Publications by authors named "J M Cabezudo Artero"

Article Synopsis
  • The text indicates that there is a correction to an article referenced by the DOI: 10.1371/journal.pone.0035263.
  • This correction likely addresses errors or inaccuracies in the original publication.
  • Such corrections are common in academic publishing to ensure the integrity and accuracy of research findings.
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Article Synopsis
  • The article DOI: 10.1371/journal.pone.0035263 has been revised or updated to correct inaccuracies or errors present in the original publication.
  • The corrections aim to enhance the reliability and clarity of the research findings discussed in that article.
  • Readers are encouraged to refer to the updated version for the most accurate information on the study's conclusions and data.
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Study Design: A retrospective study.

Purpose: We report our experience with 5-aminolevulinic acid (5-ALA)-assisted resection of spinal cord ependymomas in adults.

Overview Of Literature: Ependymoma is the most frequent primary spinal cord tumor in adults.

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Background: TNM staging of cancer is used to establish the treatment and prognosis for cancer patients, and also allows the assessment of screening programmes and hospital performance. Collection of staging data is becoming a cornerstone for cancer registries. The objective of the study was to assess the completeness of T, N, M and stage grouping registration for all cancers in the Mallorca Cancer Registry in 2006-2008 and to explore differences in T, N, M and stage grouping completeness by site, gender, age and type of hospital.

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In this work, we study dynamical properties of an extremophilic protein, Initiation Factor 6 (IF6), produced by the archeabacterium Methanocaldococcus jannascii, which thrives close to deep-sea hydrothermal vents where temperatures reach 80 °C and the pressure is up to 750 bar. Molecular dynamics simulations (MD) and quasi-elastic neutron scattering (QENS) measurements give new insights into the dynamical properties of this protein with respect to its eukaryotic and mesophilic homologue. Results obtained by MD are supported by QENS data and are interpreted within the framework of a fractional Brownian dynamics model for the characterization of protein relaxation dynamics.

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