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31	Protein NMR studies of two systems involved in bacterial pathogenicity / Untersuchungen mittels Protein NMR an zwei Systemen mit Einfluss auf bakterielle Pathogenität Rumpel, Sigrun 01 November 2006 (has links) No description available. 540 Chemie Mathematics and Computer Science NMR Homodimer Lösungsstruktur Docken pathogene Bakterien Typ III Proteinsekretion Antibiotikaresistenz residuale dipolare Kopplungen paramagnetische Relaxationsverstärkung NMR homodimer solution structure docking pathogenic bacteria type III protein secretion antibiotic-resistant infections residual dipolar couplings (RDC) 35.25 35.62 SXL 440: Struktur {Biochemie}
32	Condensation of the β-cell secretory granule luminal cargoes pro/insulin and ICA512 RESP18 homology domain Toledo, Pamela L., Vazquez, Diego S., Gianotti, Alejo R., Abate, Milagros B., Wegbrod, Carolin, Torkko, Juha M., Solimena, Michele, Ermácora, Mario R. 16 August 2023 (has links) ICA512/PTPRN is a receptor tyrosine-like phosphatase implicated in the biogenesis and turnover of the insulin secretory granules (SGs) in pancreatic islet beta cells. Previously we found biophysical evidence that its luminal RESP18 homology domain (RESP18HD) forms a biomolecular condensate and interacts with insulin in vitro at close-to-neutral pH, that is, in conditions resembling those present in the early secretory pathway. Here we provide further evidence for the relevance of these findings by showing that at pH 6.8 RESP18HD interacts also with proinsulin—the physiological insulin precursor found in the early secretory pathway and the major luminal cargo of β-cell nascent SGs. Our light scattering analyses indicate that RESP18HD and proinsulin, but also insulin, populate nanocondensates ranging in size from 15 to 300 nm and 10e2 to 10e6 molecules. Co-condensation of RESP18HD with proinsulin/insulin transforms the initial nanocondensates into microcondensates (size >1 μm). The intrinsic tendency of proinsulin to self-condensate implies that, in the ER, a chaperoning mechanism must arrest its spontaneous intermolecular condensation to allow for proper intramolecular folding. These data further suggest that proinsulin is an early driver of insulin SG biogenesis, in a process in which its co-condensation with RESP18HD participates in their phase separation from other secretory proteins in transit through the same compartments but destined to other routes. Through the cytosolic tail of ICA512, proinsulin co-condensation with RESP18HD may further orchestrate the recruitment of cytosolic factors involved in membrane budding and fission of transport vesicles and nascent SGs. info:eu-repo/classification/ddc/610 ddc:610

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Protein NMR studies of two systems involved in bacterial pathogenicity / Untersuchungen mittels Protein NMR an zwei Systemen mit Einfluss auf bakterielle Pathogenität

Condensation of the β-cell secretory granule luminal cargoes pro/insulin and ICA512 RESP18 homology domain