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Programa Argó a l’IBB: Què podem fer per reduir la resistència als antibiòtics?

Programa Argó a l’IBB: Què podem fer per reduir la resistència als antibiòtics?

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L'Institut de Ciències de l'Educació de la UAB dóna suport a la transició entre la secundària i la universitat mitjançant el Programa Argó. Aquesta iniciativa permet ampliar el coneixement mutu entre la Universitat i la secundària, facilitar a l'alumnat de batxillerat i de cicles formatius la transició i l’acollida a la Universitat i per altra banda, oferir al professorat de secundària la possibilitat d’actualitzar coneixements i conèixer centres d’estudis, projectes i recerques que es fan a la UAB. Dins d’aquest programa, enguany s’ofereixen una trentena de cursos d’estiu impartits per diferents professors de la UAB experts en diferents disciplines i van dirigits a estudiants de 3r i de 4t d'ESO, Batxillerat i Cicles Formatius d’instituts de tot Catalunya. Del 5 al 9 de juliol,
Comparative and Functional Genomics: “Mapping the human genetic architecture of COVID-19”

Comparative and Functional Genomics: “Mapping the human genetic architecture of COVID-19”

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COVID-19 Host Genetics Initiative. Mapping the human genetic architecture of COVID-19. Nature (2021). https://doi.org/10.1038/s41586-021-03767-x https://www.nature.com/articles/s41586-021-03767-x https://doi.org/10.1038/s41586-021-03767-x Abstract The genetic makeup of an individual contributes to susceptibility and response to viral infection. While environmental, clinical and social factors play a role in exposure to SARS-CoV-2 and COVID-19 disease severity1,2, host genetics may also be important. Identifying host-specific genetic factors may reveal biological mechanisms of therapeutic relevance and clarify causal relationships of modifiable environmental risk factors for SARS-CoV-2 infection and outcomes. We formed a global network of researchers to investigate the role...
Protein Folding and Conformational Diseases: “α-Helical peptidic scaffolds to target α-synuclein toxic species with nanomolar affinity”

Protein Folding and Conformational Diseases: “α-Helical peptidic scaffolds to target α-synuclein toxic species with nanomolar affinity”

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Nature Communications volume 12, Article number: 3752 (2021) Abstract α-Synuclein aggregation is a key driver of neurodegeneration in Parkinson’s disease and related syndromes. Accordingly, obtaining a molecule that targets α-synuclein toxic assemblies with high affinity is a long-pursued objective. Here, we exploit the biophysical properties of toxic oligomers and amyloid fibrils to identify a family of α-helical peptides that bind to these α-synuclein species with low nanomolar affinity, without interfering with the monomeric functional protein. This activity is translated into a high anti-aggregation potency and the ability to abrogate oligomer-induced cell damage. Using a structure-guided search we identify a human peptide expressed in the brain and the gastro
Nanobiotechnology: “Human &-Galactosidase A Mutants: Priceless Tools to DevelopNovel Therapies for Fabry Disease”

Nanobiotechnology: “Human &-Galactosidase A Mutants: Priceless Tools to DevelopNovel Therapies for Fabry Disease”

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Int. J. Mol. Sci. 2021, 22(12), 6518; https://www.mdpi.com/1422-0067/22/12/6518 Abstract Fabry disease (FD) is a lysosomal storage disease caused by mutations in the gene for the α-galactosidase A (GLA) enzyme. The absence of the enzyme or its activity results in the accumulation of glycosphingolipids, mainly globotriaosylceramide (Gb3), in different tissues, leading to a wide range of clinical manifestations. More than 1000 natural variants have been described in the GLA gene, most of them affecting proper protein folding and enzymatic activity. Currently, FD is treated by enzyme replacement therapy (ERT) or pharmacological chaperone therapy (PCT). However, as both approaches show specific drawbacks, new strategies (such as new forms of ERT, organ/cell transplant, substrate
Protein Folding and Conformational Diseases: “Prion-like proteins: from computational approaches to proteome-wide analysis”

Protein Folding and Conformational Diseases: “Prion-like proteins: from computational approaches to proteome-wide analysis”

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https://doi.org/10.1002/2211-5463.13213 Abstract Prions are self-perpetuating proteins able to switch between a soluble state and an aggregated-and-transmissible conformation. These proteinaceous entities have been widely studied in yeast, where they are involved in hereditable phenotypic adaptations. The notion that such proteins could play functional roles and be positively selected by evolution has triggered the development of computational tools to identify prion-like proteins in different kingdoms of life. These algorithms have succeeded in screening multiple proteomes, allowing the identification of prion-like proteins in a diversity of unrelated organisms, evidencing that the prion phenomenon is well conserved among species. Interestingly enough, prion-like proteins are n...
Comparative Molecular Physiology: “Lineage-level divergence of copepod glycerol transporters and the emergence of isoform-specific trafficking regulation”

Comparative Molecular Physiology: “Lineage-level divergence of copepod glycerol transporters and the emergence of isoform-specific trafficking regulation”

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Communications Biology volume 4, Article number: 643 (2021)  https://doi.org/10.1038/s42003-021-01921-9 Abstract Transmembrane conductance of small uncharged solutes such as glycerol typically occurs through aquaglyceroporins (Glps), which are commonly encoded by multiple genes in metazoan organisms. To date, however, little is known concerning the evolution of Glps in Crustacea or what forces might underly such apparent gene redundancy. Here, we show that Glp evolution in Crustacea is highly divergent, ranging from single copy genes in species of pedunculate barnacles, tadpole shrimps, isopods, amphipods and decapods to up to 10 copies in diplostracan water fleas although with monophyletic origins in each lineage. By contrast the evolution of Glps in Copepoda appears to
Protein Folding and Conformational Diseases: “Critical assessment of protein intrinsic disorder prediction”

Protein Folding and Conformational Diseases: “Critical assessment of protein intrinsic disorder prediction”

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Nature Methods volume 18, pages 472–481 (2021) https://doi.org/10.1038/s41592-021-01117-3 Abstract Intrinsically disordered proteins, defying the traditional protein structure–function paradigm, are a challenge to study experimentally. Because a large part of our knowledge rests on computational predictions, it is crucial that their accuracy is high. The Critical Assessment of protein Intrinsic Disorder prediction (CAID) experiment was established as a community-based blind test to determine the state of the art in prediction of intrinsically disordered regions and the subset of residues involved in binding. A total of 43 methods were evaluated on a dataset of 646 proteins from DisProt. The best methods use deep learning techniques and notably outperform physicochemical metho
Celular Immunology: “New paradigm in NKT cell antigens: MCS-0208 (2-(Hydroxymethyl)phenylthio-phytoceramide) an aryl-phytoceramide compound with a single hydroxyl group stimulates NKT cells”

Celular Immunology: “New paradigm in NKT cell antigens: MCS-0208 (2-(Hydroxymethyl)phenylthio-phytoceramide) an aryl-phytoceramide compound with a single hydroxyl group stimulates NKT cells”

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ChemMedChem. 2021 Apr 6.  doi: 10.1002/cmdc.202000992. Online ahead of print. Abstract NKT cells play an important role in the immune response and can be activated by glycolipids presented by CD1d protein. We present MCS-0208 an unprecedented arylthioether-phytoceramide able to induce potent iNKT cell activation, notably when tested in human iNKT cells. This arylsphingolipid analog has a simple phenyl group containing a single hydroxyl substituent as a surrogate of the sugar ring. The phenylthioether structure contrasts with a-galactosylceramide (1), the prototypical glycolipid used to induce iNKT cell stimulation, where the galactose 2'-OH and 3'-OH substituents are accepted as the minimal footprint and considered critical for NKT TCR recognition. A computational study suppo
Protein Folding and Conformational Diseases: “AlphaFold and the amyloid landscape”

Protein Folding and Conformational Diseases: “AlphaFold and the amyloid landscape”

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https://doi.org/10.1016/j.jmb.2021.167059 Highlights In this review, we discuss the applications and limitations of AlphaFold in the field of protein aggregation.• AlphaFold might help in the computationally assisted optimization of the solubility of globular proteins with biomedical and industrial interest.• In amyloid diseases, the heterogeneous nature of aggregation intermediates and amyloid fibrils hinders the use of AlphaFold.• Residue covariation in functional amyloids suggests that AlphaFold could be trained to predict their structure, ultimately assisting in the design of amyloid-based nanomaterials. Abstract Protein aggregation is a widespread phenomenon with important implications in many scientific areas. Although amyloid formation is typi
Protein Folding and Conformational Diseases: “Dual Antibody-Conjugated Amyloid Nanorods to Promote Selective Cell–Cell Interactions”

Protein Folding and Conformational Diseases: “Dual Antibody-Conjugated Amyloid Nanorods to Promote Selective Cell–Cell Interactions”

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ACS Appl. Mater. Interfaces 2021, 13, 13, 14875–14884 Publication Date: March 24, 2021 https://doi.org/10.1021/acsami.0c21996 Abstract Grafting biomolecules on nanostructures’ surfaces is an increasingly used strategy to target pathogenic cells, with both diagnostic and therapeutic applications. However, nanomaterials monofunctionalized by conjugating a single type of ligand find limited uses in pathologies/therapies that require two or more targets/receptors to be targeted and/or activated with a single molecular entity simultaneously. Therefore, multivalent nanomaterials for dual- or multitargeting are attracting significant interest. This study provides a proof of concept of such nanostructures. We have recently developed a modular methodology that allows obtaining amyloid