Search Results - "Estaña, Alejandro"
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Realistic Ensemble Models of Intrinsically Disordered Proteins Using a Structure-Encoding Coil Database
Published in Structure (London) (05-02-2019)“…Intrinsically disordered proteins (IDPs) play fundamental roles in signaling, regulation, and cell homeostasis by specifically interacting with their partners…”
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Small-angle scattering studies of intrinsically disordered proteins and their complexes
Published in Current opinion in structural biology (01-02-2017)“…[Display omitted] •Despite the absence of permanent structure, IDPs perform crucial functions in biology.•Structural studies of IDPs require the combination of…”
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Evidence of the Reduced Abundance of Proline cis Conformation in Protein Poly Proline Tracts
Published in Journal of the American Chemical Society (29-04-2020)“…Proline is found in a cis conformation in proteins more often than other proteinogenic amino acids, where it influences structure and modulates function, being…”
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Predicting Secondary Structure Propensities in IDPs Using Simple Statistics from Three-Residue Fragments
Published in Journal of molecular biology (04-09-2020)“…Intrinsically disordered proteins (IDPs) play key functional roles facilitated by their inherent plasticity. In most of the cases, IDPs recognize their…”
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Investigating the Formation of Structural Elements in Proteins Using Local Sequence-Dependent Information and a Heuristic Search Algorithm
Published in Molecules (Basel, Switzerland) (22-03-2019)“…Structural elements inserted in proteins are essential to define folding/unfolding mechanisms and partner recognition events governing signaling processes in…”
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Conformational buffering underlies functional selection in intrinsically disordered protein regions
Published in Nature structural & molecular biology (01-08-2022)“…Many disordered proteins conserve essential functions in the face of extensive sequence variation, making it challenging to identify the mechanisms responsible…”
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Flanking Regions Determine the Structure of the Poly-Glutamine in Huntingtin through Mechanisms Common among Glutamine-Rich Human Proteins
Published in Structure (London) (07-07-2020)“…The causative agent of Huntington's disease, the poly-Q homo-repeat in the N-terminal region of huntingtin (httex1), is flanked by a 17-residue-long fragment…”
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Interdomain linkers tailor the stability of immunoglobulin repeats in polyproteins
Published in Biochemical and biophysical research communications (23-04-2021)“…Linkers in polyproteins are considered as mere spacers between two adjacent domains. However, a series of studies using single-molecule force spectroscopy have…”
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The structure of pathogenic huntingtin exon 1 defines the bases of its aggregation propensity
Published in Nature structural & molecular biology (01-03-2023)“…Huntington’s disease is a neurodegenerative disorder caused by a CAG expansion in the first exon of the HTT gene, resulting in an extended polyglutamine…”
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Multi-site-specific isotopic labeling accelerates high-resolution structural investigations of pathogenic huntingtin exon-1
Published in Structure (London) (01-06-2023)“…Huntington’s disease neurodegeneration occurs when the number of consecutive glutamines in the huntingtin exon-1 (HTTExon1) exceeds a pathological threshold of…”
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Hybrid parallelization of a multi-tree path search algorithm: Application to highly-flexible biomolecules
Published in Parallel computing (01-09-2018)“…•A new strategy to parallelize a randomized path planning algorithm is proposed.•Our hybrid approach exploits both multithreading and message-passing…”
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Flanking regions determine the structure of the poly-glutamine homo- repeat in huntingtin through mechanisms common among glutamine-rich human proteins
Published in Structure (London) (01-07-2020)“…The causative agent of Huntington's disease, the poly-Q homo-repeat in the N-terminal region of huntingtin (httex1), is flanked by a 17-residue-long fragment…”
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13
Small-angle scattering studies of intrinsically disordered proteins and their complexes
Published 07-11-2016“…Current Opinion in Structural Biology, Elsevier, 2017, 42, pp.15 - 23 Intrinsically Disordered Proteins (IDPs) perform a broad range of biological functions…”
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