Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

Christopher M Dobson

Showing results (461-470 of 516) with videos related to

Pageof 52
Sort By:
Nature Communications|December 9, 2016
Multi-dimensional super-resolution imaging enables surface hydrophobicity mappingMarie N Bongiovanni, Julien Godet, Mathew H Horrocks, et al.
The EMBO Journal|October 31, 2009
Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by HipCintia Roodveldt, Carlos W Bertoncini, August Andersson, et al.
ACS Chemical Biology|June 28, 2019
Fast Fluorescence Lifetime Imaging Reveals the Aggregation Processes of α-Synuclein and Polyglutamine in Aging <i>Caenorhabditis elegans</i>Romain F Laine, Tessa Sinnige, Kai Yu Ma, et al.
Journal of Molecular Biology|July 31, 2007
Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallinsSarah Meehan, Tuomas P J Knowles, Andrew J Baldwin, et al.
ACS Central Science|September 5, 2019
Enhancement of the Anti-Aggregation Activity of a Molecular Chaperone Using a Rationally Designed Post-Translational ModificationPhilip R Lindstedt, Francesco A Aprile, Maria J Matos, et al.
The Journal of Physical Chemistry. B|August 8, 2013
A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formationErwin De Genst, Pak-Ho Chan, Els Pardon, et al.
Nature Structural & Molecular Biology|February 17, 2015
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomersSamuel I A Cohen, Paolo Arosio, Jenny Presto, et al.
Nature Chemistry|May 9, 2018
Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranesJohnny Habchi, Sean Chia, Céline Galvagnion, et al.
Scientific Reports|September 18, 2020
A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's diseaseTatsuya Ikenoue, Francesco A Aprile, Pietro Sormanni, et al.
The Journal of Biological Chemistry|May 31, 2019
Defining α-synuclein species responsible for Parkinson's disease phenotypes in miceJessica M Froula, Marta Castellana-Cruz, Nadia M Anabtawi, et al.
Pageof 52

Showing results (461-470 of 516) with videos related to

Sort By:
Pageof 52
Nature Communications|December 9, 2016
Multi-dimensional super-resolution imaging enables surface hydrophobicity mappingMarie N Bongiovanni, Julien Godet, Mathew H Horrocks, et al.
The EMBO Journal|October 31, 2009
Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by HipCintia Roodveldt, Carlos W Bertoncini, August Andersson, et al.
ACS Chemical Biology|June 28, 2019
Fast Fluorescence Lifetime Imaging Reveals the Aggregation Processes of α-Synuclein and Polyglutamine in Aging <i>Caenorhabditis elegans</i>Romain F Laine, Tessa Sinnige, Kai Yu Ma, et al.
Journal of Molecular Biology|July 31, 2007
Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallinsSarah Meehan, Tuomas P J Knowles, Andrew J Baldwin, et al.
ACS Central Science|September 5, 2019
Enhancement of the Anti-Aggregation Activity of a Molecular Chaperone Using a Rationally Designed Post-Translational ModificationPhilip R Lindstedt, Francesco A Aprile, Maria J Matos, et al.
The Journal of Physical Chemistry. B|August 8, 2013
A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formationErwin De Genst, Pak-Ho Chan, Els Pardon, et al.
Nature Structural & Molecular Biology|February 17, 2015
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomersSamuel I A Cohen, Paolo Arosio, Jenny Presto, et al.
Nature Chemistry|May 9, 2018
Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranesJohnny Habchi, Sean Chia, Céline Galvagnion, et al.
Scientific Reports|September 18, 2020
A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's diseaseTatsuya Ikenoue, Francesco A Aprile, Pietro Sormanni, et al.
The Journal of Biological Chemistry|May 31, 2019
Defining α-synuclein species responsible for Parkinson's disease phenotypes in miceJessica M Froula, Marta Castellana-Cruz, Nadia M Anabtawi, et al.
Pageof 52