Familial Property
Mostrando 1-7 de 7 artigos, teses e dissertações.
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1. Perfil da propriedade contemporânea : (destaque da propriedade fundiária)
The author assesses the dialectics of property through the ages, of its radical denial, agent of corruption and of every wrong for society, and of its inconditional consecration, vital agent of liberty and achievement of man, while stressing that every society, whatever be its political regime, will have to deal with the discipline of relations among men abo
Publicado em: 2009
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2. Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants
Mutations in Cu, Zn superoxide dismutase (SOD1) cause the neurodegenerative disease familial amyotrophic lateral sclerosis from an as-yet-unidentified toxic property(ies). Analysis in Saccharomyces cerevisiae of a broad range of human familial amyotrophic lateral sclerosis–linked SOD1 mutants (A4V, G37R, G41D, H46R, H48Q, G85R, G93C, and I113T) reveals one
The National Academy of Sciences.
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3. Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant
Mutations in superoxide dismutase 1 (SOD1; EC 1.15.1.1) are responsible for a proportion of familial amyotrophic lateral sclerosis (ALS) through acquisition of an as-yet-unidentified toxic property or properties. Two proposed possibilities are that toxicity may arise from imperfectly folded mutant SOD1 catalyzing the nitration of tyrosines [Beckman, J. S.,
The National Academy of Sciences of the USA.
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4. A Common Property of Amyotrophic Lateral Sclerosis-associated Variants: DESTABILIZATION OF THE COPPER/ZINC SUPEROXIDE DISMUTASE ELECTROSTATIC LOOP*
At least 119 mutations in the gene encoding copper/zinc superoxide dismutase (SOD1) cause amyotrophic lateral sclerosis by an unidentified toxic gain of function. We compared the dynamic properties of 13 as-isolated, partially metallated, SOD1 variant enzymes using hydrogen-deuterium exchange. We identified a shared property of these familial amyotrophic lat
American Society for Biochemistry and Molecular Biology.
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5. Absence of neurofilaments reduces the selective vulnerability of motor neurons and slows disease caused by a familial amyotrophic lateral sclerosis-linked superoxide dismutase 1 mutant
Mutations in superoxide dismutase 1 (SOD1), the only proven cause of amyotrophic lateral sclerosis (ALS), provoke disease through an unidentified toxic property. Neurofilament aggregates are pathologic hallmarks of both sporadic and SOD1-mediated familial ALS. By deleting NF-L, the major neurofilament subunit required for filament assembly, onset and progres
The National Academy of Sciences.
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6. Fitzgerald Trait: Deficiency of a Hitherto Unrecognized Agent, Fitzgerald Factor, Participating in Surface-Mediated Reactions of Clotting, Fibrinolysis, Generation of Kinins, and the Property of Diluted Plasma Enhancing Vascular Permeability (PF/Dil)
The prolonged partial thromboplastin time observed in the plasma of a 71-yr-old asymptomatic man was related to the deficiency of a hitherto unrecognized agent. The patient's plasma also exhibited impaired surface-mediated fibrinolysis and esterolytic activity and impaired generation of kinins and of the property enhancing vascular permeability designated PF
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7. Inherited resistance to activated protein C is corrected by anticoagulant cofactor activity found to be a property of factor V.
Recently, our laboratory described a defect in anticoagulant response to activated protein C (APC). This response, APC resistance, was shown to be inherited and associated with familial thrombophilia. As other possible mechanisms were excluded, APC resistance was hypothesized to be due to deficiency of a previously unrecognized cofactor of APC. The aim of th