Zobrazeno 1 - 10
of 56
pro vyhledávání: '"Alexander Miguel Monzon"'
Autor:
Juan Mac Donagh, Abril Marchesini, Agostina Spiga, Maximiliano José Fallico, Paula Nazarena Arrías, Alexander Miguel Monzon, Aimilia-Christina Vagiona, Mariane Gonçalves-Kulik, Pablo Mier, Miguel A. Andrade-Navarro
Publikováno v:
International Journal of Molecular Sciences, Vol 25, Iss 5, p 2994 (2024)
Tandem repeats (TRs) in protein sequences are consecutive, highly similar sequence motifs. Some types of TRs fold into structural units that pack together in ensembles, forming either an (open) elongated domain or a (closed) propeller, where the last
Externí odkaz:
https://doaj.org/article/a5901b4ef39441deb91eb3af2906b338
Autor:
Marcela Soledad Bertolio, Anabela La Colla, Alejandra Carrea, Ana Romo, Gabriela Canziani, Stella Maris Echarte, Sabrina Campisano, German Patricio Barletta, Alexander Miguel Monzon, Tania Melina Rodríguez, Andrea Nancy Chisari, Ricardo Alfredo Dewey
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 9 (2021)
We describe, for the first time, a new splice variant of the human TGF-β type II receptor (TβRII). The new transcript lacks 149 nucleotides, resulting in a frameshift and the emergence of an early stop codon, rendering a truncated mature protein of
Externí odkaz:
https://doaj.org/article/7da6d1743f4e4075852741ee15319b9a
Autor:
Damiano Piovesan, Andras Hatos, Giovanni Minervini, Federica Quaglia, Alexander Miguel Monzon, Silvio C E Tosatto
Publikováno v:
PLoS Computational Biology, Vol 16, Iss 6, p e1007967 (2020)
Post-translational modification (PTM) sites have become popular for predictor development. However, with the exception of phosphorylation and a handful of other examples, PTMs suffer from a limited number of available training examples and sparsity i
Externí odkaz:
https://doaj.org/article/622e220bd713406783649d3739009b3a
Publikováno v:
Biomolecules, Vol 12, Iss 1, p 92 (2022)
Biomolecular condensates challenge the classical concepts of molecular recognition. The variable composition and heterogeneous conformations of liquid-like protein droplets are bottlenecks for high-resolution structural studies. To obtain atomistic i
Externí odkaz:
https://doaj.org/article/03b606d1c86548d88123b506bac13ee7
Autor:
Mehedi Hassan, Aishwarya Alex Namasivayam, Dan DeBlasio, Nazeefa Fatima, Benjamin Siranosian, R. Gonzalo Parra, Bart Cuypers, Sayane Shome, Alexander Miguel Monzon, Julien Fumey, Farzana Rahman
Publikováno v:
BMC Bioinformatics, Vol 19, Iss S12, Pp 1-8 (2018)
Abstract This article describes the motivation, origin and evolution of the student symposia series organised by the ISCB Student Council. The meeting series started thirteen years ago in Madrid and has spread to four continents. The article conclude
Externí odkaz:
https://doaj.org/article/16b1730fd0a14333ba31d8e045c11a06
Autor:
Ana Julia Velez Rueda, Alexander Miguel Monzon, Sebastián M. Ardanaz, Luis E. Iglesias, Gustavo Parisi
Publikováno v:
BMC Bioinformatics, Vol 19, Iss 1, Pp 1-10 (2018)
Abstract Background Biocatalysis in organic solvents is nowadays a common practice with a large potential in Biotechnology. Several studies report that proteins which are co-crystallized or soaked in organic solvents preserve their fold integrity sho
Externí odkaz:
https://doaj.org/article/341909386f2d402db3bc09f3ae3c2846
Autor:
Alexander Miguel Monzon, Marco Necci, Federica Quaglia, Ian Walsh, Giuseppe Zanotti, Damiano Piovesan, Silvio C. E. Tosatto
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 12, p 4496 (2020)
Intrinsically disordered protein regions are commonly defined from missing electron density in X-ray structures. Experimental evidence for long disorder regions (LDRs) of at least 30 residues was so far limited to manually curated proteins. Here, we
Externí odkaz:
https://doaj.org/article/e1acc286f2a44e91b0b34aad82e9a160
Autor:
Alexander Miguel Monzon, Diego Javier Zea, María Silvina Fornasari, Tadeo E Saldaño, Sebastian Fernandez-Alberti, Silvio C E Tosatto, Gustavo Parisi
Publikováno v:
PLoS Computational Biology, Vol 13, Iss 2, p e1005398 (2017)
Protein motions are a key feature to understand biological function. Recently, a large-scale analysis of protein conformational diversity showed a positively skewed distribution with a peak at 0.5 Å C-alpha root-mean-square-deviation (RMSD). To unde
Externí odkaz:
https://doaj.org/article/53bc9cf9c23447c4a5a7d78b8fc09bcf
Publikováno v:
PLoS ONE, Vol 11, Iss 5, p e0154923 (2016)
Computational modeling of tertiary structures has become of standard use to study proteins that lack experimental characterization. Unfortunately, 3D structure prediction methods and model quality assessment programs often overlook that an ensemble o
Externí odkaz:
https://doaj.org/article/ba138114b5cb400bbe5bcb986a07289e
Autor:
Damiano Piovesan, Alessio Del Conte, Damiano Clementel, Alexander Miguel Monzon, Martina Bevilacqua, Maria Cristina Aspromonte, Javier A Iserte, Fernando E Orti, Cristina Marino-Buslje, Silvio C E Tosatto
Publikováno v:
Nucleic Acids Research. 51:D438-D444
The MobiDB database (URL: https://mobidb.org/) is a knowledge base of intrinsically disordered proteins. MobiDB aggregates disorder annotations derived from the literature and from experimental evidence along with predictions for all known protein se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e098be07bb56ab7eb3355a685bf60bd9
https://doi.org/10.1093/nar/gkac1065
https://doi.org/10.1093/nar/gkac1065