[HTML][HTML] Intrinsically disordered proteins and their “mysterious”(meta) physics

VN Uversky - Frontiers in Physics, 2019 - frontiersin.org
Recognition of the natural abundance and functional importance of intrinsically disordered
proteins (IDPs), and protein hybrids that contain both intrinsically disordered protein regions …

Unusual biophysics of intrinsically disordered proteins

VN Uversky - Biochimica et Biophysica Acta (BBA)-Proteins and …, 2013 - Elsevier
Research of a past decade and a half leaves no doubt that complete understanding of
protein functionality requires close consideration of the fact that many functional proteins do …

[HTML][HTML] The E. coli MinCDE system in the regulation of protein patterns and gradients

B Ramm, T Heermann, P Schwille - Cellular and Molecular Life Sciences, 2019 - Springer
Molecular self-organziation, also regarded as pattern formation, is crucial for the correct
distribution of cellular content. The processes leading to spatiotemporal patterns often …

[HTML][HTML] The Min oscillator uses MinD-dependent conformational changes in MinE to spatially regulate cytokinesis

KT Park, W Wu, KP Battaile, S Lovell, T Holyoak… - Cell, 2011 - cell.com
In E. coli, MinD recruits MinE to the membrane, leading to a coupled oscillation required for
spatial regulation of the cytokinetic Z ring. How these proteins interact, however, is not clear …

[HTML][HTML] Highly canalized MinD transfer and MinE sequestration explain the origin of robust MinCDE-protein dynamics

J Halatek, E Frey - Cell reports, 2012 - cell.com
Min-protein oscillations in Escherichia coli are characterized by the remarkable robustness
with which spatial patterns dynamically adapt to variations of cell geometry. Moreover …

Membrane-bound MinDE complex acts as a toggle switch that drives Min oscillation coupled to cytoplasmic depletion of MinD

AG Vecchiarelli, M Li, M Mizuuchi… - Proceedings of the …, 2016 - National Acad Sciences
The Escherichia coli Min system self-organizes into a cell-pole to cell-pole oscillator on the
membrane to prevent divisions at the cell poles. Reconstituting the Min system on a lipid …

Protein self-organization: lessons from the min system

M Loose, K Kruse, P Schwille - Annual review of biophysics, 2011 - annualreviews.org
One of the most fundamental features of biological systems is probably their ability to self-
organize in space and time on different scales. Despite many elaborate theoretical models …

MinE conformational switching confers robustness on self-organized Min protein patterns

J Denk, S Kretschmer, J Halatek… - Proceedings of the …, 2018 - National Acad Sciences
Protein patterning is vital for many fundamental cellular processes. This raises two intriguing
questions: Can such intrinsically complex processes be reduced to certain core principles …

Determination of the structure of the MinD–ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and …

W Wu, KT Park, T Holyoak… - Molecular …, 2011 - Wiley Online Library
The three Min proteins spatially regulate Z ring positioning in Escherichia coli and are
dynamically associated with the membrane. MinD binds to vesicles in the presence of ATP …

The Min-protein oscillations in Escherichia coli: an example of self-organized cellular protein waves

L Wettmann, K Kruse - … of the Royal Society B: Biological …, 2018 - royalsocietypublishing.org
In the rod-shaped bacterium Escherichia coli, selection of the cell centre as the division site
involves pole-to-pole oscillations of the proteins MinC, MinD and MinE. This spatio-temporal …