Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Luciano Censoni"'
Autor:
Carolina A. Parada, Ivan Pires de Oliveira, Mayara C. F. Gewehr, João Agostinho Machado-Neto, Keli Lima, Rosangela A. S. Eichler, Lucia R. Lopes, Luiz R. G. Bechara, Julio C. B. Ferreira, William T. Festuccia, Luciano Censoni, Ivarne Luis S. Tersariol, Emer S. Ferro
Publikováno v:
Cells, Vol 11, Iss 3, p 385 (2022)
Intracellular peptides (InPeps) generated by proteasomes were previously suggested as putative natural regulators of protein–protein interactions (PPI). Here, the main aim was to investigate the intracellular effects of intracellular peptide VFDVEL
Externí odkaz:
https://doaj.org/article/0af4787aeba54bdd8849adf74bbaf058
Publikováno v:
Journal of Neurophysiology. 127:225-238
It has been hypothesized that to perform sensorimotor transformations efficiently, somatosensory information being fed back to a particular motor circuit is organized in accordance with the mechanical loading patterns of the skin that result from the
Autor:
Luciano Censoni, Pär Halje, Jan Axelsson, Katrine Skovgård, Arash Ramezani, Evgenya Malinina, Per Petersson
Background: Large-scale microelectrode recordings offer a unique opportunity to study neurophysiological processes at the network level with single cell resolution. However, in the small brains of many experimental animals, it is often technically ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bc7695eaeacbd1d5df82ade26bf552d
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-200388
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-200388
Publikováno v:
Bioinformatics. 33:2106-2113
Motivation The flow of vibrational energy in proteins has been shown not to obey expectations for isotropic media. The existence of preferential pathways for energy transport, with probable connections to allostery mechanisms, has been repeatedly dem
Autor:
Luciano Censoni, Leandro Martínez
Publikováno v:
Bioinformatics (Oxford, England). 34(23)
Motivation The majority of the inter-residue distances in a protein structure are correlated given a fixed topology. Here, we investigate whether we are able to predict a structure’s folding rate, which is known to depend on the complexity of its f