Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Glyn L. Devlin"'
Autor:
Glyn L. Devlin, Jitendra P. Mata, Aidan B. Grosas, Elmira Bahraminejad, Heath Ecroyd, John A. Carver, Carl Holt, Margaret Sunde, David C. Thorn, Peter Hoffmann, Tomas Koudelka
Bovine milk alpha(S2)-casein, an intrinsically disordered protein, readily forms amyloid fibrils in vitro and is implicated in the formation of amyloid fibril deposits in mammary tissue. Its two cysteine residues participate in the formation of eithe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04ad6c867a473a99857612503d6eb7a5
https://hdl.handle.net/11541.2/147494
https://hdl.handle.net/11541.2/147494
Autor:
David C, Thorn, Elmira, Bahraminejad, Aidan B, Grosas, Tomas, Koudelka, Peter, Hoffmann, Jitendra P, Mata, Glyn L, Devlin, Margaret, Sunde, Heath, Ecroyd, Carl, Holt, John A, Carver
Publikováno v:
Biophysical chemistry. 270
Bovine milk α
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1f4423eaac042ecf74ad1c9cfba6146b
https://pubmed.ncbi.nlm.nih.gov/33545456
https://pubmed.ncbi.nlm.nih.gov/33545456
Autor:
John A. Carver, Elizabeth Vierling, Andrew Baldwin, Glyn L. Devlin, Agata Rekas, Justin L. P. Benesch, Eman Basha, Florian Stengel, Carol V. Robinson, J. Andrew Aquilina, Joseph Horwitz, Robyn A. Lindner
SummaryThe function of ScHSP26 is thermally controlled: the heat shock that causes the destabilization of target proteins leads to its activation as a molecular chaperone. We investigate the structural and dynamical properties of ScHSP26 oligomers th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e32dc96a60ea2b110db0fe0314992410
https://ora.ox.ac.uk/objects/uuid:194c62c3-2d41-4e1f-8956-a003b3448fcd
https://ora.ox.ac.uk/objects/uuid:194c62c3-2d41-4e1f-8956-a003b3448fcd
Autor:
Christopher M. Dobson, Michele Vendruscolo, Mark E. Welland, Eugene M. Terentjev, Tuomas P. J. Knowles, Glyn L. Devlin, Samuel I. A. Cohen, Christopher A. Waudby, Adriano Aguzzi
Publikováno v:
Science. 326:1533-1537
Dissecting Amyloid Formation Amyloid fibrils are associated with clinical disorders ranging from Alzheimer's disease to type II diabetes. Their self-assembly can be described by a master equation that takes into account nucleation-dependent polymeriz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92dc88dfa4efaa8fba078ca251220ee8
https://doi.org/10.1126/science.1178250
https://doi.org/10.1126/science.1178250
Autor:
David Klenerman, Christopher M. Dobson, Angel Orte, Glyn L. Devlin, Richard W. Clarke, Neil R. Birkett
Publikováno v:
Proceedings of the National Academy of Sciences. 105:14424-14429
A key issue in understanding the pathogenic conditions associated with the aberrant aggregation of misfolded proteins is the identification and characterization of species formed during the aggregation process. Probing the nature of such species has,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1acc10b6ecdeb3e707b17473d91f7ad3
https://doi.org/10.1073/pnas.0803086105
https://doi.org/10.1073/pnas.0803086105
Autor:
David C. Thorn, Danielle M. Williams, Glyn L. Devlin, Peter Hoffmann, Heath Ecroyd, Thomas Koudelka, John A. Carver
Publikováno v:
Journal of Biological Chemistry. 283:9012-9022
Amyloid fibrils are aggregated and precipitated forms of protein in which the protein exists in highly ordered, long, unbranching threadlike formations that are stable and resistant to degradation by proteases. Fibril formation is an ordered process
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ccb08c81d1235675f4a8a5ef37abd3b
https://doi.org/10.1074/jbc.m709928200
https://doi.org/10.1074/jbc.m709928200
Autor:
Anna K Tickler, Sally L. Gras, Glyn L. Devlin, Michael A. Horton, Cait E. MacPhee, Christopher M. Dobson, Adam M. Squires
Publikováno v:
Biomaterials. 29:1553-1562
We describe experiments designed to explore the possibility of using amyloid fibrils as new nanoscale biomaterials for promoting and exploiting cell adhesion, migration and differentiation in vitro. We created peptides that add the biological cell ad
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::defc04fce675df0c987d83eff2235c1d
https://doi.org/10.1016/j.biomaterials.2007.11.028
https://doi.org/10.1016/j.biomaterials.2007.11.028
Publikováno v:
Journal of biological chemistry, 2008, Vol.283(16), pp.10500-10512 [Peer Reviewed Journal]
Here we investigate the effects of a myopathy-causing mutation in alphaB-crystallin, Q151X, upon its structure and function. This mutation removes the C-terminal domain of alphaB-crystallin, which is expected to compromise both its oligomerization an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f47c58cdbb7bd0e11766b592bc861a7
https://doi.org/10.1074/jbc.m706453200
https://doi.org/10.1074/jbc.m706453200
Autor:
Tuomas P. J. Knowles, Mark E. Welland, Glyn L. Devlin, Stefan Auer, Wenmiao Shu, Christopher M. Dobson, Sarah Meehan
Publikováno v:
Proceedings of the National Academy of Sciences. 104:10016-10021
Aggregation of proteins and peptides is a widespread and much-studied problem, with serious implications in contexts ranging from biotechnology to human disease. An understanding of the proliferation of such aggregates under specific conditions requi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52fadacdc2d23f7f4e4bc2e1013f443b
https://doi.org/10.1073/pnas.0610659104
https://doi.org/10.1073/pnas.0610659104
Publikováno v:
Biophysical Journal. 92(4):1336-1342
Protein aggregation is a problem with a multitude of consequences, ranging from affecting protein expression to its implication in many diseases. Of recent interest is the specific form of aggregation leading to the formation of amyloid fibrils, stru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d3e8c1e056e35ec7ae721465b59ddf4