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Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

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Christopher M Dobson

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Nano Letters|December 6, 2013

Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopyDorothea Pinotsi, Alexander K Buell, Celine Galvagnion, et al.

Journal of the American Chemical Society|March 12, 2004

Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding proteinKresten Lindorff-Larsen, Sigridur Kristjansdottir, Kaare Teilum, et al.

Scientific Reports|September 14, 2016

Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseasesElisa Evangelisti, Roberta Cascella, Matteo Becatti, et al.

Journal of Molecular Biology|June 11, 2002

The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic studyJohn A Carver, Robyn A Lindner, Charles Lyon, et al.

Advances in Experimental Medicine and Biology|November 13, 2019

Dynamics and Control of Peptide Self-Assembly and AggregationGeorg Meisl, Thomas C T Michaels, Paolo Arosio, et al.

Journal of Cell Science|February 21, 2012

Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomersElisa Evangelisti, Cristina Cecchi, Roberta Cascella, et al.

Biochemistry|August 17, 2010

High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure Marvin J Bayro, Thorsten Maly, Neil R Birkett, et al.

Scientific Reports|July 28, 2016

Towards a structural biology of the hydrophobic effect in protein foldingCarlo Camilloni, Daniela Bonetti, Angela Morrone, et al.

Plos One|November 9, 2016

Bifunctional Anti-Non-Amyloid Component α-Synuclein Nanobodies Are Protective In SituDavid C Butler, Shubhada N Joshi, Erwin De Genst, et al.

Scientific Reports|July 14, 2021

Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegansMichele Perni, Benedetta Mannini, Catherine K Xu, et al.

Pageof 52

Search research articles

Showing results (211-220 of 516) with videos related to

Sort By:

Pageof 52

Nano Letters|December 6, 2013

Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopyDorothea Pinotsi, Alexander K Buell, Celine Galvagnion, et al.

Journal of the American Chemical Society|March 12, 2004

Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding proteinKresten Lindorff-Larsen, Sigridur Kristjansdottir, Kaare Teilum, et al.

Scientific Reports|September 14, 2016

Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseasesElisa Evangelisti, Roberta Cascella, Matteo Becatti, et al.

Journal of Molecular Biology|June 11, 2002

The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic studyJohn A Carver, Robyn A Lindner, Charles Lyon, et al.

Advances in Experimental Medicine and Biology|November 13, 2019

Dynamics and Control of Peptide Self-Assembly and AggregationGeorg Meisl, Thomas C T Michaels, Paolo Arosio, et al.

Journal of Cell Science|February 21, 2012

Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomersElisa Evangelisti, Cristina Cecchi, Roberta Cascella, et al.

Biochemistry|August 17, 2010

High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure Marvin J Bayro, Thorsten Maly, Neil R Birkett, et al.

Scientific Reports|July 28, 2016

Towards a structural biology of the hydrophobic effect in protein foldingCarlo Camilloni, Daniela Bonetti, Angela Morrone, et al.

Plos One|November 9, 2016

Bifunctional Anti-Non-Amyloid Component α-Synuclein Nanobodies Are Protective In SituDavid C Butler, Shubhada N Joshi, Erwin De Genst, et al.

Scientific Reports|July 14, 2021

Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegansMichele Perni, Benedetta Mannini, Catherine K Xu, et al.

Pageof 52