Výsledky vyhledávání - "Andreas M. Küffner"

The interface of condensates of the hnRNPA1 low complexity domain promotes formation of amyloid fibrils

Autor: Miriam Linsenmeier, Lenka Faltova, Umberto Capasso Palmiero, Charlotte Seiffert, Andreas M. Küffner, Dorothea Pinotsi, Jiangtao Zhou, Raffaele Mezzenga, Paolo Arosio

The maturation of liquid-like protein condensates into amyloid fibrils has been associated with neurodegenerative diseases. Here, we analyze the amyloid formation mediated by condensation of the low-complexity domain of hnRNPA1, a protein involved in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b2671bd153390fbe0aa5cfb74f63628a
https://doi.org/10.1101/2022.05.23.493075

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Programmable zwitterionic droplets as biomolecular sorters and model of membraneless organelles

Autor: Miriam Linsenmeier, Umberto Capasso Palmiero, Marie R.G. Kopp, Carolina Paganini, Paolo Arosio, Andreas M. Küffner

Publikováno v: Advanced Materials, 34 (4)

Increasing evidence indicates that cells can regulate biochemical functions in time and space by generating membraneless compartments with well-defined mesoscopic properties. One important mechanism underlying this control is simple coacervation driv

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a9c43e553b8bcccb608840fc79da654
https://doi.org/10.26434/chemrxiv-2021-35cn8

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Sequestration within biomolecular condensates inhibits Aβ-42 amyloid formation

Autor: Lenka Faltova, Andreas M. Küffner, Umberto Capasso Palmiero, Miriam Linsenmeier, Paolo Arosio, Fulvio Grigolato, Remo Zuccarini, Marc Prodan

Publikováno v: Chemical Science, 12 (12)
Chemical Science

Biomolecular condensates are emerging as an efficient strategy developed by cells to control biochemical reactions in space and time by locally modifying composition and environment. Yet, local increase in protein concentration within these compartme

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d230927fd2ebfcd9ddf1daf285a9c88a
https://hdl.handle.net/20.500.11850/478092

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Adaptive Chemoenzymatic Microreactors Composed of Inorganic Nanoparticles and Bioinspired Intrinsically Disordered Proteins

Autor: Frank Krumeich, Lenka Faltova, Andreas M. Küffner, Umberto Capasso Palmiero, Paolo Arosio

Publikováno v: Angewandte Chemie. International Edition, 59 (21)

The assembly of protein and inorganic nanoparticles represents an attractive approach to generate composite materials with multiple functions. Herein, we functionalize inorganic nanoparticles with intrinsically disordered protein domains associated w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6aa0670776f8b66319e5fe0b7c2d0644
https://hdl.handle.net/20.500.11850/412161

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Acceleration of an Enzymatic Reaction in Liquid Phase Separated Compartments Based on Intrinsically Disordered Protein Domains

Autor: Remo Zuccarini, Marc Prodan, Umberto Capasso Palmiero, Andreas M. Küffner, Paolo Arosio, Lenka Faltova

Publikováno v: ChemSystemsChem, 2 (4)

Spontaneous liquid demixing of biomolecules appears to be an efficient strategy developed by cells to organize reactions in space and time. This process allows cells to modulate biochemical reactions by locally changing the concentration and the envi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4128faa5fc298d6231a957ad004da54
https://doi.org/10.1002/syst.202000001

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A Counter Propagating Lens-Mirror System for Ultrahigh Throughput Single Droplet Detection

Autor: Ying Du, Jordan Van Wyk, Andrew J. deMello, Jing Wang, Andreas M. Küffner, Paolo Arosio, Peter Fischer, Xiaobao Cao, Stavros Stavrakis

Publikováno v: Small, 16 (20)

Fluorescence-based detection schemes provide for multiparameter analysis in a broad range of applications in the chemical and biological sciences. Toward the realization of fully portable analysis systems, microfluidic devices integrating diverse fun

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4571555779afbb04d5fdc1cc872fbc28
https://pubmed.ncbi.nlm.nih.gov/32309905

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