activity
20092019
most citedGlucagon stop-go kinetics supports a monomer-trimer fibrillation model

11 citations · 19 across the 5 of their papers we have counts for

collaborators

5 papers

physics.bio-ph2019

Relaxing the aquaporin crystal structure in a membrane with surface vibrational spectroscopy

L. Schmüser, M. Trefz, S. J. Roeters +7

High-resolution structural information on membrane proteins is essential for understanding cell biology and for structure-based design of new medical drugs and drug delivery strate…

cond-mat.soft2019★ 4 cited

The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth

Erik van Dijk, Juami Hermine Mariama van Gils, Alessia Peduzzo +6

Many proteins have the potential to aggregate into amyloid fibrils, which are associated with a wide range of human disorders including Alzheimer's and Parkinson's disease. In cont…

physics.bio-ph2014★ 11 cited

Glucagon stop-go kinetics supports a monomer-trimer fibrillation model

Andrej Kosmrlj, Pia Cordsen, Anders Kyrsting +3

We investigate in vitro fibrillation kinetics of the hormone peptide glucagon at various concentrations using confocal microscopy and determine the glucagon fibril persistence leng…

q-bio.CB2012

Quality Control System Response to Stochastic Growth of Amyloid Fibrils

Simone Pigolotti, Ludvig Lizana, Daniel Otzen +1

We introduce a stochastic model describing aggregation of misfolded proteins and degradation by the protein quality control system in a single cell. In analogy with existing litera…

physics.bio-ph2009★ 4 cited

Stop-and-go kinetics in amyloid fibrillation

Jesper Fonslet, Christian Beyschau Andersen, Sandeep Krishna +6

Many human diseases are associated with protein aggregation and fibrillation. We present experiments on in vitro glucagon fibrillation using total internal reflection fluorescence…