Browsing by Author "Fernandes, Rita"
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- Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondiiPublication . Delgado, Inês; Gonçalves, João; Fernandes, Rita; Zúquete, Sara; Basto, Afonso P.; Leitão, Alexandre; Soares, Helena; Nolasco, SofiaThe success of the intracellular parasite Toxoplasma gondii in invading host cells relies on the apical complex, a specialized microtubule cytoskeleton structure associated with secretory organelles. The T. gondii genome encodes three isoforms of both α- and β-tubulin, which undergo specific post-translational modifications (PTMs), altering the biochemical and biophysical proprieties of microtubules and modulating their interaction with associated proteins. Tubulin PTMs represent a powerful and evolutionarily conserved mechanism for generating tubulin diversity, forming a biochemical 'tubulin code' interpretable by microtubule-interacting factors. T. gondii exhibits various tubulin PTMs, including α-tubulin acetylation, α-tubulin detyrosination, Δ5α-tubulin, Δ2α-tubulin, α- and β-tubulin polyglutamylation, and α- and β-tubulin methylation. Tubulin glutamylation emerges as a key player in microtubule remodeling in Toxoplasma, regulating stability, dynamics, interaction with motor proteins, and severing enzymes. The balance of tubulin glutamylation is maintained through the coordinated action of polyglutamylases and deglutamylating enzymes. This work reviews and discusses current knowledge on T. gondii tubulin glutamylation. Through in silico identification of protein orthologs, we update the recognition of putative proteins related to glutamylation, contributing to a deeper understanding of its role in T. gondii biology.
- Balancing act: tubulin glutamylation and microtubule dynamics in Toxoplasma gondiiPublication . Delgado, Inês L.S.; Gonçalves, João; Fernandes, Rita; Zúquete, Sara; Basto, Afonso P.; Leitão, Alexandre; Soares, Helena; Nolasco, SofiaThe success of Toxoplasma gondii (intracellular parasite) host cell invasion relies on the apical complex, a specialized microtubule cytoskeleton structure associated with secretory organelles. The genome encodes three isoforms of both α- and β-tubulin which are altered by specific post-translational modifications (PTMs), changing the biochemical/biophysical proprieties of microtubules, and modulating their interaction with associated proteins. Tubulin PTMs are a powerful and evolutionarily conserved mechanism to generate tubulin diversity, forming a biochemical ‘tubulin code’ that can be ‘read’ by microtubule-interacting factors. The T. gondii tubulin PTMs are: α-tubulin acetylation, α-tubulin detyrosination, Δ5α-tubulin, Δ2α-tubulin, α- and β-tubulin polyglutamylation, and α- and α-tubulin methylation. Tubulin glutamylation is a key candidate to assist microtubule remodeling in Toxoplasma, being involved in the regulation of microtubule stability, dynamics, interaction with motor proteins, and severing enzymes. The correct balance of tubulin glutamylation is achieved by the coordinated action of polyglutamylases and deglutamylating enzymes. In this work, we will review and discuss the current knowledge on T. gondii tubulin glutamylation. By in silico identification of mammalian protein orthologs, we explored and updated the identification of putative proteins related to glutamylation, contributing to a better understanding of the role of tubulin glutamylation in T. gondii.
- Markerless three-dimensional gait analysis in healthy older adults: test–retest reliability and measurement errorPublication . Carvalho, Andreia; Vanrenterghem, Jos; Cabral, Sílvia; Assunção, Ana; Fernandes, Rita; Veloso, António P.; Moniz-Pereira, VeraIn older adults, gait analysis may detect changes that signal early disease states, yet challenges in biomechanical screening limit widespread use in clinical or community settings. Recently, a markerless method from multi-camera video data has become accessible, making screenings less challenging. This study evaluated the test-retest reliability and measurement error of markerless gait kinematics and kinetics in healthy older adults. Twenty-nine healthy older adults performed gait analysis on two occasions, at preferred walking speed, using their everyday clothes. Lower limb angles and moments were averaged from 8 gait cycles. Integrated pointwise indices [Intraclass Correlation Coefficient (ICCA,K) and Standard Error of Measurement (SEM)] were calculated for curve data, as well as ICCA,K, and SEM [95 % confidence intervals] for selected peaks. Generally, kinematic ICCs were good (>0.75) and reasonably stable throughout the gait cycle, except for the hip kinematics during the swing phase in the sagittal plane and pelvis tilt and rotation. The integrated and peaks SEM were <2.4°. The reliability of kinetics was similar (ICC>0.75), except for the transverse hip moment and abduction peak, fluctuating more during the swing than through the stance phase. SEM were < 0.07Nm/Kg. In conclusion, these results showed good overall test-retest reliability for markerless gait kinematics and kinetics for the hip, knee, and ankle joints, moderate for the pelvis angles, and error levels of ≤5°, and SEM%≤5% for the sagittal plane. This supports this method's use in assessing gait in healthy older adults, including kinetics, for which reliability data from markerless systems is difficult to find reported.