Identificación de marcadores de superficie celular en célulasin iniciadoras del cáncer procedentes de pacientes con glioma

Comunicaciones a congreso

A comparison of quantitative proteomics methodologies on a differential experiment on test samples

Comunicaciones a congreso

Effect of autoimmune regulator protein (AIRE) expression of the cellular proteome

Comunicaciones a congreso

Caracterización de nuevos sustratos de metaloproteasas en cáncer de mama mediante marcaje metabólico diferencial (SILAC)

Comunicaciones a congreso

Cancer degradomics: ADAMI7 regulates TGF-BETA signaling through the cleavage of vasorin

Comunicaciones a congreso

Evaluation of peptide alkylation side-resctions in common protein digestion protocols

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Expresión proteica diferencial de tratamiento de fotocoagulación con láser en células ARPE

Comunicaciones a congreso

A proteored multi-centric study to assess reproducibility of relative quantification by LC-MS proteomic analysis

Comunicaciones a congreso

Disulfide driven folding for a conditionally disordered protein

Altres ajuts: ICREA, ICREA-Academia 2015 to S.V.Conditionally disordered proteins are either ordered or disordered depending on the environmental context. The substrates of the mitochondrial intermembrane space (IMS) oxidoreductase Mia40 are synthesized on cytosolic ribosomes and diffuse as intrinsically disordered proteins to the IMS, where they fold into their functional conformations; behaving thus as conditionally disordered proteins. It is not clear how the sequences of these polypeptides encode at the same time for their ability to adopt a folded structure and to remain unfolded. Here we characterize the disorder-to-order transition of a Mia40 substrate, the human small copper chaperone Cox17. Using an integrated real-time approach, including chromatography, fluorescence, CD, FTIR, SAXS, NMR, and MS analysis, we demonstrate that in this mitochondrial protein, the conformational switch between disordered and folded states is controlled by the formation of a single disulfide bond, both in the presence and in the absence of Mia40. We provide molecular details on how the folding of a conditionally disordered protein is tightly regulated in time and space, in such a way that the same sequence is competent for protein translocation and activity