31 research outputs found

    Clinical Psychology and the COVID-19 Pandemic: A Mixed Methods Survey Among Members of the European Association of Clinical Psychology and Psychological Treatment (EACLIPT)

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    Background: The COVID-19 pandemic has affected people globally both physically and psychologically. The increased demands for mental health interventions provided by clinical psychologists, psychotherapists and mental health care professionals, as well as the rapid change in work setting (e.g., from face-to-face to video therapy) has proven challenging. The current study investigates European clinical psychologists and psychotherapists' views on the changes and impact on mental health care that occurred due to the COVID-19 pandemic. It further aims to explore individual and organizational processes that assist clinical psychologists' and psychotherapists' in their new working conditions, and understand their needs and priorities. Method: Members of the European Association of Clinical Psychology and Psychological Treatment (EACLIPT) were invited (N = 698) to participate in a survey with closed and open questions covering their experiences during the first wave of the pandemic from June to September 2020. Participants (n = 92) from 19 European countries, mostly employed in universities or hospitals, completed the online survey. Results: Results of qualitative and quantitative analyses showed that clinical psychologists and psychotherapists throughout the first wave of the COVID-19 pandemic managed to continue to provide treatments for patients who were experiencing emotional distress. The challenges (e.g., maintaining a working relationship through video treatment) and opportunities (e.g., more flexibleflexibleflexibleworking hours) of working through this time were identified. Conclusions: Recommendations for mental health policies and professional organizations are identified, such as clear guidelines regarding data security and workshops on conducting video therapy

    Borophosphate — eine vernachlässigte Verbindungsklasse: die Kristallstrukturen von M<sup>II</sup>[BPO<sub>5</sub>] (M<sup>II</sup> = Ca, Sr) und Ba<sub>3</sub>[BP<sub>3</sub>O<sub>12</sub>]

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    BO4- und PO4-Tetraeder, die über gemeinsame Ecken miteinander verknüpft sind, bilden das Gerüst der Titelverbindungen. Ca[BPO5] und Sr[BPO5] kristallisieren im Stillwellit-Typ und enthalten Tetraeder-Anionenverbände math image[BPOmath image], die als cyclisch verzweigte Dreier-Einfachketten beschrieben werden können. In Ba3[BP3O12] liegen math imageTetraeder-Anionenverbände in Form von zweifach offen verzweigten Vierer-Einfachketten vor. Nach diesen Befunden und mit Blick auf bekannte Verknüpfungsprinzipien von Tetraedereinheiten ist zu erwarten, daß auch Borophosphate mit Schicht-, Gerüst- und Hohlraumstrukturen zugänglich sind

    Cis-elements required for the demethylation of the mouse M-lysozyme downstream enhancer

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    Borophosphates—A Neglected Class of Compounds: Crystal Structures of M<sup>II</sup>[BPO<sub>5</sub>] (M<sup>II</sup> = Ca, Sr) and Ba<sub>3</sub>[BP<sub>3</sub>O<sub>12</sub>]

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    Vertex-sharing BO4 and PO4 tetrahedra form the framework of the title compounds. Ca[BPO5] and Sr[BPO5] crystallize in the stillwellite structural type and contain tetrahedral chain anions math image[BPOmath image], which can be described as loop-branched “dreier” single chains. In Ba3[BP3O12] the math imagetetrahedral anions form “zweifach” open “vierer” single chains. Given these results and the known linking modes of tetrahedral units, it is expected that borophosphates with layered and framework structures, as well as microporous structures, can be found

    Functional interaction of an axin homolog, conductin, with beta-catenin, APC, and GSK3beta

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    Control of stability of beta-catenin is central in the wnt signaling pathway. Here, the protein conductin was found to form a complex with both beta-catenin and the tumor suppressor gene product adenomatous polyposis coli (APC). Conductin induced beta-catenin degradation, whereas mutants of conductin that were deficient in complex formation stabilized beta-catenin. Fragments of APC that contained a conductin-binding domain also blocked beta-catenin degradation. Thus, conductin is a component of the multiprotein complex that directs beta-catenin to degradation and is located downstream of APC. In Xenopus embryos, conductin interfered with wnt-induced axis formation
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