Publication

Three branches to rule them all? UPR signalling in response to chemically versus misfolded proteins-induced ER stress

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Ubiquitin-specific protease 19 (USP19) is one of the deubiquitinating enzymes (DUBs) involved in regulating the ubiquitination status of substrate proteins. There are two major isoforms of USP19 with distinct C-termini; the USP19_a isoform has a transmembr ...
Public Library of Science2016

Spider silk thread as a fiber optic chemical sensor

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Monitoring the properties of light transmitted through a thread of spider silk enables detection of trace amounts of chemical compounds. ...
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The chromatin remodeller Chd7 and the calcium ATPase Serca2 - adding new facets to the role of Notch in Hematopoiesis and T-ALL

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Project I: Chd7 Deficiency does not affect N1-driven T-ALL Induction and Maintenance nor impair Hematopoiesis Notch1 has been shown to be a key driver in pediatric T-cell acute lymphobastic leukemia (T-ALL). Previous work in the lab identified the chromati ...
EPFL2015

N-linked sugar-regulated protein folding and quality control in the ER

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Asparagine-linked glycans (N-glycans) are displayed on the majority of proteins synthesized in the endoplasmic reticulum (ER). Removal of the outermost glucose residue recruits the lectin chaperone malectin possibly involved in a first triage of defective ...
Academic Press Ltd- Elsevier Science Ltd2015

Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones

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Hsp70s are a class of ubiquitous and highly conserved molecular chaperones playing a central role in the regulation of proteostasis in the cell. Hsp70s assist a myriad of cellular processes by binding unfolded or misfolded substrates during a complex bioch ...
Public Library Science2015

Proteostasis: Bad news and good news from the endoplasmic reticulum

Maurizio Molinari

The endoplasmic reticulum (ER) is an intracellular compartment dedicated to the synthesis and maturation of secretory and membrane proteins, totalling about 30% of the total eukaryotic cells proteome. The capacity to produce correctly folded polypeptides a ...
E M H Swiss Medical Publishers Ltd2014

Active Conformation Control of Unfolded Proteins by Hyperthermal Collision with a Metal Surface

Klaus Kern, Stephan Rauschenbach, Gordon Rinke

The physical and chemical properties of macromolecules like proteins are strongly dependent on their conformation. The degrees of freedom of their chemical bonds generate a huge conformational space, of which, however, only a small fraction is accessible i ...
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UDP-glucose:glycoprotein glucosyltransferase (UGGT1) promotes substrate solubility in the endoplasmic reticulum

Maurizio Molinari

Protein folding in the endoplasmic reticulum (ER) is error prone, and ER quality control (ERQC) processes ensure that only correctly folded proteins are exported from the ER. Glycoproteins can be retained in the ER by ERQC, and this retention contributes t ...
Amer Soc Cell Biology2013

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