496 research outputs found
Kulonbozo oktatasi rendszerek es formak kozotti tudastranszfer es annak merhetosege
Az informáciĂł megszerzĂ©se Ă©s átadása sohasem volt olyan nagy jelentĹ‘sĂ©gű mint napjainkban. Aki a legfrissebb, legmagasabb szintű informáciĂłval rendelkezik az elĹ‘nyre tesz versenytársaival szemben. Igy Ă©rthetĹ‘, hogy a gazdaság Ă©s az erĹ‘södĹ‘ piaci verseny egyre nagyobb nyomást gyakorol az oktatási intĂ©zmĂ©nyekre is. A vásárlĂłk (hallgatĂłk) a világ minden táján kritikusan figyelik, hogy a pĂ©nzĂĽkĂ©rt naprakĂ©sz tudást kapnak-e. Az oktatási intĂ©zmĂ©nyeket (közĂ©piskolákat Ă©s egyetemeket) Nagy-Britanniában pĂ©ldául rangsorolják mind az oktatás szĂnvonala, mind a kutatásban elĂ©rt eredmĂ©nyei alapján. Ezek az informáciĂłk megjelennek a napilapokban Ă©s egyĂ©rtelműen jelzik az adott intĂ©zmĂ©ny rangját Ă©s a kibocsátott diploma piaci Ă©rtĂ©kĂ©t. Az egyre erĹ‘södĹ‘ hallgatĂłkĂ©rt törtĂ©nĹ‘ versenyben tehát igen fontos szerepe van a naprakĂ©sz tudásnak Ă©s a több terĂĽleten is felhasználhatĂł kĂ©szsĂ©gek oktatásának. A felsĹ‘oktatás egyre inkább szolgáltatĂł nagyĂĽzemmĂ© válik, amely igyekszik minĂ©l gyorsabban reagálni a piac igĂ©nyeire. A piac nagy választĂ©kot, rugalmas formákat Ă©s egymásra Ă©pĂthetĹ‘sĂ©get kĂván, Ăgy az egyetemek tárgyai legtöbb helyen már modulokbĂłl Ă©pĂĽlnek fel, ahol a hallgatĂłnak a kötött tantárgyak mellett választhatĂł tantárgyaik is vannak.
Másik világjelensĂ©g az egĂ©sz Ă©leten keresztĂĽl tartĂł folyamatos tanulás igĂ©nye. Elfogadott tĂ©ny, hogy bár kĂĽlönbözĹ‘ idĹ‘ alatt szakterĂĽlettĹ‘l fĂĽggĹ‘en elavul a tudás. Igy a diploma csak egy állomása, de nem a vĂ©gállomása a tanulásnak. Hogyan tudnak az oktatási intĂ©zmĂ©nyek megfelelni az egyre növekvĹ‘ számĂş elsĹ‘ diplomás kĂ©pzĂ©sĂ©nek Ă©s egy idĹ‘ben hogyan tudják kielĂ©gĂteni a posztgraduális hosszabb, rövidebb ideig tartĂł kĂ©pzĂ©sek iránti igĂ©nyt.
Ez a dilemma jelen van a nyugati Ă©s a keleti oktatási intĂ©zmĂ©nyekben egyaránt. A lĂ©nyeges kĂĽlönbsĂ©g a rendelkezĂ©sre állĂł idĹ‘ben van. Ami Nagy Britanniában pĂ©ldául mintegy ötven Ă©v alatt zajlott le az Magyarországon megprĂłbál megtörtĂ©nni tĂz Ă©v alatt. A felgyorsulás Ă©rzĂ©keltetĂ©sĂ©re talán cĂ©lszerű röviden vĂ©gigtekintenĂĽnk a brit oktatásban vĂ©gbemenĹ‘ változásokat az elmĂşlt ötven Ă©vben. Ha ezt párhuzamba állĂtjuk a magyarországi 1990-töl 2000-ig terjedĹ‘ tĂz esztendĹ‘ fĹ‘bb lĂ©pĂ©seivel elgondolkodtatĂł kĂ©pet kapunk
Non-BCS behavior of optical properties across the cuprate phase diagram
The finite-frequency optical properties of the underdoped cuprates, in both
the normal and superconducting state, display features which go beyond a Fermi
liquid and a BCS description. We provide an understanding of these properties
within a simplified analytical model, which has been evolved out of the Hubbard
model and ideas based on a resonating valence bond spin liquid. We find that:
1) in underdoped samples, the missing area integrals reveal a second energy
scale due to the pseudogap, not present at optimum or overdoping; 2) the real
part of the optical self-energy shows a large sharp peak, that emerges with the
opening of the pseudogap which exists within the superconducting state and
persists in the normal state; and 3) the amount of optical spectral weight
which is transferred to the condensate is greatly reduced by the presence of
the pseudogap as compared to the Fermi liquid case. These non-BCS features of
the superconducting state are in good qualitative agreement with a body of
experimental work on different cuprate systems and provide strong evidence from
optical conductivity that they are all a manifestation of the pseudogap energy
scale.Comment: to appear in PRB Rapid Communication
Linking the structure of alpha-synuclein oligmers to function in Parkinson's disease.
Misfolding and aggregation of alpha-synuclein (a-syn) are associated with a range of neurological disorders, including Parkinson's disease (PD). Fibrillar, insoluble aggregates of a-syn, known as Lewy bodies (LBs) are deposited in the substantia nigra and are a pathological hallmark of PD. a-syn is a natively unstructured protein, co-populating extended and more compact conformational forms under equilibrium. The fine balance of this equilibrium can be shifted due to changes in its environment such as alterations in metal content, ionic strength, free dopamine or others, promoting the assembly of a-syn into toxic conformations. Small, soluble oligomers preceding LB formation are thought to be causative, in vitro, different a-syn oligomers have been produced with alternate biochemical properties. Here the primary objective was to uncover the link between conformation and toxic gain of function by the use of functional assays in combination with ESI-IMS-MS. Epitope mapping procedures indicated that different a-syn oligomers have unique epitope features. Dye binding assays such as ThT and ANS fluorescence inferred that the various oligomer types differ in their amyloidogenicity and hydrophobicity. Furthermore, intracellular aggregation assays, MTT cell proliferation and Ca(ll) influx analysis in SH-SY5Y neuroblastoma cells showed that cellular effects correlated with structural features. ESI-IMS-MS spectra of the different oligomers have been acquired and allowed the conformations of the oligomer subsets to be determined. The oligomers assembled up to a hexameric form with a closed ring-like conformation. These results demonstrated that unique structural features are required for toxicity and that a subset of oligomers with characteristic structures may be pivotal in PD
Nonlinear photoluminescence spectra from a quantum dot-cavity system: Direct evidence of pump-induced stimulated emission and anharmonic cavity-QED
We investigate the power-dependent photoluminescence spectra from a strongly
coupled quantum dot-cavity system using a quantum master equation technique
that accounts for incoherent pumping, pure dephasing, and fermion or boson
statistics. Analytical spectra at the one-photon correlation level and the
numerically exact multi-photon spectra for fermions are presented. We compare
to recent experiments on a quantum dot-micropiller cavity system and show that
an excellent fit to the data can be obtained by varying only the incoherent
pump rates in direct correspondence with the experiments. Our theory and
experiments together show a clear and systematic way of studying
stimulated-emission induced broadening and anharmonic cavity-QED.Comment: We have reworked our previous arXiv paper and submitted this latest
version for peer revie
Amyloid-β(1-42) aggregation initiates its cellular uptake and cytotoxicity
The accumulation of amyloid beta peptide(1-42) (Abeta(1-42)) in extracellular plaques is one of the pathological hallmarks of Alzheimer disease (AD). Several studies have suggested that cellular reuptake of Abeta(1-42) may be a crucial step in its cytotoxicity, but the uptake mechanism is not yet understood. Abeta may be present in an aggregated form prior to cellular uptake. Alternatively, monomeric peptide may enter the endocytic pathway and conditions in the endocytic compartments may induce the aggregation process. Our study aims to answer the question whether aggregate formation is a prerequisite or a consequence of Abeta endocytosis. We visualized aggregate formation of fluorescently labeled Abeta(1-42) and tracked its internalization by human neuroblastoma cells and neurons. beta-Sheet-rich Abeta(1-42) aggregates entered the cells at low nanomolar concentration of Abeta(1-42). In contrast, monomer uptake faced a concentration threshold and occurred only at concentrations and time scales that allowed Abeta(1-42) aggregates to form. By uncoupling membrane binding from internalization, we found that Abeta(1-42) monomers bound rapidly to the plasma membrane and formed aggregates there. These structures were subsequently taken up and accumulated in endocytic vesicles. This process correlated with metabolic inhibition. Our data therefore imply that the formation of beta-sheet-rich aggregates is a prerequisite for Abeta(1-42) uptake and cytotoxicity
Neuromodulation via the Cerebrospinal Fluid: Insights from Recent in Vitro Studies
The cerebrospinal fluid (CSF) occupies the brain’s ventricles and subarachnoid space
and, together with the interstitial fluid (ISF), forms a continuous fluidic network that
bathes all cells of the central nervous system (CNS). As such, the CSF is well positioned
to actively distribute neuromodulators to neural circuits in vivo via volume transmission.
Recent in vitro experimental work in brain slices and neuronal cultures has shown that
human CSF indeed contains neuromodulators that strongly influence neuronal activity.
Here we briefly summarize these new findings and discuss their potential relevance to
neural circuits in health and disease
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