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Christopher M Dobson

Showing results (431-440 of 516) with videos related to

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ACS Chemical Neuroscience|February 23, 2019
Increased Secondary Nucleation Underlies Accelerated Aggregation of the Four-Residue N-Terminally Truncated Aβ42 Species Aβ5-42Tanja Weiffert, Georg Meisl, Patrick Flagmeier, et al.
Biochemistry|April 11, 2014
Rare individual amyloid-β oligomers act on astrocytes to initiate neuronal damagePriyanka Narayan, Kira M Holmström, Dong-Hyun Kim, et al.
Journal of the American Chemical Society|October 4, 2021
Accelerating Reaction Rates of Biomolecules by Using Shear Stress in Artificial Capillary SystemsTuuli A Hakala, Emma V Yates, Pavan K Challa, et al.
Molecules (Basel, Switzerland)|February 25, 2022
The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular ToxicityCatherine K Xu, Marta Castellana-Cruz, Serene W Chen, et al.
ACS Nano|October 30, 2018
Quantifying Co-Oligomer Formation by α-SynucleinMarija Iljina, Alexander J Dear, Gonzalo A Garcia, et al.
Nature Chemistry|April 15, 2020
Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptideThomas C T Michaels, Andela Šarić, Samo Curk, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 22, 2015
Force generation by the growth of amyloid aggregatesTherese W Herling, Gonzalo A Garcia, Thomas C T Michaels, et al.
Nano Letters|November 2, 2018
Mapping Surface Hydrophobicity of α-Synuclein Oligomers at the NanoscaleJi-Eun Lee, Jason C Sang, Margarida Rodrigues, et al.
ACS Chemical Biology|November 9, 2013
Single point mutations induce a switch in the molecular mechanism of the aggregation of the Alzheimer's disease associated Aβ42 peptideBenedetta Bolognesi, Samuel I A Cohen, Pablo Aran Terol, et al.
Nature Chemistry|April 19, 2020
Author Correction: Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptideThomas C T Michaels, Andela Šarić, Samo Curk, et al.
Pageof 52

Showing results (431-440 of 516) with videos related to

Sort By:
Pageof 52
ACS Chemical Neuroscience|February 23, 2019
Increased Secondary Nucleation Underlies Accelerated Aggregation of the Four-Residue N-Terminally Truncated Aβ42 Species Aβ5-42Tanja Weiffert, Georg Meisl, Patrick Flagmeier, et al.
Biochemistry|April 11, 2014
Rare individual amyloid-β oligomers act on astrocytes to initiate neuronal damagePriyanka Narayan, Kira M Holmström, Dong-Hyun Kim, et al.
Journal of the American Chemical Society|October 4, 2021
Accelerating Reaction Rates of Biomolecules by Using Shear Stress in Artificial Capillary SystemsTuuli A Hakala, Emma V Yates, Pavan K Challa, et al.
Molecules (Basel, Switzerland)|February 25, 2022
The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular ToxicityCatherine K Xu, Marta Castellana-Cruz, Serene W Chen, et al.
ACS Nano|October 30, 2018
Quantifying Co-Oligomer Formation by α-SynucleinMarija Iljina, Alexander J Dear, Gonzalo A Garcia, et al.
Nature Chemistry|April 15, 2020
Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptideThomas C T Michaels, Andela Šarić, Samo Curk, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 22, 2015
Force generation by the growth of amyloid aggregatesTherese W Herling, Gonzalo A Garcia, Thomas C T Michaels, et al.
Nano Letters|November 2, 2018
Mapping Surface Hydrophobicity of α-Synuclein Oligomers at the NanoscaleJi-Eun Lee, Jason C Sang, Margarida Rodrigues, et al.
ACS Chemical Biology|November 9, 2013
Single point mutations induce a switch in the molecular mechanism of the aggregation of the Alzheimer's disease associated Aβ42 peptideBenedetta Bolognesi, Samuel I A Cohen, Pablo Aran Terol, et al.
Nature Chemistry|April 19, 2020
Author Correction: Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptideThomas C T Michaels, Andela Šarić, Samo Curk, et al.
Pageof 52