The biosynthetic origin of ribofuranose in bacterial polysaccharides

Autor: Steven D. Kelly, Danielle M. Williams, Jeremy T. Nothof, Taeok Kim, Todd L. Lowary, Matthew S. Kimber, Chris Whitfield

Publikováno v: Nature Chemical Biology. 18:530-537

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::51dbc7d5daf81deffa4d9d32cfa8a593
https://doi.org/10.1038/s41589-022-01006-6

The amyloid fibril-forming β-sheet regions of amyloid β and α-synuclein preferentially interact with the molecular chaperone 14-3-3ζ

Autor: Christopher M. Dobson, David C. Thorn, Danielle M. Williams, Sarah Meehan, John A. Carver, Joanna M. Woodcock, Sophie E. Jackson

Publikováno v: Molecules, Vol 26, Iss 6120, p 6120 (2021)
Molecules
Volume 26
Issue 20

14-3-3 proteins are abundant, intramolecular proteins that play a pivotal role in cellular signal transduction by interacting with phosphorylated ligands. In addition, they are molecular chaperones that prevent protein unfolding and aggregation under

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f44396113b16fa2d71bab2c48c0bd6d9
https://hdl.handle.net/11541.2/27094

Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation.

Autor: Teresa M Treweek, Heath Ecroyd, Danielle M Williams, Sarah Meehan, John A Carver, Mark J Walker

Publikováno v: PLoS ONE, Vol 2, Iss 10, p e1046 (2007)

BackgroundAlzheimer's, Parkinson's and Creutzfeldt-Jakob disease are associated with inappropriate protein deposition and ordered amyloid fibril assembly. Molecular chaperones, including alphaB-crystallin, play a role in the prevention of protein dep

Externí odkaz: https://doaj.org/article/d49f0f914aee4690b4b52bada14e2151

In Vitro Characterization of a Multidomain Glycosyltransferase Using Fluorescently Tagged Synthetic Acceptors

Autor: Danielle M Williams, Chris Whitfield, Olga G Ovchinnikova

Publikováno v: Methods in Molecular Biology ISBN: 9781493991532

In vitro assays using fluorescently tagged sugar residues can facilitate the characterization of glycosyltransferase function. Here we describe the use of in vitro assays to characterize the three glycosyltransferase modules of the protein designated

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ea4c4c03fca215328de0d0aa69eb2aa9
https://doi.org/10.1007/978-1-4939-9154-9_19

Fabrication of Modularly Functionalizable Microcapsules Using Protein-Based Technologies

Autor: Hong-fei Wang, Chinedum O. Osuji, Gilad Kaufman, Benjamin Rudshteyn, Elsa C. Y. Yan, Heidi P. Hendrickson, Li Fu, Wei Liu, Victor S. Batista, Ashley C. Schloss, Lynne Regan, Danielle M. Williams

Publikováno v: Schloss, A C, Liu, W, Williams, D M, Kaufman, G, Hendrickson, H P, Rudshteyn, B, Fu, L, Wang, H, Batista, V S, Osuji, C, Yan, E C Y & Regan, L 2016, ' Fabrication of Modularly Functionalizable Microcapsules Using Protein-Based Technologies ', ACS Biomaterials Science and Engineering, vol. 2, no. 11, pp. 1856-1861 . https://doi.org/10.1021/acsbiomaterials.6b00447

Proteins are desirable building blocks to create self-assembled, spatially defined structures and interfaces on length-scales that are inaccessible by traditional methods. Here, we describe a novel approach to create functionalized monolayers using t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77a517668c3176345b21445dd19180e5
https://pubmed.ncbi.nlm.nih.gov/29805990