K
Kem A. Sochacki
Researcher at National Institutes of Health
Publications - 51
Citations - 1621
Kem A. Sochacki is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Clathrin & Endocytosis. The author has an hindex of 16, co-authored 40 publications receiving 1200 citations. Previous affiliations of Kem A. Sochacki include University of Wisconsin-Madison.
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Journal ArticleDOI
Real-time attack on single Escherichia coli cells by the human antimicrobial peptide LL-37
TL;DR: These findings strongly suggest that disruption of the cytoplasmic membrane is not the growth-halting mechanism, and enable dissection of antimicrobial design criteria into two parts: translocation across the OM and the subsequent halting of growth.
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Endocytic proteins are partitioned at the edge of the clathrin lattice in mammalian cells.
TL;DR: It is proposed that endocytosis is driven by the recruitment, reorganization and loss of proteins within these partitioned nanoscale zones within which the presence or concentrations of proteins vary at distinct stages of organelle development.
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Correlative super-resolution fluorescence and metal replica transmission electron microscopy
TL;DR: Super-resolution localization fluorescence microscopy with transmission electron microscopy of metal replicas is used to locate proteins on the landscape of the cellular plasma membrane at the nanoscale and finds the previously unknown three-dimensional position of the endocytic protein epsin on clathrin-coated structures at the plasma membrane.
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Clathrin-adaptor ratio and membrane tension regulate the flat-to-curved transition of the clathrin coat during endocytosis.
Delia Bucher,Felix J. Frey,Kem A. Sochacki,Susann Kummer,Jan-Philip Bergeest,William J. Godinez,William J. Godinez,Hans-Georg Kräusslich,Karl Rohr,Karl Rohr,Justin W. Taraska,Ulrich S. Schwarz,Steeve Boulant,Steeve Boulant +13 more
TL;DR: The results support the notion that BSC-1 mammalian cells dynamically regulate the flat-to-curved transition in clathrin-mediated endocytosis by both biochemical and mechanical factors.
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Cytoplasmic Protein Mobility in Osmotically Stressed Escherichia coli
Michael C. Konopka,Kem A. Sochacki,Benjamin P. Bratton,Irina A. Shkel,M. Thomas Record,James C. Weisshaar +5 more
TL;DR: The effective axial diffusion coefficient of green fluorescent protein (D(GFP) in the cytoplasm of E. coli cells as a function of (phi) for both plasmolyzed and adapted cells is measured and it is shown that the data cannot be explained by crowding theory.