Výsledky vyhledávání - "Precious G. Motshwene"

Two human MYD88 variants, S34Y and R98C, interfere with MyD88-IRAK4-myddosome assembly

Autor: Julie George, Precious G. Motshwene, Hui Wang, Andriy V. Kubarenko, Anna Rautanen, Tara C. Mills, Adrian V.S. Hill, Nicholas J. Gay, Alexander N.R. Weber

Publikováno v: The Journal of Biological Chemistry

Innate immune receptors detect microbial pathogens and subsequently activate adaptive immune responses to combat pathogen invasion. MyD88 is a key adaptor molecule in both Toll-like receptor (TLR) and IL-1 receptor superfamily signaling pathways. Thi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b8a2f45c864104d16428a0b73062e93
https://ora.ox.ac.uk/objects/uuid:c3ebc1c8-34e5-4a10-bb6f-1bb0dcf69089

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An oligomeric signaling platform formed by the Toll-like receptor signal transducers MyD88 and IRAK-4

Autor: Precious G. Motshwene, Martin C. Moncrieffe, J. Günter Grossmann, Cheng Kao, Murali Ayaluru, Alan M. Sandercock, Carol V. Robinson, Eicke Latz, Nicholas J. Gay

Toll-like receptors (TLRs) mediate responses to pathogen-associated molecules as part of the vertebrate innate immune response to infection. Receptor dimerization is coupled to downstream signal transduction by the recruitment of a post-receptor comp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d98b1fc3025a7952da5147a48de868e0
https://doi.org/10.1074/jbc.m109.022392

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The N-terminal loop of IRAK-4 death domain regulates ordered assembly of the Myddosome signalling scaffold

Autor: Anthony C G, Dossang, Precious G, Motshwene, Yang, Yang, Martyn F, Symmons, Clare E, Bryant, Satty, Borman, Julie, George, Alexander N R, Weber, Nicholas J, Gay

Publikováno v: Scientific Reports

Activation of Toll-like receptors induces dimerization and the recruitment of the death domain (DD) adaptor protein MyD88 into an oligomeric post receptor complex termed the Myddosome. The Myddosome is a hub for inflammatory and oncogenic signaling a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::646a144fa2d90256229a0c241559878e
https://pubmed.ncbi.nlm.nih.gov/27876844

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LEA (late embryonic abundant)-like protein Hsp 12 (heat-shock protein 12) is present in the cell wall and enhances the barotolerance of the yeast Saccharomyces cerevisiae

Autor: Wolf F. Brandt, Gail Kgari, George G. Lindsey, Robert J. Karreman, Precious G. Motshwene

Yeast cells Saccharomyces cerevisiae, late embryogenic abundant-like stress response protein Hsp 12 (heat-shock protein 12) were found by immunocytochemistry to be located both in the cytoplasm and in the cell wall, from where they could be extracted

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16d1629ba86f7660101ed76bf691ab64
https://europepmc.org/articles/PMC1223906/

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Significant quantities of the glycolytic enzyme phosphoglycerate mutase are present in the cell wall of yeast Saccharomyces cerevisiae

Autor: Precious G. Motshwene, George G. Lindsey, Wolf F. Brandt

Publikováno v: The Biochemical journal. 369(Pt 2)

NaOH was used to extract proteins from the cell walls of the yeast Saccharomyces cerevisiae. This treatment was shown not to disrupt yeast cells, as NaOH-extracted cells displayed a normal morphology upon electron microscopy. Moreover, extracted and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f73b002455551d802f93030487c7b285
https://pubmed.ncbi.nlm.nih.gov/12238949

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