Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Diego Javier Zea"'
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract The revolution brought about by AlphaFold2 opens promising perspectives to unravel the complexity of protein-protein interaction networks. The analysis of interaction networks obtained from proteomics experiments does not systematically prov
Externí odkaz:
https://doaj.org/article/8ba175b227b842cc8f80f008a77cbac5
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
Alternative splicing of repeats in proteins provides a mechanism for rewiring and fine-tuning protein interaction networks. In this work, we developed a robust and versatile method, ASPRING, to identify alternatively spliced protein repeats from gene
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::92600aacd5f8c5906528aa8ff113b00a
https://doi.org/10.1101/2023.04.29.538821
https://doi.org/10.1101/2023.04.29.538821
Publikováno v:
Methods in Molecular Biology ISBN: 9781071629734
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::79881c530d81904d57858e2e665f0631
https://doi.org/10.1007/978-1-0716-2974-1_5
https://doi.org/10.1007/978-1-0716-2974-1_5
Autor:
Diego Javier Zea, Juan Mac Donagh, Guillermo Benitez, Cristian Guisande Donadio, Julia Marchetti, Nicolas Palopoli, María Silvina Fornasari, Gustavo Parisi
The emerging picture of protein nature reveals its intrinsic metastability. According to this idea, although a protein is kinetically trapped in a local free energy minimum that defines its native state, those kinetic barriers can be overcome by a co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::08ddbd13ac907afb3c1d882c5dbbe037
https://doi.org/10.1101/2022.09.07.506994
https://doi.org/10.1101/2022.09.07.506994
Autor:
María Silvina Fornasari, Nahuel Escobedo, Agustina García Melani, Sebastian Fernandez Alberti, Tomás Peters, Gustavo Parisi, Nicolás Demitroff, Ana Julia Velez Rueda, Juan Mac Donagh, Eduardo Gonik, Nicolas Palopoli, Diego Javier Zea, Julieta Novomisky Nechcoff, Tadeo E. Saldaño, Julia Marchetti, Martín N. Salas
Publikováno v:
Bioinformatics (Oxford, England).
Motivation After the outstanding breakthrough of AlphaFold in predicting protein 3D models, new questions appeared and remain unanswered. The ensemble nature of proteins, for example, challenges the structural prediction methods because the models sh
Autor:
Elizabeth Martínez-Pérez, Miguel Angel Molina-Vila, Diego Javier Zea, Soledad Ochoa, Cristina Marino-Buslje
Publikováno v:
Human Mutation. 40:413-425
Malignant tumors originate from somatic mutations and other genomic and epigenomic alterations, which lead to loss of control of the cellular circuitry. These alterations present patterns of co‐occurrence and mutual exclusivity that can influence p
Publikováno v:
Genome Research
Genome Research, Cold Spring Harbor Laboratory Press, In press
HAL
Genome Research, In press
Genome Res
Genome Research, Cold Spring Harbor Laboratory Press, In press
HAL
Genome Research, In press
Genome Res
Understanding how protein function has evolved and diversified is of great importance for human genetics and medicine. Here, we tackle the problem of describing the whole transcript variability observed in several species by generalising the definiti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e97ccf1706d49300e1d4a0641598ff7c
https://doi.org/10.1101/2020.11.14.382820
https://doi.org/10.1101/2020.11.14.382820
Autor:
Gustavo Parisi, Alexander Miguel Monzon, Nicolas Palopoli, Diego Javier Zea, Silvio C. E. Tosatto, María Silvina Fornasari, Julia Marchetti
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Intrinsically disordered proteins (IDPs) lack stable tertiary structure under physiological conditions. The unique composition and complex dynamical behaviour of IDPs make them a challenge for structural biology and molecular evolution studies. Using
Autor:
Diego Javier Zea
Represent and analyze data using Plots to find actionable insights using Julia programmingKey FeaturesLearn to use static and interactive plots to explore data with JuliaBecome well versed with the various plotting attributes needed to customize your