6 results on '"Ferreira, Luis M."'
Search Results
2. Outcome and quality of life after endovascular abdominal aortic aneurysm repair in octogenarians.
- Author
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Pol, Robert A., Zeebregts, Clark J., van Sterkenburg, Steven M. M., Ferreira, Luis M., Goktay, Yigit, and Reijnen, Michel M. P. J.
- Abstract
Objective This study determined outcome and quality of life (QOL) in octogenarians, compared with patients aged <80 years, 1 year after endovascular aortic aneurysm repair (EVAR). Methods From March 2009 until April 2011, 1263 patients in the Endurant Stent Graft Natural Selection Global Postmarket Registry (ENGAGE) registry with an abdominal aortic aneurysm were treated with EVAR using the Endurant endograft (Medtronic Cardiovascular, Santa Rosa, Calif). The patients were grouped according to those aged ≥80 years (290 [22.9%]) and those aged <80 years (973 [77.1%]) at the time of the procedure. QOL was assessed using composite EuroQoL 5-Dimensions Questionnaire (EQ-5D) index scores. Baseline, perioperative, and follow-up data were analyzed at 1 year. Results Octogenarians had poorer anatomic characteristics. The technical success rate was almost 99% for both cohorts, with no deaths. The duration of the implant procedure was significantly longer in the elderly patients (P = .002), with significant differences in overall (P < .001) and postprocedure (P < .001) hospital stays in favor of the younger group. At 1 year, there was a significant difference in all-cause mortality (P = .002) and in the number of major adverse events (P = .003), including secondary rupture (P = .01), to the detriment of octogenarians. There were no significant differences in conversion to open surgery or in overall secondary endovascular procedures. The octogenarians scored lower in their overall health care perception (P < .001) but with no significant difference in the EQ-5D index. Compared with the group aged <80 years, they had still not completely recovered their QOL after 1 year (P = .01). Conclusions Octogenarians are more difficult to treat by EVAR than younger patients due to poorer anatomic suitability and a higher incidence of complications. Recovery of QOL in octogenarians takes longer (>12 months) than expected. [ABSTRACT FROM AUTHOR]
- Published
- 2014
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3. Fenestrated endovascular aortic aneurysm repair promotes positive infrarenal neck remodeling and greater sac shrinkage compared with endovascular aortic aneurysm repair.
- Author
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Teter, Katherine, Li, Chong, Ferreira, Luis M., Ferrer, Miguel, Rockman, Caron, Jacobowitz, Glenn, Cayne, Neal, Garg, Karan, and Maldonado, Thomas S.
- Abstract
Endovascular aortic aneurysm repair (EVAR) has become the standard of care for abdominal aortic aneurysms (AAAs) in the modern era. Although numerous devices exist for standard infrarenal AAA repair, fenestrated EVAR (fEVAR) offers a minimally invasive alternative to traditional open repair for patients with a short infrarenal neck. Over time, aortic neck dilation can occur, leading to loss of the proximal seal, endoleaks, and AAA sac growth. In the present study, we analyzed aortic remodeling after EVAR vs fEVAR and further evaluated whether fEVAR confers a benefit in terms of sac shrinkage. A retrospective review of prospectively collected data from 120 patients who had undergone EVAR was performed. Of these 120 patients, 30 had been treated with fEVAR (Zenith fenestrated; Cook Medical Inc, Bloomington, IN) and 90 patients were treated with EVAR devices (30 each with Endurant [Medtronic, Dublin, Ireland], Excluder [W.L. Gore & Associates, Flagstaff, AZ], and Zenith [Cook Medical Inc]). The demographic data were recorded. Also, anatomic measurements were performed for each patient preoperatively, at 30 days postoperatively, and at the longest follow-up point using three-dimensional reconstruction software. No significant differences were found in demographic data between the four groups. fEVAR had been used more often in aortas with large necks and irregular morphology (P =.004). At the longest follow-up, the suprarenal aorta encompassing 5, 10, and 15 mm above the lowest renal artery had dilated the most for the fEVAR group vs all EVAR groups. However, the infrarenal segment had tended to increase the least, or to even have regressed, for fEVAR compared with all three EVAR groups and was associated with the overall greatest proportion of sac shrinkage for the fEVAR group compared with the Medtronic, Gore, and Cook devices (−13.90% vs −5.75% vs −2.31% vs −4.68%, respectively; P =.025). Compared with EVAR, the patients treated with fEVAR had experienced greater suprarenal dilation over time, consistent with an overall greater burden of disease in the proximal native aorta. However, the infrarenal segment had dilated significantly less over time in the fEVAR group compared with all three EVAR groups, suggesting that fEVAR might stabilize the infrarenal neck, promoting positive sac remodeling, which was evidenced by the greatest degree of decrease in the largest AAA diameter in the fEVAR group. [ABSTRACT FROM AUTHOR]
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- 2022
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4. Fenestrated EVAR Promotes Positive Infrarenal Neck Remodeling Leading to Greater Sac Shrinkage Compared With EVAR.
- Author
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Teter, Katherine, Li, Chong, Ferreira, Luis M., Ferrer, Miguel, Rockman, Caron B., Cayne, Neal S., Garg, Karan, and Maldonado, Thomas S.
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- 2021
- Full Text
- View/download PDF
5. The Family 6 Carbohydrate Binding Module CmCBM6-2 Contains Two Ligand-binding Sites with Distinct Specificities.
- Author
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Henshaw, Joanna L., Bolam, David N., Pires, Virgínia M. R., Czjzek, Mirjam, Henrissat, Bernard, Ferreira, Luis M. A., Fontes, Carlos M. G. A., and Gilbert, Harry J.
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CARRIER proteins , *PROTEIN binding , *BIOLOGICAL transport , *CARBOHYDRATES , *CARBON cycle , *ENZYMES , *HYDROLYSIS , *CATALYSTS , *LIGANDS (Biochemistry) , *BINDING sites - Abstract
The microbial degradation of the plant cell wall is an important biological process, representing a major component of the carbon cycle. Enzymes that mediate the hydrolysis of this composite structure are modular proteins that contain non-catalytic carbohydrate binding modules (CBMs) that enhance catalytic activity. CBMs are grouped into sequence-based families, and in a previous study we showed that a family 6 CBM (CBM6) that interacts with xylan contains two potential ligand binding clefts, designated cleft A and cleft B. Mutagenesis and NMR studies showed that only cleft A in this protein binds to xylan. Family 6 CBMs bind to a range of polysaccharides, and it was proposed that the variation in ligand specificity observed in these proteins reflects the specific cleft that interacts with the target carbohydrate. Here the biochemical properties of the C-terminal cellulose binding CBM6 (CmCBM6-2) from Cellvibrio mixtus endoglucanase 5A were investigated. The CBM binds to the β1,4-β1,3-mixed linked glucans lichenan and barley β-glucan, cello-oligosaccharides, insoluble forms of cellulose, the β1,3-glucan laminarin, and xylooligosaccharides. Mutagenesis studies, informed by the crystal structure of the protein (presented in the accompanying paper, Pires, V. M. R., Henshaw, J. L., Prates, J. A. M., Bolam, D., Ferreira, L. M. A. Fontes, C. M. G. A., Henrissat, B., Planas, A., Gilbert, H. J., Czjzek, M. (2004) J. Biol. Chem. 279, 21560–21568), show that both cleft A and B can accommodate cello-oligosaccharides and laminarin displays a preference for cleft A, whereas xylooligosaccharides exhibit absolute specificity for this site, and the βl,4,-βl,3-mixed linked glucans interact only with cleft B. The binding of CmCBM6-2 to insoluble cellulose involves synergistic interactions between cleft A and cleft B. These data show that CmCBM6-2 contains two binding sites that display differences in ligand specificity, supporting the view that distinct binding clefts with different specificities can contribute to the variation in ligand recognition displayed by family 6 CBMs. This is in sharp contrast to other CBM families, where variation in ligand binding is a result of changes in the topology of a single carbohydrate-binding site. [ABSTRACT FROM AUTHOR]
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- 2004
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6. The Mechanisms by Which Family 10 Glycoside Hydrolases Bind Decorated Substrates.
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Pell, Gavin, Taylor, Edward J., Gloster, Tracey M., Turkenburg, Johan P., Fontes, Carlos M. G. A., Ferreira, Luis M. A., Nagy, Tibor, Clark, Samantha J., Davies, Gideon J., and Gilbert, Harry J.
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XYLANASES , *XYLANS , *PLANT cell walls , *X-ray crystallography , *URONIC acids , *BINDING sites , *HYDROLYSIS - Abstract
Endo-β-l,4-xylanases (xylanases), which cleave β-1,4 glycosidic bonds in the xylan backbone, are important components of the repertoire of enzymes that catalyze plant cell wall degradation. The mechanism by which these enzymes are able to hydrolyze a range of decorated xylans remains unclear. Here we reveal the threedimensional structure, determined by x-ray crystallography, and the catalytic properties of the Cellvibrio mixtus enzyme Xynl0B (CmXynl0B), the most active GH10 xylanase described to date. The crystal structure of the enzyme in complex with xylopentaose reveals that at the +1 subsite the xylose moiety is sandwiched between hydrophobic residues, which is likely to mediate tighter binding than in other GH10 xylanases. The crystal structure of the xylanase in complex with a range of decorated xylooligosaccharides reveals how this enzyme is able to hydrolyze substituted xylan. Solvent exposure of the O-2 groups of xylose at the +4, +3, + 1, and -3 subsites may allow accommodation of the α-l,2linked 4-O-methyl-v-glucuronic acid side chain in glucuronoxylan at these locations. Furthermore, the uronic acid makes hydrogen bonds and hydrophobic interactions with the enzyme at the +1 subsite, indicating that the sugar decorations in glucuronoxylan are targeted to this proximal aglycone binding site. Accommodation of 3t-linked L-arabinofuranoside decorations is observed in the -2 subsite and could, most likely, be tolerated when bound to xylosides in -3 and +4. A notable feature of the binding mode of decorated substrates is the way in which the subsite specificities are tailored both to prevent the formation of ’dead-end’ reaction products and to facilitate synergy with the xylan degradation-accessory enzymes such as α-glucuronidase. The data described in this report and in the accompanying paper (Fujimoto, Z., Kaneko, S., Kuno, A., Kobayashi, H., Kusakabe, I., and Mizuno, H. (2004) J. Biol. Chem. 279, 9606–9614) indicate that the complementarity in the binding of decorated substrates between the glycone and aglycone regions appears to be a conserved feature of GH10 xylanases. [ABSTRACT FROM AUTHOR]
- Published
- 2004
- Full Text
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