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Applied Semantics, International Summer School, APPSEM 2000, Caminha, Portugal, September 9-15, 2000, Advanced Lectures (LNCS 2395)
- 2002
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Samlingsverk (redaktörskap) (refereegranskat)abstract
- This book presents revised and extended versions of lectures given at an international summer school on applied semantics that took place in Caminha, Portugal in September. The nine lectures included present recent developments in programming language research in a coherent and systematic way. Among the topics addressed are - description of existing programming languages features - design of new programming languages features - implementation and analysis of programming languages - transformation and generation of programs - verification of programs.
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- Goldsteins, Gundars, et al.
(författare)
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Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants
- 1999
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 96:6, s. 3108-3113
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Tidskriftsartikel (refereegranskat)abstract
- The structural requirements for generation of amyloid from the plasma protein transthyretin (TTR) are not known, although it is assumed that TTR is partly misfolded in amyloid. In a search for structural determinants important for amyloid formation, we generated a TTR mutant with high potential to form amyloid. We demonstrated that the mutant represents an intermediate in a series of conformational changes leading to amyloid. Two monoclonal antibodies were generated against this mutant; each displayed affinity to ex vivo TTR and TTR mutants with amyloidogenic folding but not to wild-type TTR or mutants exhibiting the wild-type fold. Two cryptic epitopes were mapped to a domain of TTR, where most mutations associated with amyloidosis occur and which we propose is displaced at the initial phase of amyloid formation, opening up new surfaces necessary for autoaggregation of TTR monomers. The results provide direct biochemical evidence for structural changes in an amyloidogenic intermediate of TTR.
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- Gustavsson, Åsa
(författare)
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Transthyretin in senile systemic amyloidosis and familial amyloidotic polyneuropathy
- 1994
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- The amyloidoses comprise a heterogeneous group of disorders characterized by the deposition of fibrillar, proteinaceous amyloid deposits in various organs and tissues. To date, 17 different proteins of various sizes have been identified as amyloid proteins. Irrespective of the specific protein comprising the amyloid fibrils, the fibrils are all about 10 nm wide and of indefinite length.In the most common familial form of amyloidosis, familial amyloidotic polyneuropathy (FAP), the amyloid fibril protein is the plasma protein transthyretin (TTR). In FAP type I, which is the type found in Sweden, there is a mutation in the TTR gene leading to the substitution of a methionine for valine at position 30. This mutation leads to a form of amyloidosis characterized by polyneuropathy starting in the lower limbs and usually slowly progressing until death occurs. Another TTR-derived form of amyloidosis is senile systemic amyloidosis (SSA). This form of amyloidosis is present in about 25% of people 80 years of age or older. In SSA, amyloid is deposited mainly in the heart but deposits are also found in many other organs.In this study it is demonstrated that normal TTR can form fibrils in vitro. Fibril formation studies were also performed in vitro with synthetic peptides corresponding to parts of the TTR amino acid sequence. These results indicate that TTR peptides with 13-strand secondary structure are fibrillogenic in vitro and are likely important in in vivo amyloidogenesis.The TTR amino acid and DNA sequences in cases with SSA were determined and found to be normal, thus showing that no mutation is necessary for development of this form of amyloidosis. However, cleavage of TTR may be important in fibrillogenesis since TTR fragments lacking 45-51 N-terminal amino acid residues predominated in the amyloid.Antigenic epitopes exposed on normal TTR and TTR derived from amyloid deposits were also examined. The 13-strand H was found to be exposed in amyloid TTR and not in normal TTR, thus suggesting a changed structural conformation of TTR in amyloid fibrils.
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- Mendes, Emilia, et al.
(författare)
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Using Bayesian Network to Estimate the Value of Decisions within the Context of Value-Based Software Engineering : A Multiple Case Study
- 2019
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Ingår i: International journal of software engineering and knowledge engineering. - : World Scientific Publishing Co. Pte Ltd. - 0218-1940. ; 29:11-12, s. 1629-1671
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Tidskriftsartikel (refereegranskat)abstract
- Companies must make a paradigm shift in which both short- and long-term value aspects are employed to guide their decision-making. Such need is pressing in innovative industries, such as ICT, and is the core of Value-based Software Engineering (VBSE). Objective: This paper details three case studies where value estimation models using Bayesian Network (BN) were built and validated. These estimation models were based upon value-based decisions made by key stakeholders in the contexts of feature selection, test cases execution prioritization, and user interfaces design selection. Methods: All three case studies were carried out according to a Framework called VALUE - improVing decision-mAking reLating to software-intensive prodUcts and sErvices development. This framework includes a mixed-methods approach, comprising several steps to build and validate company-specific value estimation models. Such a building process uses as input data key stakeholders' decisions (gathered using the Value tool), plus additional input from key stakeholders. Results: Three value estimation BN models were built and validated, and the feedback received from the participating stakeholders was very positive. Conclusions: We detail the building and validation of three value estimation BN models, using a combination of data from past decision-making meetings and also input from key stakeholders. © 2019 World Scientific Publishing Company.
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- Paulsson, Johan F, et al.
(författare)
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There is a role for proIAPP in islet amyloid fibrillogenesis
- 2008
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Annan publikation (övrigt vetenskapligt/konstnärligt)abstract
- Islet amyloid polypeptide (IAPP) can aggregate into amyloid, a common pathological finding present extracellularly in the islets of Langerhans in individuals with type 2 diabetes. IAPP arises from posttranslational processing of the precursor proIAPP. Accumulation of proIAPP in the secretory granules can result in proIAPP-amyloid formation. We raise the following hypothesis; proIAPP can under not yet defined circumstances aggregate into amyloid-like fibrils intracellularly and at this location act as template and cross-seed amyloid formation of IAPP. We have produced recombinant peptides corresponding to proIAPP and IAPP. These peptides aggregate readily into fibrils with typical amyloid characteristics. Sonicated recproIAPP- and recIAPP- preformed fibrillar aggregates were injected intravenously to +/hIAPP/-mIAPP transgenic mice. Male mice from this strain develop islet amyloid in response to high fat diet. Control animals received an injection of preformed amyloid fibrils from the proinsulin processing intermediate (C-peptide/A-chain) or sodium chloride. All animals were fed a diet high in fat over a ten month period. The presence of islet amyloid was studied after Congo red staining. We found amyloid in 20 % of the islets in animals injected with preformed recIAPP fibrils and in 10 % of the islets in animals injected with preformed recproIAPP fibrils. Control animals developed amyloid in 1-2% of the islets. Our results support the hypothesis that proIAPP-fibrils can act as template and induce conformational changes in soluble IAPP that results in propagation of the amyloid fibrils. This is the first report on in vivo seeding of a localized amyloid form and we present data that support transport of amyloid between islets as a putative route for the spreading of islet amyloid. Our finding suggests that therapies, which use capping of fibril endings, might be useless.
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- Saraiva, Joao, et al.
(författare)
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Farming Fish
- 2022
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Ingår i: Routledge Handbook of Animal Welfare. - London : Routledge. - 9781032022062 ; , s. 115-127
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Bokkapitel (refereegranskat)abstract
- Fishes in aquaculture face several potential challenges that may affect their welfare. These challenges may be ethological (spatial, social, reproductive, feeding), physiological (homeostasis and health issues including disease and parasites), environmental (water quality and characteristics, light, complexity) and human-induced (operations and routines, stunning and slaughter). We review the major issues that affect welfare for each of the main aquaculture fish systems used for farming fishes. Given the plethora of welfare challenges, we propose that the species chosen for farming should have an amenable life history and behavioural profile that make them suitable for farming conditions.
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