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Mauriz A. Lichtenstein on Muck Rack

Mauriz A. Lichtenstein

As seen in: Nature, Science Magazine, BioRxiv
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Articles

Design of facilitated dissociation enables timing of cytokine signalling - Nature

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By Adam Broerman, Yang Zhao, Mauriz A. Lichtenstein, Masato Ogishi, Danny D. Sahtoe, Alex Kang, Banumathi Sankaran, Asim K. Bera, Daniel Zuckerman, Stefan Stoll, K. Christopher Garcia, Florian Praetorius, Jacob Piehler
| Nature Verified
Abstract Protein design has focused on the design of ground states, ensuring that they are sufficiently low energy to be highly populated1. Designing the kinetics and dynamics of a system requires, in addition, the design of excited states that are traversed in transitions from one low-lying state to another2,3.
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Bottom-up reconstruction of functional death fold signalosomes reveals a requirement for polymer stability and avidity

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By Guan Wang, Jedediah F. Brodie, Thao-Quyen Nguyen, Mauriz A. Lichtenstein
| Science Magazine Verified
Editor’s summary Scaffolding of proteins into organized complexes is a recurrent property of biological signaling mechanisms that helps to provide efficiency, specificity, and tunability. Lichtenstein et al. explored the biophysical properties of the myddosome, a scaffold of proteins that functions in the innate immune system. The myddosome forms in response to Toll-like receptors and interleukin-1 receptors.
Open in Who Shared Issue with article?

Design of facilitated dissociation enables control over cytokine signaling duration

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By Adam Broerman, Christoph Pollmann, Mark Jackson, Mauriz A. Lichtenstein
| BioRxiv
Abstract Protein design has focused primarily on the design of ground states, ensuring they are sufficiently low energy to be highly populated. Designing the kinetics and dynamics of a system requires, in addition, the design of excited states that are traversed in transitions from one low-lying state to another.
Open in Who Shared Issue with article?
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