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1.
Mov Disord Clin Pract ; 11(3): 257-264, 2024 Mar.
Article in English | MEDLINE | ID: mdl-38468507

ABSTRACT

BACKGROUND: Parkinson's disease (PD) is associated with psychosocial distress that affects patients' quality of life. The distress thermometer (DT) is an 11-point visual analogue scale that is used as a screening tool for the assessment of psychosocial distress, originally developed for oncological diseases. OBJECTIVES: To validate the DT for PD and to explore contributing factors. METHODS: The DT scale was administered to 105 people with Parkinson's Disease (PwPD). Along with it, we assessed motor symptoms (Unified Parkinson's Disease Rating Scale part III [UPDRS III], Hoehn and Yahr-stage [H&Y]), non-motor symptoms (Non-motor Symptom Questionnaire [NMSQ]), anxiety and depression (Hospital Anxiety and Depression Scale [HADS], Fear of Progression-Questionnaire Short Form [FOP-Q-SF], Generalized Anxiety Disorder Scale-7 [GAD-7], 9-question Patient Health Questionnaire [PHQ-9]), the feeling of hope (Herth Hope Index [HHI]) and quality of life (Schedule for the Evaluation of Individual Quality of Life [SEIQoL]). RESULTS: With a cut-off of 4, the DT identified PwPD with distress with a sensitivity of 97% and a specificity of 38%. With this cut-off, the DT will yield false negative results in 1 out of 100 cases. Factor analyses and a random forest regression of the dataset revealed that distress can be predicted by two factors, which we termed "anxiety" and "depression/resilience/motor symptoms". CONCLUSION: The DT is an ultra-short and reliable screening tool for distress in PwPD. DT values below 4 rule out distress with a high degree of certainty. Anxiety and depression are important factors in distress but are counterbalanced by the individuals' psychological resilience.


Subject(s)
Parkinson Disease , Resilience, Psychological , Humans , Parkinson Disease/diagnosis , Depression/diagnosis , Quality of Life/psychology , Thermometers , Visual Analog Scale
2.
Biochem J ; 395(1): 31-7, 2006 Apr 01.
Article in English | MEDLINE | ID: mdl-16336192

ABSTRACT

The digestion of the plant cell wall requires the concerted action of a diverse repertoire of enzyme activities. An important component of these hydrolase consortia are arabinofuranosidases, which release L-arabinofuranose moieties from a range of plant structural polysaccharides. The anaerobic bacterium Clostridium thermocellum, a highly efficient plant cell wall degrader, possesses a single alpha-L-arabinofuranosidase (EC 3.2.1.55), CtAraf51A, located in GH51 (glycoside hydrolase family 51). The crystal structure of the enzyme has been solved in native form and in 'Michaelis' complexes with both alpha-1,5-linked arabinotriose and alpha-1,3 arabinoxylobiose, both forming a hexamer in the asymmetric unit. Kinetic studies reveal that CtAraf51A, in contrast with well-characterized GH51 enzymes including the Cellvibrio japonicus enzyme [Beylot, McKie, Voragen, Doeswijk-Voragen and Gilbert (2001) Biochem. J. 358, 607-614], catalyses the hydrolysis of alpha-1,5-linked arabino-oligosaccharides and the alpha-1,3 arabinosyl side chain decorations of xylan with equal efficiency. The paucity of direct hydrogen bonds with the aglycone moiety and the flexible conformation adopted by Trp(178), which stacks against the sugar at the +1 subsite, provide a structural explanation for the plasticity in substrate specificity displayed by the clostridial arabinofuranosidase.


Subject(s)
Clostridium thermocellum/enzymology , Glycoside Hydrolases/chemistry , Glycoside Hydrolases/metabolism , Binding Sites , Catalysis , Enzyme Stability , Glycoside Hydrolases/classification , Ligands , Models, Molecular , Protein Conformation , Substrate Specificity , Xylans/metabolism
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