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Different approaches analyze the strength of a natural language argument in different ways. This paper contrasts the dialectical, structural, probabilistic (or Bayesian), computational, and empirical approaches by exemplarily applying them to a single argumentative text (Epicureans on Squandering Life; Aikin & Talisse, 2019). Rather than pitching these approaches against one another, our main goal is to show the room for fruitful interaction. Our focus is on a dialectical analysis of the squandering argument as an argumentative response that voids an interlocutor’s right to assertion. This analysis addresses the pragmatic dimensions of arguing and implies an argument structure that is consistent with empirical evidence of perceived argument strength. Results show that the squandering argument can be evaluated as a (non-fallacious) ad hominem argument, which however is not necessarily stronger than possible arguments attacking it.

In September 2018, the ArgDiaP association, along with colleagues from Germany and the UK, organised one of the longest and most interdisciplinary series of events ever dedicated to argumentation - Warsaw Argumentation Week, WAW 2018. The eleven-day ‘week’ featured a five day graduate school on computational and linguistic perspectives on argumentation (3rd SSA school); five workshops: on systems and algorithms for formal argumentation (2nd SAFA), argumentation in relation to society (1st ArgSoc), philosophical approaches to argumentation (1st ArgPhil), legal argumentation (2ndMET-ARG) and argumentation in rhetoric (1st MET-RhET); and two conferences: on computational models of argumentation (7th COMMA conference) and on argumentation and corpus linguistics (16th ArgDiaP conference). WAW hosted twelve tutorials and eight invited talks as well as welcoming over 130 participants. All the conferences and workshops publish pre- or post-proceedings in the top journals and book series in the field.

The paper presents the analysis of thermal processes occurring in thermal energy storage tanks used for heating hot water systems. Three-dimensional Computational Fluid Dynamics (CFD) methods were used. The standard buffer charging stage was modelled for three tank inlets’ diameters DN20, DN40 and DN80. With a constant charging water flow and temperature the port diameter affects inlet velocity, heat storage dynamics, thermal stratification and thermocline thickness in storage tank. The smallest diameter causes unfavourable thermal mixing of accumulated water, and the largest diameter supports thermal stratification

Immunoglobulin G (IgG) is the most abundant glycoprotein in human serum. All IgG subclasses have a single-conserved N-linked glycosylation site at Asn297 of the heavy chain and 10-30% of IgGs are N-glycosylated also in a Fab region. N-glycans of Fc are sialylated and fucosylated biantennary complex-type structures. Glycosylation plays a key role in antibody function, and IgG N-glycans are essential for the proper activity of the immune system. Fc glycans are important for IgG effector functions, whereas Fab oligosaccharides modulate antigen binding. Glycosylation changes of IgG are associated with the development of various human diseases, including autoimmune states. The modification of one sugar moiety in N-glycan structure may result in the stimulation or suppression of immune response. The lack of core fucose leads to the enhancement of pro-inflammatory activity, whereas an increase of sialylation determines immunosuppressive properties of IgG. The contribution of IgG Fc glycosylation changes has been demonstrated in the pathogenesis of rheumatoid arthritis, lupus erythematosus and Crohn's disease. A decrease in IgG galactosylation and sialylation, found in these diseases, activates effector cells and triggers inflammatory reactions. A detailed analysis of changes in IgG glycosylation and their effects on the development of autoimmune diseases is important in the treatment of these diseases. IgGs with modified a2,6-sialylation are used as therapeutic antibodies with anti-inflammatory properties. Numerous studies on IgG glycosylation have provided evidence of the role of this post-translational modification in the proper functioning of antibodies and the importance of changes in the structure of IgG glycans, mainly incomplete galactosylation and desialylation, in the pathogenesis of many diseases. The continuation of these studies may contribute to explaining the mechanisms of autoimmunity that is still poorly understood. [ABSTRACT FROM AUTHOR]