657 research outputs found
Supplemental Material - Resveratrol and lycopene ameliorate contrast-induced nephropathy in a rabbit model
Supplemental Material for Resveratrol and lycopene ameliorate contrast-induced nephropathy in a rabbit model by Eirini Fragkiadoulaki, Aristides Tsatsakis, Dragana Nikitovic, Georgios Georgiadis, Alexandra Kalogeraki, Konstantinos Kaloudis, Athanasios Alegkakis, Vasiliki Karzi and Charalampos Mamoulakis in Human & Experimental Toxicology</p
Supplemental Material—Risk of recurrent thromboembolic events according to treatment duration in patients with superficial vein thrombosis treated with intermediate dose of tinzaparin
Supplementary Material for Risk of recurrent thromboembolic events according to treatment duration in patients with superficial vein thrombosis treated with intermediate dose of tinzaparin by Christos Karathanos, Stavros K Kakkos, Georgios Georgiadis, Christos Ioannou, Spyros Vasdekis, Dimitrios Chatzis, Panagiotis Latzios, and Athanasios D Giannoukas On Behalf of the SeVEN Collaborators in Phlebology.</p
Critical role of interdomain interactions in the conformational change and catalytic mechanism of endoplasmic reticulum aminopeptidase 1
Endoplasmic reticulum aminopeptidase 1 (ERAP1) is an intracellular enzyme that is important for the generation of antigenic epitopes and major histocompatibility class I-restricted adaptive immune responses. ERAP1 processes a vast variety of different peptides but still shows length and sequence selectivity, although the mechanism behind these properties is poorly understood. X-ray crystallographic analysis has revealed that ERAP1 can assume at least two distinct conformations in which C-terminal domain IV is either proximal or distal to active site domain II. To improve our understanding of the role of this conformational change in the catalytic mechanism of ERAP1, we used site-directed mutagenesis to perturb key salt bridges between domains II and IV. Enzymatic analysis revealed that these mutations, although located away from the catalytic site, greatly reduce the catalytic efficiency and change the allosteric kinetic behavior. The variants were more efficiently activated by small peptides and bound a competitive inhibitor with weaker affinity and faster dissociation kinetics. Molecular dynamics analysis suggested that the mutations affect the conformational distribution of ERAP1, reducing the population of closed states. Small-angle X-ray scattering indicated that both the wild type and the ERAP1 variants are predominantly in an open conformational state in solution. Overall, our findings suggest that electrostatic interactions between domains II and IV in ERAP1 are crucial for driving a conformational change that regulates the structural integrity of the catalytic site. The extent of domain opening in ERAP1 probably underlies its specialization for antigenic peptide precursors and should be taken into account in inhibitor development efforts.</p
ABSENCE OF ANOMALOUS DISSIPATION FOR WEAK SOLUTIONS OF THE MAXWELL–STEFAN SYSTEM
In this paper we give a short and self-contained proof of the fact that weak solutions to the Maxwell-Stefan system automatically satisfy an entropy equality, establishing the absence of anomalous dissipation
The Δρομοδείχτης της Ελλάδος of 1824 and Athanasios Stageirites (Τίτλος περίληψης)
σ. [281]-290Κείμενο στα ελληνικά με περίληψη στα αγγλικά με τον τίτλο: The Δρομοδείχτης της Ελλάδος of 1824 and Athanasios StageiritesThe article first examines the close relationship between the publication “Δρομοδείχτης της Ελλάδος” [1824] and the publication “Ηπειρωτικά” (1819) by Athanasios Stageirites and then suggests that Athanasios Stageirites is the likeliest author of the “Δρομοδείχτης της Ελλάδος”.Δωδώνη: Τεύχος Πρώτο: επιστημονική επετηρίδα του Τμήματος Ιστορίας και Αρχαιολογίας της Φιλοσοφικής Σχολής του Πανεπιστημίου Ιωαννίνων; Τόμ. 43-44 (2014-2015
Crystal structure of insulin-regulated aminopeptidase with bound substrate analogue provides insight on antigenic epitope precursor recognition and processing
Aminopeptidases that generate antigenic peptides influence immunodominance and adaptive cytotoxic immune responses. The mechanisms that allow these enzymes to efficiently process a vast number of different long peptide substrates are poorly understood. In this work, we report the structure of insulin-regulated aminopeptidase, an enzyme that prepares antigenic epitopes for crosspresentation in dendritic cells, in complex with an antigenic peptide precursor analog. Insulin-regulated aminopeptidase is found in a semiclosed conformation with an extended internal cavity with limited access to the solvent. The N-terminal moiety of the peptide is located at the active site, positioned optimally for catalysis, whereas the C-terminal moiety of the peptide is stabilized along the extended internal cavity lodged between domains II and IV. Hydrophobic interactions and shape complementarity enhance peptide affinity beyond the catalytic site and support a limited selectivity model for antigenic peptide selection that may underlie the generation of complex immunopeptidomes.</p
Dataset in support of the Southampton doctoral thesis 'The boatbuilding tradition of the Aegean during the Late Neolithic – Early Bronze Age periods. Typological classification, digital reconstruction and seakeeping assessment'
Dataset in support of the Southampton doctoral thesis 'The boatbuilding tradition of the Aegean during the Late Neolithic – Early Bronze Age periods. Typological classification, digital reconstruction and seakeeping assessment' Appendix D - Resistance data and Appendix C - Stability data.
This dataset is focused on two appendices:
Appendix D - Resistance data. D.1 Resistance data produced by the author via MAXSURF Resistance for this thesis.
Appendix C - Stability data
C1. Stability data – STIX and ISO criteria, produced by the author via MAXSURF Stability software for his thesis
This research was funded by Southampton Marine and Maritime Institute (SMMI), Vice-Chancellor's Scholarship, Greek Archaeological Committee UK (GACUK)
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Alignment via Friction for Nonisothermal Multicomponent Fluid Systems
The derivation of an approximate Class–I model for nonisothermal multicomponent systems of fluids, as the high-friction limit of a Class–II model is justified, by validating the Chapman–Enskog expansion performed from the Class–II model towards the Class–I model. The analysis proceeds by comparing two thermomechanical theories via relative entropy.Research partially supported by King Abdullah University of Science and Technology (KAUST) baseline funds. The first author acknowledges partial support from the Austrian Science Fund (FWF), grants P33010 and F65. This work has received funding from the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme, ERC Advanced Grant no. 101018153
<i>H<sup>p</sup></i>-bounds for spectral multipliers on Riemannian manifolds
AbstractLet M be a Riemannian manifold which satisfies the doubling volume property. Let Δ be the Laplace–Beltrami operator on M and m(λ), λ∈R, a multiplier satisfying the Mikhlin–Hörmander condition. We also assume that the heat kernel satisfies certain upper Gaussian estimates and we prove that there is a geometric constant p0<1, such that the spectral multiplier m(Δ) is bounded on the Hardy spaces Hp for all p∈(p0,1]
Modellierung und Analysis von Multikomponentensystemen für Gasmischungen
The aim of this thesis is to understand and analyze diffussive and thermal effects in multicomponent systems for gas mixtures through the perspective of partial differential equations. Starting from Class–II models of thermodynamics,diffusion equations are derived formally by a Chapman–Enskog expansion and the expansion is justified as a relaxation limit by means of the relative entropy method.Das Ziel dieser Arbeit ist das Verständnis und die Analyse von diffusiven und thermischen Effekten in Mehrkomponentensystemen für Gasgemische aus der Perspektive partieller Differentialgleichungen. Ausgehend von Klasse-II-Modellen der Thermodynamik,werden Diffusionsgleichungen formal durch eine Chapman-Enskog-Erweiterung abgeleitet und die Expansion wird als Relaxationsgrenze mit Hilfe der Methode der relativen Entropie Methode begründet
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