shirley, Marion E Weir, Emily A Bruce, Bryan A Ballif, Jason Botten

Publikováno v: PLoS Pathogens, Vol 15, Iss 11, p e1008100 (2019)

Viral late domains are used by many viruses to recruit the cellular endosomal sorting complex required for transport (ESCRT) to mediate membrane scission during viral budding. Unlike the P(S/T)AP and YPX(1-3)L late domains, which interact directly wi

Externí odkaz: https://doaj.org/article/b77f00b06c8a41729f32479998049880

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FYN and ABL Regulate the Interaction Networks of the DCBLD Receptor Family

Autor: Bryan A. Ballif, Karen L. Hinkle, Jaye L. Weinert, Kathryn S. Albretsen, Anna M. Schmoker, Jacob M. Markwood, Michelle L. Lunde, Marion E. Weir, Alicia M. Ebert

Publikováno v: Molecular & Cellular Proteomics : MCP

The FYN- and ABL-regulated interactomes of DCBLD proteins have been determined using quantitative mass spectrometry-based proteomics. FYN and ABL drove the binding of several signaling molecules to DCBLD1 and DCBLD2, including members of the 14-3-3 f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31235713b406416cf5b6bf9e2b028389
https://pubmed.ncbi.nlm.nih.gov/32606017

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Fyn‐dependent phosphorylation of PlexinA1 and PlexinA2 at conserved tyrosines is essential for zebrafish eye development

Autor: Marion E. Weir, Sarah E. Emerson, Riley M. St. Clair, Alicia M. Ebert, Anna M. Schmoker, Bryan A. Ballif, Kristen P. D'Elia

Publikováno v: The FEBS Journal. 285:72-86

Plexins (Plxns) are semaphorin (Sema) receptors that play important signaling roles, particularly in the developing nervous system and vasculature. Sema-Plxn signaling regulates cellular processes such as cytoskeletal dynamics, proliferation, and dif

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ed705d25736e4b63a113b256035b964
https://doi.org/10.1111/febs.14313

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