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Nature Chemical Biology
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January 13, 2025
Transforming an ATP-dependent enzyme into a dissipative, self-assembling system
Yiying Li, Jie Zhu, Zhiyin Zhang, et al.
Nature Physics
|
April 30, 2019
Physical determinants of the self-replication of protein fibrils
Anđela Šarić, Alexander K Buell, Georg Meisl, et al.
Plos One
|
January 22, 2021
In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers
Enrico Zurlo, Pravin Kumar, Georg Meisl, et al.
Chemical Science
|
June 7, 2021
Effects of sedimentation, microgravity, hydrodynamic mixing and air-water interface on α-synuclein amyloid formation
Jiangtao Zhou, Francesco S Ruggeri, Manuela R Zimmermann, et al.
Annual Review of Physical Chemistry
|
March 1, 2018
Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation
Thomas C T Michaels, Anđela Šarić, Johnny Habchi, et al.
Chemical Communications (Cambridge, England)
|
July 7, 2018
Secondary nucleation in amyloid formation
Mattias Törnquist, Thomas C T Michaels, Kalyani Sanagavarapu, et al.
Scientific Reports
|
May 5, 2016
Self-assembly of MPG1, a hydrophobin protein from the rice blast fungus that forms functional amyloid coatings, occurs by a surface-driven mechanism
Chi L L Pham, Anthony Rey, Victor Lo, et al.
Nature Protocols
|
January 8, 2016
Molecular mechanisms of protein aggregation from global fitting of kinetic models
Georg Meisl, Julius B Kirkegaard, Paolo Arosio, et al.
ACS Nano
|
March 12, 2020
The Influence of Pathogenic Mutations in α-Synuclein on Biophysical and Structural Characteristics of Amyloid Fibrils
Francesco Simone Ruggeri, Patrick Flagmeier, Janet R Kumita, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
June 19, 2014
Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides
Georg Meisl, Xiaoting Yang, Erik Hellstrand, et al.
Page
of 13
Search research articles
Search
Showing results (51-60 of 121) with videos related to
Sort By:
Page
of 13
Nature Chemical Biology
|
January 13, 2025
Transforming an ATP-dependent enzyme into a dissipative, self-assembling system
Yiying Li, Jie Zhu, Zhiyin Zhang, et al.
Nature Physics
|
April 30, 2019
Physical determinants of the self-replication of protein fibrils
Anđela Šarić, Alexander K Buell, Georg Meisl, et al.
Plos One
|
January 22, 2021
In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers
Enrico Zurlo, Pravin Kumar, Georg Meisl, et al.
Chemical Science
|
June 7, 2021
Effects of sedimentation, microgravity, hydrodynamic mixing and air-water interface on α-synuclein amyloid formation
Jiangtao Zhou, Francesco S Ruggeri, Manuela R Zimmermann, et al.
Annual Review of Physical Chemistry
|
March 1, 2018
Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation
Thomas C T Michaels, Anđela Šarić, Johnny Habchi, et al.
Chemical Communications (Cambridge, England)
|
July 7, 2018
Secondary nucleation in amyloid formation
Mattias Törnquist, Thomas C T Michaels, Kalyani Sanagavarapu, et al.
Scientific Reports
|
May 5, 2016
Self-assembly of MPG1, a hydrophobin protein from the rice blast fungus that forms functional amyloid coatings, occurs by a surface-driven mechanism
Chi L L Pham, Anthony Rey, Victor Lo, et al.
Nature Protocols
|
January 8, 2016
Molecular mechanisms of protein aggregation from global fitting of kinetic models
Georg Meisl, Julius B Kirkegaard, Paolo Arosio, et al.
ACS Nano
|
March 12, 2020
The Influence of Pathogenic Mutations in α-Synuclein on Biophysical and Structural Characteristics of Amyloid Fibrils
Francesco Simone Ruggeri, Patrick Flagmeier, Janet R Kumita, et al.
Proceedings of the National Academy of Sciences of the United States of America
|
June 19, 2014
Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides
Georg Meisl, Xiaoting Yang, Erik Hellstrand, et al.
Page
of 13