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Protein Folding and Conformational Diseases: “Cryptic amyloidogenic regions in intrinsically disordered proteins: Function and disease association”

Protein Folding and Conformational Diseases: “Cryptic amyloidogenic regions in intrinsically disordered proteins: Function and disease association”

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https://doi.org/10.1016/j.csbj.2021.07.019 Abstract The amyloid conformation is considered a fundamental state of proteins and the propensity to populate it a generic property of polypeptides. Multiple proteome-wide analyses addressed the presence of amyloidogenic regions in proteins, nurturing our understanding of their nature and biological implications. However, these analyses focused on highly aggregation-prone and hydrophobic stretches that are only marginally found in intrinsically disordered regions (IDRs). Here, we explore the prevalence of cryptic amyloidogenic regions (CARs) of polar nature in IDRs. CARs are widespread in IDRs and associated with IDPs function, with particular involvement in protein–protein interactions, but their presence is also connected to a risk o
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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FEBS Open Bio 11 (2021) 2400–2417 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. Interestin
Nanobiotechnology: “Biparatopic Protein Nanoparticles for the Precision Therapy of CXCR4+ Cancers”

Nanobiotechnology: “Biparatopic Protein Nanoparticles for the Precision Therapy of CXCR4+ Cancers”

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Cancers 2021, 13(12), 2929  https://doi.org/10.3390/cancers13122929 Abstract The accumulated molecular knowledge about human cancer enables the identification of multiple cell surface markers as highly specific therapeutic targets. A proper tumor targeting could significantly avoid drug exposure of healthy cells, minimizing side effects, but it is also expected to increase the therapeutic index. Specifically, colorectal cancer has a particularly poor prognosis in late stages, being drug targeting an appropriate strategy to substantially improve the therapeutic efficacy. In this study, we have explored the potential of the human albumin-derived peptide, EPI-X4, as a suitable ligand to target colorectal cancer via the cell surface protein CXCR4, a chemokine receptor overexpress
Identifiquen nous gens relacionats amb una vida reproductiva més llarga en les dones

Identifiquen nous gens relacionats amb una vida reproductiva més llarga en les dones

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L'equip de recerca que dirigeix Ignasi Roig a l'IBB de la UAB. D'esquerra a dreta: Maria López Panadès, Andros Maldonado Linares, Mònica Ferrer Roda, Cristina Madrid Sandín, Yan Huang i Ignasi Roig Navarro. Una recerca internacional codirigida per la UAB ha identificat prop de 300 variacions gèniques que influeixen en la vida reproductiva de les dones. En l'estudi també s'han manipulat amb èxit gens clau en ratolins associats a aquestes variants tot incrementant la seva vida reproductiva. Els resultats, publicats a Nature, augmenten substancialment el coneixement sobre el procés d'envelliment reproductiu i aporten maneres de millorar la predicció de les dones que podrien arribar a la menopausa abans que altres. L’edat en què les dones passen per la menopausa és fonamen
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”

News
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