Publications by authors named "Amar S Patel"

Objectives: The objective of this study was to study the interrelations of demoralization, depression, and resilience in patients with Parkinson disease, and, more specifically, to determine if higher resilience in patients with Parkinson disease is associated with lower demoralization, lower depression, or both.

Methods: Outpatients with Parkinson disease ( = 95) were assessed for demoralization, depression, and resilience, as well as sociodemographic, clinical, and treatment-related variables. Bivariable associations, standard regressions, linear regression with copula correction, and correspondence analysis were used to analyze the data.

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Objective: To determine the prevalence and associated features of demoralization in Parkinson disease (PD).

Methods: Participants with PD and controls were prospectively recruited from outpatient movement disorder clinics and the community. Demoralization was defined as scoring positively on the Diagnostic Criteria for Psychosomatic Research, Demoralization questionnaire or Kissane Demoralization Scale score ≥24.

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Background: Velopharyngeal dysfunction produces a nasal speech pattern because of the inability to close the nasal airway during speech, most often associated with anatomical abnormalities of the palate.

Case Report: We describe two cases of possible velopharyngeal dystonia, a task-specific movement disorder causing a speech pattern similar to velopharyngeal dysfunction. Both patients experienced treatment response with anticholinergic medication.

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Clinical Vignette: A 67-year-old female with advanced Parkinson's disease (PD), medically refractory tremor, and a history of significant depression presented for evaluation of deep brain stimulation (DBS) candidacy.

Clinical Dilemma: Traditionally, the subthalamic nucleus (STN) has been preferred over the globus pallidus interna (GPi) as a DBS target for PD patients with levodopa-responsive fluctuations in rigidity and akinesia, for whom tremor is also a significant source of impairment. However, STN stimulation is avoided in patients with a significant pre-surgical history of mood disorder.

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When increasing ambulation speed in Parkinson's disease, step cadence increases more than stride length, indicating movement scaling difficulties that affect step generation in particular. We investigated whether step length variation when increasing ambulation speed was related to disease progression. Patients with Parkinson's disease (N = 39) and controls (N = 152) performed two timed ambulation tasks: at a 'free' (self-selected) pace and then at 'maximal' speed.

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Mammalian thioredoxin reductase (TR) is a pyridine nucleotide disulfide oxidoreductase that uses the rare amino acid selenocysteine (Sec) in place of the more commonly used amino acid cysteine (Cys) in the redox-active tetrapeptide Gly-Cys-Sec-Gly motif to catalyze thiol/disulfide exchange reactions. Sec can accelerate the rate of these exchange reactions (i) by being a better nucleophile than Cys, (ii) by being a better electrophile than Cys, (iii) by being a better leaving group than Cys, or (iv) by using a combination of all three of these factors, being more chemically reactive than Cys. The role of the selenolate as a nucleophile in the reaction mechanism was recently demonstrated by creating a mutant of human thioredoxin reductase-1 in which the Cys497-Sec498 dyad of the C-terminal redox center was mutated to either a Ser497-Cys498 dyad or a Cys497-Ser498 dyad.

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In vitro protein folding of disulfide containing proteins is aided by the addition of a redox buffer, which is composed of a small molecule disulfide and/or a small molecule thiol. In this study, we examined redox buffers containing asymmetric dithiols 1-5, which possess an aromatic and aliphatic thiol, and symmetric dithiols 6 and 7, which possess two aromatic thiols, for their ability to fold reduced lysozyme at pH 7.0 and 8.

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The production of proteins using recombinant DNA technology often requires the use of in vitro protein folding. In order to facilitate in vitro protein folding, a redox buffer is added to the protein folding mixture. The redox buffer is composed of a small molecule disulfide and/or a small molecule thiol.

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