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Wanneer het om het verbeteren van onze zorg gaat, telt de stem van elke patiënt. Door aandacht te schenken aan hoe een zorgtraject ervaren wordt, kun je als zorgverlener of onderzoeker ook je eigen werkpunten aanpakken. Dat perspectief wordt echter nog te vaak vergeten.In Van mens tot mens verklaren zes uiteenlopende getuigenissen hoe meer aandacht voor de beleving van patiënten in hun behandeling kan bijdragen tot een sterkere zorgsector. Het resultaat is een concreet stappenplan en een dagelijkse houvast voor zorgverleners.Dit boek is een pleidooi voor warmte en menselijkheid in een sector waar technische vooruitgang en efficiëntie soms de bovenhand nemen.(https://www.lannoo.be/nl/van-mens-tot-mens)

Kwaliteitszorg --- Gezondheidszorg --- zorgverlening --- Relatie cliënt --- Hulpverlening --- Interactie --- Zorgverlening --- Verbindende communicatie --- Verbindend werken --- Patiëntenparticipatie --- Buddy's --- Ethiek --- Zorg --- 614.25 --- kwaliteitszorg --- patiëntenzorg --- Sociology of health --- patiënt-verpleegkundige relatie --- arts-patiënt relatie --- arts-patiënt-verpleegkundige relatie --- Buddy --- Kwaliteitszorg ; gezondheidszorg --- Gezondheidszorg ; België

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Plants [Effect of nitrogen on ] --- Nitrogen fertilizers

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γ-Secretase complexes constitute a family of proteases first identified in Alzheimer's disease (AD) patients and involved in multiple signaling pathways. These unusual enzymes are embedded in the membrane where they cut consecutively several substrates, including the amyloid precursor protein (APP). Pathogenic mutations in the catalytic core of γ-secretase (PSEN), as well as, in APP cause early onset familial AD (FAD, <65 y). The fact that AD linked mutations are found both in the enzyme (PSEN/γ-secretase) and substrate (APP) that generate Aβ peptides strongly supports the amyloid cascade hypothesis, which proposes that AD is caused by an imbalance between Aβ peptides production and their clearance.Independently of the position and nature of the mutation in PSEN, all pathogenic substitutions exert a common impairment on γ-secretase processivity, which leads to production of longer, amyloidogenic Aβ peptides. Majority of pathogenic mutations in APP impact the aggregation properties of APP, either directly or indirectly, by affecting the carboxypeptidase like processing of APP resulting in longer Aβ peptides. Despite its relevance, an experimentally verified and internally consistent model explaining the effects of PSEN and APP pathogenic substitutions on γ-secretase function is lacking. Moreover, an increasing amount of data is emerging giving evidence for possible alterations of Aβ production in a subset of sporadic AD patients, further underlying the significance of deciphering the molecular basis of γ-secretase dysfunction.The rational of this PhD project is based on the high conformational plasticity and metastable fold of PSEN. We propose that PSEN structural flexibility resulting from the inefficient structural packing plays key roles in global activity and processivity of γ-secretase. Our goal is to decipher the molecular mechanisms and structural determinants underlying the pathogenic effects mediated by γ-secretase in both familial and sporadic forms of AD.

Presenile dementia --- Alzheimer's disease --- Academic collection