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Eva M. Schmid

Researcher at University of California, Berkeley

Publications -  27
Citations -  1945

Eva M. Schmid is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Phagocytosis & Signal transducing adaptor protein. The author has an hindex of 15, co-authored 26 publications receiving 1658 citations. Previous affiliations of Eva M. Schmid include Medical University of Vienna & University of California.

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Membrane bending by protein-protein crowding

TL;DR: A third general mechanism for bending fluid cellular membranes: protein–protein crowding is proposed, and it is found that even proteins unrelated to membrane curvature, such as green fluorescent protein (GFP), can bend membranes when sufficiently concentrated.
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Integrating molecular and network biology to decode endocytosis

TL;DR: It is shown here how a careful understanding of a given biological pathway can refine an interactome approach, which permits the elucidation of additional design principles and of spatio-temporal dynamics behind pathways, and aids in experimental design and interpretation.
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Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly.

TL;DR: It is proposed that clathrin, which interacts with the β-appendage, achieves ligand displacement in vivo by self-polymerisation as the coated pit matures, which changes the interaction environment from liquid-phase, affinity-driven interactions, to interactions driven by solid-phase stability (“matricity”).
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Forming giant vesicles with controlled membrane composition, asymmetry, and contents

TL;DR: This method for creating giant vesicles can be used to test models of biological processes that depend on confined volume and complex membrane composition, and it may be useful in constructing functional systems for therapeutic and biomaterials applications.
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Evolving nature of the AP2 α‐appendage hub during clathrin‐coated vesicle endocytosis

TL;DR: Using crystallography, it is shown that FxDxF and WVxF peptide motifs from synaptojanin bind to distinct subdomains on α‐appendages, called ‘top’ and 'side’ sites, which contribute to adaptor clustering.