Zobrazeno 1 - 10
of 81
pro vyhledávání: '"Julián Echave"'
Autor:
Julián Echave
Publikováno v:
Molecular Biology and Evolution. 36:613-620
The rate of evolution varies among sites within proteins. In enzymes, two rate gradients are observed: rate decreases with increasing local packing and it increases with increasing distance from catalytic residues. The rate-packing gradient would be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec108de1f798c4acf769b11360aeb93c
https://doi.org/10.1093/molbev/msy244
https://doi.org/10.1093/molbev/msy244
Autor:
Julián Echave
Publikováno v:
Biophys J
Recent studies proposed that enzyme active sites induce evolutionary constraints at long distances. The physical origin of such long-range evolutionary coupling is unknown. Here, I use a recent biophysical model of evolution to study the relationship
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09a01372fdbb0b122e8d32843f6e0c50
https://pubmed.ncbi.nlm.nih.gov/34480927
https://pubmed.ncbi.nlm.nih.gov/34480927
Autor:
Julián Echave
Publikováno v:
PeerJ
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
PeerJ, Vol 9, p e11330 (2021)
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
PeerJ, Vol 9, p e11330 (2021)
Studying the effect of perturbations on protein structure is a basic approach in protein research. Important problems, such as predicting pathological mutations and understanding patterns of structural evolution, have been addressed by computational
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e02cde61d8c678c9d17dd8859acbaa3
https://pubmed.ncbi.nlm.nih.gov/33976988
https://pubmed.ncbi.nlm.nih.gov/33976988
Autor:
Julián Echave
Studying the effect of perturbations on protein structure is a basic approach in protein research. Important problems, such as predicting pathological mutations and understanding patterns structural evolution, have been addressed by computational sim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bda911c1071425ba61bb87e5172f9ab0
https://doi.org/10.1101/2020.10.23.352955
https://doi.org/10.1101/2020.10.23.352955
Autor:
María Laura Marcos, Julián Echave
Publikováno v:
Current Research in Structural Biology
Current Research in Structural Biology, Vol 2, Iss, Pp 156-163 (2020)
Current Research in Structural Biology, Vol 2, Iss, Pp 156-163 (2020)
Protein structures do not evolve uniformly, but the degree of structure divergence varies among sites. The resulting site-dependent structure divergence patterns emerge from a process that involves mutation and selection, which may both, in principle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b6fd847fa738254f9cae8fd47998576
https://doi.org/10.1101/2020.07.10.196998
https://doi.org/10.1101/2020.07.10.196998
Publikováno v:
Nature Reviews Genetics. 17:109-121
It has long been recognized that certain sites within a protein, such as sites in the protein core or catalytic residues in enzymes, are evolutionarily more conserved than other sites. However, our understanding of rate variation among sites remains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8c03b7568c140784cbaeb380bc2fb50
https://doi.org/10.1038/nrg.2015.18
https://doi.org/10.1038/nrg.2015.18
Autor:
Julián Echave
Proteins trace trajectories in sequence space as their amino acids become substituted by other amino acids. The number of substitutions per unit time, the rate of evolution, varies among sites because of biophysical constraints. Several properties th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7d572b017e0ac42c9a258a514cda5f2
Autor:
Julián Echave, Claus O. Wilke
Publikováno v:
Annual review of biophysics. 46
For decades, rates of protein evolution have been interpreted in terms of the vague concept of “functional importance”. Slowly evolving proteins or sites within proteins were assumed to be more functionally important and thus subject to stronger
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0358a9bab2d99ffe939133c8daedab3
https://pubmed.ncbi.nlm.nih.gov/28301766
https://pubmed.ncbi.nlm.nih.gov/28301766
Autor:
Sung-Huan Yu, Tsun-Tsao Huang, So-Wei Yeh, Jenn-Kang Hwang, Chien Hua Shih, Jen-Wei Liu, Julián Echave
Publikováno v:
BioMed Research International, Vol 2014 (2014)
BioMed Research International
BioMed Research International
Functional and biophysical constraints result in site-dependent patterns of protein sequence variability. It is commonly assumed that the key structural determinant of site-specific rates of evolution is the Relative Solvent Accessibility (RSA). Howe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e23e209e88ab8121cc158e3f8988278
https://doi.org/10.1155/2014/572409
https://doi.org/10.1155/2014/572409
Publikováno v:
Current opinion in structural biology. 42
The integration of molecular evolution and protein biophysics is an emerging theme that steadily gained importance during the last 15 years, significantly advancing both fields. The central integrative concept is the stability of the native state, al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9df86f9e247e64a52a977d18603cd318
https://pubmed.ncbi.nlm.nih.gov/27865208
https://pubmed.ncbi.nlm.nih.gov/27865208