17 results on '"Guilherme G, Moreira"'
Search Results
2. Tau liquid–liquid phase separation is modulated by the Ca 2+ ‐switched chaperone activity of the <scp>S100B</scp> protein
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Guilherme G. Moreira and Cláudio M. Gomes
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Cellular and Molecular Neuroscience ,Biochemistry - Published
- 2023
3. Tau liquid-liquid phase separation is modulated by the Ca
- Author
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Guilherme G, Moreira and Cláudio M, Gomes
- Abstract
Aggregation of the microtubule-associated protein tau is implicated in several neurodegenerative tauopathies including Alzheimer's disease (AD). Recent studies evidenced tau liquid-liquid phase separation (LLPS) into droplets as an early event in tau pathogenesis with the potential to enhance aggregation. Tauopathies like AD are accompanied by sustained neuroinflammation and the release of alarmins at early stages of inflammatory responses encompass protective functions. The Ca
- Published
- 2022
4. Dynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding
- Author
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Urmi Sengupta, Guilherme G. Moreira, Ana P. Carapeto, Filipa S. Carvalho, Andrea Quezada, Mário Rodrigues, Isabel Cardoso, Guenter Fritz, Nicha Puangmalai, Isabelle Landrieu, Federico Herrera, Rakez Kayed, Cláudio M. Gomes, Joana S. Cristóvão, François Xavier Cantrelle, Universidade de Lisboa = University of Lisbon (ULISBOA), Biologie Structurale Intégrative (ERL 9002 - BSI ), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Facteurs de Risque et Déterminants Moléculaires des Maladies liées au Vieillissement - U 1167 (RID-AGE), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), The University of Texas Medical Branch (UTMB), Universidade do Porto = University of Porto, Instituto de Ciências Biomédicas de Abel Salazar (ICBAS), University of Hohenheim, This work was funded by Fundação para a Ciência e Tecnologia (Portugal) through research grants PTDC/NEU-NMC/2138/2014 (to C.M.G.), PTDC/BIA-BQM/29963/2017 (F.S.C.), PTDC/MED-NEU/31417/2017 (to F.H.), and POCI-01-0145-FEDER-007274 (to I.C.), investigator grants CEECIND/00031/2017 (to A.P.C.) and IF/00094/2013/CP1173/CT0005 (to F.H.), PhD fellowship SFRH/BD/101171/2014 (to J.S.C.) and DFA/BD/6443/2020 (to G.G.M.), and center grants UIDB/04046/2020 and UID/MULTI/04046/2020 (to BioISI) and Norte-01-0145-FEDER-000008 (to IBMC/I3S)., Landrieu, Isabelle, Universidade de Lisboa (ULISBOA), and Universidade do Porto
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[SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] ,Science ,Tau protein ,General Physics and Astronomy ,tau Proteins ,S100 Calcium Binding Protein beta Subunit ,Protein Aggregation, Pathological ,Article ,Biophysical Phenomena ,General Biochemistry, Genetics and Molecular Biology ,Cell Line ,03 medical and health sciences ,0302 clinical medicine ,Microtubule ,Biophysical chemistry ,Calcium-binding protein ,mental disorders ,Humans ,Protein folding ,[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM] ,Nuclear Magnetic Resonance, Biomolecular ,[SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM] ,030304 developmental biology ,0303 health sciences ,Multidisciplinary ,biology ,[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] ,Chemistry ,Neurodegenerative Diseases ,General Chemistry ,Kinetics ,Proteostasis ,Structural biology ,Chaperone (protein) ,biology.protein ,Biophysics ,Protein Structural Elements ,030217 neurology & neurosurgery ,Molecular Chaperones ,Protein Binding ,Binding domain - Abstract
The microtubule-associated protein tau is implicated in the formation of oligomers and fibrillar aggregates that evade proteostasis control and spread from cell-to-cell. Tau pathology is accompanied by sustained neuroinflammation and, while the release of alarmin mediators aggravates disease at late stages, early inflammatory responses encompass protective functions. This is the case of the Ca2+-binding S100B protein, an astrocytic alarmin which is augmented in AD and which has been recently implicated as a proteostasis regulator, acting over amyloid β aggregation. Here we report the activity of S100B as a suppressor of tau aggregation and seeding, operating at sub-stoichiometric conditions. We show that S100B interacts with tau in living cells even in microtubule-destabilizing conditions. Structural analysis revealed that tau undergoes dynamic interactions with S100B, in a Ca2+-dependent manner, notably with the aggregation prone repeat segments at the microtubule binding regions. This interaction involves contacts of tau with a cleft formed at the interface of the S100B dimer. Kinetic and mechanistic analysis revealed that S100B inhibits the aggregation of both full-length tau and of the microtubule binding domain, and that this proceeds through effects over primary and secondary nucleation, as confirmed by seeding assays and direct observation of S100B binding to tau oligomers and fibrils. In agreement with a role as an extracellular chaperone and its accumulation near tau positive inclusions, we show that S100B blocks proteopathic tau seeding. Together, our findings establish tau as a client of the S100B chaperone, providing evidence for neuro-protective functions of this inflammatory mediator across different tauopathies., The calcium binding protein S100B is an abundantly expressed protein in the brain and has neuro-protective functions by inhibiting Aβ aggregation and metal ion toxicity. Here, the authors combine cell biology and biochemical experiments with chemical kinetics and NMR measurements and show that S100B protein is an extracellular Tau chaperone and further characterize the interactions between S100B and Tau.
- Published
- 2021
5. Tetramerization of the S100B Chaperone Spawns a Ca
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António J, Figueira, Guilherme G, Moreira, Joana, Saavedra, Isabel, Cardoso, and Cláudio M, Gomes
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Amyloid beta-Peptides ,Alzheimer Disease ,Protein Conformation ,Alarmins ,Animals ,Humans ,Calcium ,S100 Calcium Binding Protein beta Subunit ,Protein Multimerization ,Protein Aggregation, Pathological ,Molecular Chaperones - Abstract
Alzheimer's disease (AD) hallmarks include the aggregation of amyloid-β (Aβ), tau and neuroinflammation promoted by several alarmins. Among these is S100B, a small astrocytic homodimeric protein, upregulated in AD, whose multiple biological activities depend on localization, concentration, and assembly state. S100B was reported to inhibit the aggregation and toxicity of Aβ42 and tau similarly to a holdase-type chaperone. This activity is dependent of Ca
- Published
- 2022
6. Cu2+-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-β aggregation
- Author
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Guilherme G. Moreira, António E. N. Ferreira, Guenter Fritz, Ana P. Carapeto, Isabel Cardoso, Filipe E. P. Rodrigues, Cláudio M. Gomes, Mário Rodrigues, Joana S. Cristóvão, and Miguel Machuqueiro
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Catalysis ,law.invention ,03 medical and health sciences ,0302 clinical medicine ,law ,Materials Chemistry ,medicine ,Extracellular ,Chaperone activity ,030304 developmental biology ,0303 health sciences ,biology ,Chemistry ,Neurodegeneration ,Metals and Alloys ,Disulfide bond ,General Chemistry ,medicine.disease ,Surfaces, Coatings and Films ,Electronic, Optical and Magnetic Materials ,Proteostasis ,Polymerization ,Chaperone (protein) ,Ceramics and Composites ,biology.protein ,Biophysics ,Suppressor ,030217 neurology & neurosurgery - Abstract
S100B is an extracellular protein implicated in Alzheimer's Disease and a suppressor of amyloid-β aggregation. Herein we report a mechanism tying Cu2+ binding to a change in assembly state yielding disulfide cross-linked oligomers with higher anti-aggregation activity. This chemical control of chaperone function illustrates a regulatory process relevant under metal and proteostasis dysfunction as in neurodegeneration.
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- 2021
7. Cu
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Joana S, Cristóvão, Guilherme G, Moreira, Filipe E P, Rodrigues, Ana P, Carapeto, Mário S, Rodrigues, Isabel, Cardoso, António E N, Ferreira, Miguel, Machuqueiro, Guenter, Fritz, and Cláudio M, Gomes
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Models, Molecular ,Protein Aggregates ,Amyloid beta-Peptides ,Binding Sites ,Cross-Linking Reagents ,Humans ,Disulfides ,S100 Calcium Binding Protein beta Subunit ,Protein Aggregation, Pathological ,Copper ,Molecular Chaperones ,Polymerization - Abstract
S100B is an extracellular protein implicated in Alzheimer's Disease and a suppressor of amyloid-β aggregation. Herein we report a mechanism tying Cu2+ binding to a change in assembly state yielding disulfide cross-linked oligomers with higher anti-aggregation activity. This chemical control of chaperone function illustrates a regulatory process relevant under metal and proteostasis dysfunction as in neurodegeneration.
- Published
- 2020
8. Contributors
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Olga Abian, Ilaria Bellezza, Ganeko Bernardo-Seisdedos, Isabel Betancor-Fernandez, Jean-Marc Blouin, Kerensa Broersen, Giulia Calloni, Barbara Cellini, Caspar E. Christensen, Francisco Conejero-Lara, Joana S. Cristóvão, Marte I. Flydal, Nicole Fontana, Douglas M. Fowler, David Gil, Cláudio M. Gomes, Sarah Good, Andreas M. Grabrucker, Fedora Grande, Silvia Grottelli, Aylin C. Hanyaloglu, Rasmus Hartmann-Petersen, Emil Hausvik, Jo Ann Janovick, Michael Maglegaard Jepsen, Kresten Lindorff-Larsen, Aurora Martinez, Thomas J. McCorvie, Oscar Millet, Guilherme G. Moreira, Bertrand Morel, Athi N. Naganathan, Jose L. Neira, Sofie V. Nielsen, Angel L. Pey, Emmanuel Richard, Bruno Rizzuti, Eduardo Salido, Signe M. Schenstrøm, Svein I. Støve, Amelie Stein, David J. Timson, Alfredo Ulloa-Aguirre, Jarl Underhaug, R. Martin Vabulas, Patricija van Oosten-Hawle, Sonia Vega, Adrian Velazquez-Campoy, Wyatt W. Yue, and Teresa Zariñán
- Published
- 2020
9. Metals and amyloid gain-of-toxic mechanisms in neurodegenerative diseases
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Andreas M. Grabrucker, Guilherme G. Moreira, Joana S. Cristóvão, and Cláudio M. Gomes
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Amyloid β ,Amyloid ,Chemistry ,Zinc ion ,chemistry.chemical_element ,Zinc ,Protein aggregation ,Neuroscience ,Homeostasis - Abstract
Protein aggregation is a cornerstone in amyloid-forming neurodegenerative diseases that is largely due to altered conditions in the biochemistry of key components of the neuronal environment, including metal ions. Indeed, trace neurometals such as calcium, zinc, and copper are vital players in brain neurobiology, whose homeostasis is altered in most neurodegenerative conditions; further, metals ions are widely found within proteinaceous inclusions from patients and animal models. This chapter briefly gives an overview of the influence of trace metals in amyloid formation in connection to their homeostasis in the brain. In particular, the role of zinc in Alzheimer’s disease is more thoroughly discussed. Indeed, the deregulation of zinc ions has well-established mechanistic links to Alzheimer’s pathophysiology, including direct interaction effects with amyloid β and tau, the two amyloid-forming proteins involved in this neurodegenerative disease.
- Published
- 2020
10. Zinc Binding to Tau Influences Aggregation Kineticsand Oligomer Distribution
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Isabelle Landrieu, Mário Rodrigues, Carlos Cordeiro, Guilherme G. Moreira, Joana S. Cristóvão, Vukosava M Torres, Cláudio M. Gomes, Ana P. Carapeto, Universidade de Lisboa (ULISBOA), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Universidade de Lisboa = University of Lisbon (ULISBOA), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), and Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS)
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Circular dichroism ,spectroscopy ,Amyloid ,Protein Conformation ,Tau protein ,chemistry.chemical_element ,tau Proteins ,Zinc ,Protein aggregation ,Oligomer ,Article ,Catalysis ,protein aggregation ,Inorganic Chemistry ,Protein Aggregates ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Dynamic light scattering ,Alzheimer Disease ,Spectroscopy, Fourier Transform Infrared ,Humans ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Benzothiazoles ,Physical and Theoretical Chemistry ,Molecular Biology ,Conformational isomerism ,ComputingMilieux_MISCELLANEOUS ,030304 developmental biology ,mass spectrometry ,0303 health sciences ,calcium ,biology ,Chemistry ,Circular Dichroism ,Organic Chemistry ,zinc ,neurodegeneration ,amyloid ,General Medicine ,intrinsically disordered protein ,Computer Science Applications ,Kinetics ,stomatognathic diseases ,Biophysics ,biology.protein ,Tau ,human activities ,030217 neurology & neurosurgery - Abstract
Metal ions are well known modulators of protein aggregation and are key players in Alzheimer&rsquo, s Disease, being found to be associated to pathologic protein deposits in diseased brains. Therefore, understanding how metals influence amyloid aggregation is critical in establishing molecular mechanisms that underlie disease onset and progression. Here, we report data on the interaction of full-length human Tau protein with calcium and zinc ions, evidencing that Tau self-assembly is differently regulated, depending on the type of bound metal ion. We established that Tau binds 4 Zn2+ and 1 Ca2+ per monomer while using native mass spectrometry analysis, without inducing order or substantial conformational changes in the intrinsically disordered Tau, as determined by structural analysis using circular dichroism and Attenuated Total Reflectance-Fourier Transform Infrared (ATR-FTIR) spectroscopies. However, Tau aggregation is found to proceed differently in the calcium- and -zinc bound forms. While the rate of aggregation, as determined from thioflavin-T (ThT) fluorescence kinetics, is highly increased in both cases, the reaction proceeds via different mechanisms, as evidenced by the absence of the lag phase in the reaction of zinc-bound Tau. Monitoring Tau aggregation using native mass spectrometry indeed evidenced a distinct distribution of Tau conformers along the reaction, as confirmed by dynamic light scattering analysis. We propose that such differences arise from zinc binding at distinct locations within the Tau sequence that prompt both the rapid formation of seeding oligomers through interactions at high affinity sites within the repeat domains, as well as amorphous aggregation, through low affinity interactions with residues elsewhere in the sequence, including at the fuzzy coat domain.
- Published
- 2019
11. Multicentric Study on Enteric Protists Occurrence in Zoological Parks in Portugal.
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Mega J, Moreira R, Moreira G, Silva-Loureiro A, Gomes da Silva P, Istrate C, Santos-Silva S, Rivero-Juarez A, Carmena D, and Mesquita JR
- Abstract
Parasitic infections of the gastrointestinal tract of domestic animals play a major role in the transmission of disease, which in turn may result in financial and productive losses. Notwithstanding, studies on the burden and distribution of diarrheagenic protists in zoological gardens are still insufficient. Given the close animal-animal and animal-human interaction in these settings, Public Health concerns under the One Health context are raised. Using molecular detection tools and phylogenetic analysis, the goal of this study was to assess the occurrence of four potentially zoonotic protists- Balantioides coli , Blastocystis sp., Cryptosporidium spp. and Giardia spp.-in animals residing in zoological parks in Portugal. Occurrence of Eimeria spp. was also assessed because of its veterinary relevance. Although Blastocystis sp. represents most of the positive samples obtained (11.6%; 95% CI: 0.08-0.17), all parasites were detected ( B. coli (2.9%; 95% CI: 0.01-0.06), and Cryptosporidium spp., Eimeria spp. and Giardia spp. presented the same prevalence (0.5%; 95% CI: 0.00-0.03)). We also describe the first molecular detection of B. coli in a collared peccary ( Tayassu tajacu ), of Blastocystis sp. in three different python species, and G. muris in a central bearded dragon ( Pogona vitticeps ), suggesting the broadening of the host range for these parasites.
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- 2024
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12. On the faecal detection of Halicephalobus gingivalis in equines in Iran.
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Ribeiro M, Gomes-Gonçalves S, Moreira G, Cardoso L, and Mesquita JR
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- Animals, Iran, Horses, Feces parasitology, Horse Diseases parasitology, Horse Diseases diagnosis
- Abstract
The life-cycle of the parasitic forms of Halicephalobus gingivalis is yet to be fully understood. In cases where there is evidence to support the presence of eggs from this parasite or its DNA in the faeces of equines, a thorough investigation of the clinical status and gastro-intestinal tract of the affected animals is warranted, as well as detailed descriptions of the employed coprological technique. Since reports of the identification of H. gingivalis eggs in faeces are sparse, objective measurements and high-quality images must be provided, in order to ensure optimal criteria for classification. Regarding research concerning H. gingivalis, no piece of information should be regarded as superfluous., (© 2024. The Author(s), under exclusive licence to Springer Nature B.V.)
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- 2024
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13. Detection of Enterocytozoon bieneusi in Non-Human Primates in Portuguese Zoos.
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Moreira G, Cruz AVS, Santos-Silva S, Moreira RSS, and Mesquita JR
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Enterocytozoon bieneusi , an intracellular eukaryote closely related to fungi, is recognized as a significant pathogen affecting humans, particularly those with compromised immune systems. While its transmission routes are still not fully elucidated, fecal-oral transmission remains the primary one. With a wide host range, the zoonotic potential of E. bieneusi is a concern, albeit direct evidence of animal-to-human transmission remains scarce. Genotyping based on the internal transcribed spacer (ITS) region facilitates the delineation of genetic diversity, with potentially zoonotic genotypes predominantly associated with Groups 1 and 2. Despite the broad spectrum of susceptible animal hosts, research into microsporidian infection among zoo animals remains limited. This study aimed to evaluate the occurrence of E. bieneusi infection across diverse captive animals, focusing on zoo settings in Portugal. Fecal samples were collected from a variety of animals, and molecular detection of E. bieneusi was conducted using nested PCR targeting the ITS region. Of 127 fecal samples, 1.57% (95% CI: 0.19-5.57) tested positive for E. bieneusi , with non-human primates (NHP's) exhibiting an 18.18% (95% CI: 2.28-51.78) occurrence. Phylogenetic analysis revealed clustering within Group 2 genotypes, indicating potential zoonotic implications. This study highlights the need for further research to understand the epidemiology of E. bieneusi in zoo environments and its potential transmission pathways to humans., Competing Interests: The authors declare no conflicts of interest.
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- 2024
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14. Postoperative pain after single-visit root canal treatments in necrotic teeth comparing instruments' kinematics and apical instrumentation limits - a prospective randomized multicenter clinical trial.
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Machado R, Moreira G, Comparin D, Barroso AP, Nascimento J, Ferraz CCR, Ignácio SA, da Fonseca Roberti Garcia L, Amaral RR, Shadid D, and da Silva Neto UX
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- Humans, Prospective Studies, Biomechanical Phenomena, Pain, Postoperative etiology, Pain, Postoperative epidemiology, Dental Pulp Cavity surgery, Root Canal Preparation
- Abstract
Objectives: This prospective randomized multicenter clinical trial (PRMCT) investigated postoperative pain after single-visit root canal treatments in teeth affected by pulp necrosis (PN), and asymptomatic apical periodontitis (AAP) (with apical radiolucent areas) or normal periradicular tissues (without apical radiolucent areas) comparing different instruments' kinematics and apical instrumentation limits., Methods: Before chemomechanical preparation, 240 patients/teeth were randomly distributed into four groups (n = 60) according to the instruments' kinematics (rotary or reciprocating) and apical instrumentation limits (with or without intentional foraminal enlargement [IFE]). After that, specimens were submitted to the same irrigation and obturation techniques, and the patients were referred to undergo the definitive restorations. No medication was prescribed, but the patients were instructed to take either paracetamol (750 mg every 6 h for three days) or ibuprofen (600 mg every 6 h for three days) in pain cases. Postoperative pain incidence and levels were assessed at 24-, 48-, and 72 h following treatment completion according to a verbal rating scale (VRS) following a score. The Kolmogorov-Smirnov test was applied to assess the normality of the data. Mann-Whitney U, Chi-square, Friedman's ANOVA, and Friedman's multiple 2 to 2 comparison tests were employed to identify potential significant statistical differences among the variables in the study groups (P < .05)., Results: Significant statistical differences were only observed among the groups considering tooth, periradicular status, and the occurrence of overfilling (sealer extrusion) (P < 0.00). Patients with teeth instrumented through rotary kinematics and without IFE experienced lower rates of postoperative pain; however, this difference was relevant only at 24 h (P < 0.05)., Conclusions: Postoperative pain was lower after using a rotary file system (Profile 04) inserted up to the apical constriction (AC). However, this finding was just statistically meaningful at 24 h., Trial Registration: This PRMCT was approved by the Human Research Ethics Committee of the Paranaense University - UNIPAR, Francisco Beltrão, PR, Brazil (CAAE. 46,774,621.6.0000.0109) on 02/09/2021. It was registered at The Brazilian Registry of Clinical Trials - ReBEC (RBR-3r967t) on 01/06/2023, was performed according to the Principles of the Helsinki Declaration and is reported following the Consolidated Standards of Reporting Trials Statement., (© 2024. The Author(s).)
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- 2024
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15. Long-term survival following unilateral lung transplantation for end-stage silicosis relative to idiopathic pulmonary fibrosis.
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Perin FA, Altmayer S, Nascimento DZ, Moreira-Hetzel G, Camargo SM, Hochhegger B, Sidney Filho LA, Camargo JJ, and Watte G
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- Humans, Idiopathic Pulmonary Fibrosis surgery, Lung Transplantation, Silicosis surgery
- Published
- 2022
- Full Text
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16. A new methodology for patient education in total knee arthroplasty: a randomized controlled trial.
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Percope de Andrade MA, Moreira de Abreu Silva G, de Oliveira Campos TV, Guen Kasuya Barbosa D, da Silva Leite D, Teodoro Rezende MV, Maciel Santos F, and Galo Magalhaes TF
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- Humans, Knee Joint surgery, Patient Education as Topic, Range of Motion, Articular, Treatment Outcome, Arthroplasty, Replacement, Knee, Osteoarthritis, Knee surgery
- Abstract
Background: We established a method in which patients are instructed before total knee arthroplasty (TKA) in a differentiated way without the necessity of reading any self-orientation, which can be applied even for illiterate patients METHODS: We developed a multidisciplinary approach to improve patient education in TKA comprising of a differentiated orientation conducted by an orthopedic surgeon, a nurse and a physiotherapist. It consists of standardized lectures regarding on pre-, intra- and postoperative issues in a randomized controlled trial of 79 consecutive patients undergoing primary TKA. Thirty-four patients received the standard education (control group), and 45 patients received the differentiated education (intervention group). The patients were evaluated during at least 6 months., Results: After a 6-month follow-up period, the Short Form Health Survey (SF-36), the Western Ontario and McMaster Universities Osteoarthritis Index (WOMAC), the visual analogue pain scale (VAS) and knee range of motion (ROM) improved significantly in both groups. Range of motion was better in the intervention group (mean and SD-106.9 ± 5.7 versus 92.5 ± 12.1 degrees, p = 0.02). Moreover, walk ability (more than 400 m) was better in the intervention group compared with the control group (97.4% versus 72.4%, p = 0.003). In the intervention and control groups, respectively, 10.5% and 31% of patients reported the need for some walking devices (p = 0.03)., Conclusions: A differentiated educational program with a multidisciplinary team had a positive impact on functional outcomes, improving ROM and walk ability of patients undergoing TKA in a short-term evaluation., (© 2021. The Author(s), under exclusive licence to Springer-Verlag France SAS, part of Springer Nature.)
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- 2022
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17. [Images in medicine. Multiple brain abscess ].
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Oliveira AP, Moreira G, Araújo B, and Carvalho JB
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- Anti-Infective Agents therapeutic use, Brain Abscess drug therapy, Cefepime, Cephalosporins therapeutic use, Humans, Magnetic Resonance Imaging, Male, Metronidazole therapeutic use, Middle Aged, Tomography, X-Ray Computed, Brain Abscess diagnosis
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- 2005
- Full Text
- View/download PDF
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