Zobrazeno 1 - 10 of 14 pro vyhledávání: '"Alex J, McDonald"'
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Akademický článek
The N-terminus of the prion protein is a toxic effector regulated by the C-terminus
Autor: Bei Wu, Alex J McDonald, Kathleen Markham, Celeste B Rich, Kyle P McHugh, Jörg Tatzelt, David W Colby, Glenn L Millhauser, David A Harris
Publikováno v: eLife, Vol 6 (2017)
PrPC, the cellular isoform of the prion protein, serves to transduce the neurotoxic effects of PrPSc, the infectious isoform, but how this occurs is mysterious. Here, using a combination of electrophysiological, cellular, and biophysical techniques,
Externí odkaz: https://doaj.org/article/e25aea8ab81e414abac02e864afe08be
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2
An inter-domain regulatory mechanism controls toxic activities of PrPC
Autor: Bei Wu, Alex J. McDonald, David A. Harris
Publikováno v: Prion. 11:388-397
The normal function of PrPC, the cellular prion protein, has remained mysterious since its first description over 30 years ago. Amazingly, although complete deletion of the gene encoding PrPC has little phenotypic consequence, expression in transgeni
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::281ed5f847dbe523f02fce7526a80567
https://doi.org/10.1080/19336896.2017.1384894
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3
Altered Domain Structure of the Prion Protein Caused by Cu
Autor: Alex J, McDonald, Deborah R, Leon, Kathleen A, Markham, Bei, Wu, Christian F, Heckendorf, Kevin, Schilling, Hollis D, Showalter, Philip C, Andrews, Mark E, McComb, M Jake, Pushie, Catherine E, Costello, Glenn L, Millhauser, David A, Harris
Publikováno v: Structure
The cellular isoform of the prion protein (PrP(C)) serves as precursor to the infectious isoform (PrP(Sc)), and as a cell-surface receptor, which binds misfolded protein oligomers as well as physiological ligands such as Cu(2+) ions. PrP(C) consists
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ec182716fe673fbd7ef9920baf6e3e6a
https://pubmed.ncbi.nlm.nih.gov/30956132
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6
Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestation
Autor: Robin A. Aglietti, Robert C.C. Mercer, Agnes Lau, Glenn L. Millhauser, Serene Wohlgemuth, Gerold Schmitt-Ulms, David Westaway, Hristina Gapeshina, Charles E. Mays, Chae Kim, Jing Yang, Jennifer Grams, Beipei Shi, Holger Wille, Nathalie Daude, Aru Balachandran, Eric D. Walter, Jiri G. Safar, Alex J. McDonald, Jacques van der Merwe
Publikováno v: EMBO Molecular Medicine
ResearcherID
The cellular prion protein (PrP(C)) comprises a natively unstructured N-terminal domain, including a metal-binding octarepeat region (OR) and a linker, followed by a C-terminal domain that misfolds to form PrP(S) (c) in Creutzfeldt-Jakob disease. PrP
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f63448d3aea1650830ed2ee01da1e5b5
http://europepmc.org/articles/PMC4364950
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7
The N-terminus of the prion protein is a toxic effector regulated by the C-terminus
Autor: Glenn L. Millhauser, Jörg Tatzelt, David W. Colby, Kyle P McHugh, David A. Harris, Celeste B. Rich, Kathleen Markham, Bei Wu, Alex J. McDonald
Publikováno v: eLife
eLife, Vol 6 (2017)
PrPC, the cellular isoform of the prion protein, serves to transduce the neurotoxic effects of PrPSc, the infectious isoform, but how this occurs is mysterious. Here, using a combination of electrophysiological, cellular, and biophysical techniques,
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d725b083d78180a90f9c804a34f8a870
http://europepmc.org/articles/PMC5469617
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9
A New Paradigm for Enzymatic Control of α-Cleavage and β-Cleavage of the Prion Protein
Autor: Alex J. McDonald, Eric G.B. Evans, Jessie P. Dibble, Glenn L. Millhauser
Publikováno v: Journal of Biological Chemistry. 289:803-813
The cellular form of the prion protein (PrP(C)) is found in both full-length and several different cleaved forms in vivo. Although the precise functions of the PrP(C) proteolytic products are not known, cleavage between the unstructured N-terminal do
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a850a7cfad58e709b9a7d91f46f359d1
https://doi.org/10.1074/jbc.m113.502351
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10
Altered Domain Structure of the Prion Protein Caused by Cu2+ Binding and Functionally Relevant Mutations: Analysis by Cross-Linking, MS/MS, and NMR
Autor: Alex J. McDonald, Kevin M. Schilling, Deborah R. Leon, M. Jake Pushie, Bei Wu, Mark E. McComb, H. D. Hollis Showalter, Catherine E. Costello, Christian F. Heckendorf, Philip C. Andrews, David A. Harris, Glenn L. Millhauser, Kathleen Markham
Publikováno v: Structure (London, England : 1993), vol 27, iss 6
The cellular isoform of the prion protein (PrPC) serves as precursor to the infectious isoform (PrPSc), and as a cell-surface receptor, which binds misfolded protein oligomers as well as physiological ligands such as Cu2+ ions. PrPC consists of two d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3dd95ba0bfcf2804dd41ea63f89ef6b0
https://doi.org/10.1016/j.str.2019.03.008
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