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amyotrophic lateral sclerosis/protease
Veza se sprema u međuspremnik
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Serine proteases purified from sera of patients with amyotrophic lateral sclerosis (ALS) induce contrasting cytopathology in murine motoneurones to IgG.
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Affinity purified IgG from sera of patients with amyotrophic lateral sclerosis (ALS) is claimed to enhance transmitter release, induce apoptotic death of cultured motoneurones, and elicit a distinctive cytopathology with raised Ca(2+) in mouse motoneurones. An alternative hypothesis attributes these
Occurrence of reduced alpha 2-macroglobulin and lowered protease inhibiting capacity in plasma of amyotrophic lateral sclerosis patients.
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Lowered levels of plasma alpha 2-macroglobulin were found in 13 patients with amyotrophic lateral sclerosis using anti-alpha 2-macroglobulin-embedded agar plates. Levels of this major protease inhibitor in ALS patients were contrasted with those in disease controls, consisting of patients with a
Protease-resistant SOD1 aggregates in amyotrophic lateral sclerosis demonstrated by paraffin-embedded tissue (PET) blot.
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OBJECTIVE
The paraffin-embedded tissue (PET) blot technique followed by limited protease digestion has been established to detect protein aggregates in prion diseases, alpha-synucleopathies, and tauopathies. We analyzed whether the scope of the method can be extended to analyze aggregates in mouse
Cytoplasmic, lysosomal and matrix protease activities in spinal cord tissue from amyotrophic lateral sclerosis (ALS) and control patients.
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The histological identification of ubiquitin-conjugated protein deposits in spinal motor neurones of patients with amyotrophic lateral sclerosis (ALS) has suggested that an underlying abnormality of intracellular protein metabolism may be responsible for the pathogenesis of the disease. In an
Studies of protease inhibitors in the sera of patients with amyotrophic lateral sclerosis.
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Serum levels of 4 protease inhibitors, alpha-1-antitrypsin, C1-inactivator, alpha-2-macroglobulin and antithrombin-III were measured in 11 patients with amyotrophic lateral sclerosis (6 males and 5 females) and a control group without neurologic disease. Our results indicated no significant
Serpin=serine protease-like complexes within neurofilament conglomerates of motoneurons in amyotrophic lateral sclerosis.
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Neurofilamentous conglomerates (NfCg), as axonal spheroids or conglomerates in motoneurons, are the histopathologic hallmarks for early stages of amyotrophic lateral sclerosis (ALS). We hypothesize that NfCg may be formed by post-translational modifications of altered Nf proteins that include: (1)
Brain Protease Activated Receptor 1 Pathway: A Therapeutic Target in the Superoxide Dismutase 1 (SOD1) Mouse Model of Amyotrophic Lateral Sclerosis.
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Glia cells are involved in upper motor neuron degeneration in amyotrophic lateral sclerosis (ALS). Protease activated receptor 1 (PAR1) pathway is related to brain pathologies. Brain PAR1 is located on peri-synaptic astrocytes, adjacent to pyramidal motor neurons, suggesting possible involvement in
Epitope mapping of antibodies against TDP-43 and detection of protease-resistant fragments of pathological TDP-43 in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.
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TAR DNA-binding protein of 43 kDa (TDP-43) is the major component of the intracellular inclusions in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Here, we show that both monoclonal (60019-2-Ig) and polyclonal (10782-2-AP) anti-TDP-43 antibodies recognize amino
Muscle acid protease activity in amyotrophic lateral sclerosis: correlation with clinical and pathologic features.
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Acid protease activity was increased in skeletal muscle of patients with ALS. The highest levels of activity were found in individuals with the clinically and histologically most affected muscle. High levels of proteolytic activity correlated with the extent of muscle atrophy, the presence of target
Concurrent variably protease-sensitive prionopathy and amyotrophic lateral sclerosis.
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Differential expression of 14 genes in amyotrophic lateral sclerosis spinal cord detected using gridded cDNA arrays.
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In order to obtain insight into the aetiology and pathogenesis of amyotrophic lateral sclerosis (ALS), high-density gene discovery arrays (GDA human version 1.2) containing 18 400 non-redundant EST cDNAs pooled from different tissue libraries have been used to monitor gene expression in lumbar
MALDI imaging of post-mortem human spinal cord in amyotrophic lateral sclerosis.
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Amyotrophic lateral sclerosis (ALS) is a devastating, rapidly progressing disease of the central nervous system that is characterized by motor neuron degeneration in the brainstem and the spinal cord. Matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry is an emerging
A role for the urokinase-type plasminogen activator system in amyotrophic lateral sclerosis.
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There is substantial evidence, implicating extracellular matrix (ECM) regulating enzymes in the pathogenesis of motor neuron degeneration in amyotrophic lateral sclerosis (ALS). The most important ECM-degrading proteases are serine proteases (plasminogen activators, PA) and matrix metalloproteinases
Neutral protease in cerebrospinal fluid from patients with multiple sclerosis and other neurological diseases.
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Neutral protease activity was significantly elevated in the cerebro-spinal fluid of patients with multiple sclerosis (MS) in exacerbation and in the acute phase of acute viral meningoencephalitis (AME) compared with that of MS in remission, amyotrophic lateral sclerosis or psychosomatic disease.
Abnormal expression of a serine protease in human dystrophic muscle.
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The activities of serine protease in muscles from normal persons and from patients with progressive muscular and neuromuscular diseases have been determined. A significant increase in the level of serine protease was found in muscle of patients with Duchenne-type muscular dystrophy and with
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