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12,215 result(s) for "complex regulation"
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miR390, Arabidopsis TAS3 tasiRNAs, and Their AUXIN RESPONSE FACTOR Targets Define an Autoregulatory Network Quantitatively Regulating Lateral Root Growth
Plants adapt to different environmental conditions by constantly forming new organs in response to morphogenetic signals. Lateral roots branch from the main root in response to local auxin maxima. How a local auxin maximum translates into a robust pattern of gene activation ensuring the proper growth of the newly formed lateral root is largely unknown. Here, we demonstrate that miR390, TAS3-derived trans-acting short-interfering RNAs (tasiRNAs), and AUXIN RESPONSE FACTORS (ARFs) form an auxin-responsive regulatory network controlling lateral root growth. Spatial expression analysis using reporter gene fusions, tasi/miRNA sensors, and mutant analysis showed that miR390 is specifically expressed at the sites of lateral root initiation where it triggers the biogenesis of tasiRNAs. These tasiRNAs inhibit ARF2, ARF3, and ARF4, thus releasing repression of lateral root growth. In addition, ARF2, ARF3, and ARF4 affect auxin-induced miR390 accumulation. Positive and negative feedback regulation of miR390 by ARF2, ARF3, and ARF4 thus ensures the proper definition of the miR390 expression pattern. This regulatory network maintains ARF expression in a concentration range optimal for specifying the timing of lateral root growth, a function similar to its activity during leaf development. These results also show how small regulatory RNAs integrate with auxin signaling to quantitatively regulate organ growth during development.
Intramolecular domain dynamics regulate synaptic MAGUK protein interactions
PSD-95 MAGUK family scaffold proteins are multi-domain organisers of synaptic transmission that contain three PDZ domains followed by an SH3-GK domain tandem. This domain architecture allows coordinated assembly of protein complexes composed of neurotransmitter receptors, synaptic adhesion molecules and downstream signalling effectors. Here we show that binding of monomeric CRIPT-derived PDZ3 ligands to the third PDZ domain of PSD-95 induces functional changes in the intramolecular SH3-GK domain assembly that influence subsequent homotypic and heterotypic complex formation. We identify PSD-95 interactors that differentially bind to the SH3-GK domain tandem depending on its conformational state. Among these interactors, we further establish the heterotrimeric G protein subunit Gnb5 as a PSD-95 complex partner at dendritic spines of rat hippocampal neurons. The PSD-95 GK domain binds to Gnb5, and this interaction is triggered by CRIPT-derived PDZ3 ligands binding to the third PDZ domain of PSD-95, unraveling a hierarchical binding mechanism of PSD-95 complex formation.
Simple rules for the developing world
Much of the discussion in favor of simplicity of legal rules and against complex regulation is rooted in economically developed countries with strong state capacity. With economic development and state capacity comes the presumption that complex rules will be enforced. Therefore, analysis focuses on the administrative and error costs, and the unintended consequences of complex rules that are enforced. This paper argues that the Epsteinian insight is even more relevant to the developing world where countries often lack enough state capacity to even take on simple governance tasks. Developing countries often have less than 20 percent of the state capacity of developed countries. However, this does not mean they limit the regulatory structure to a fifth of the tasks. Under-enforcement or non-enforcement of complex rules imposes different costs and unintended consequences on society. Using examples from India, this paper highlights problems of enforcement swamping, deadweight loss, and corruption arising from the under-enforcement of complex rules. To avoid these problems, the paper concludes that a fortiori less developed countries should favor simple rules.
Control of sulphate assimilation and glutathione synthesis: interaction with N and C metabolism
Sulphate assimilation is an essential pathway being a source of reduced sulphur for various cellular processes and for the synthesis of glutathione, a major factor in plant stress defence. Many reports have shown that sulphate assimilation is well co-ordinated with the assimilation of nitrate and carbon. It has long been known that, during nitrate deficiency, sulphate assimilation is reduced and that the capacity to reduce nitrate is diminished in plants starved for sulphate. Only recently, however, was it shown that adenosine 5′ phosphosulphate reductase (APR), the key enzyme of sulphate assimilation, is regulated by carbohydrates. In plants treated with sucrose or glucose APR was induced, whereas the activity was strongly reduced in plants grown in CO2-free air. The availability of cysteine is a crucial factor in glutathione synthesis, but an adequate supply of glutamate and glycine are also important. The molecular mechanisms for the co-ordination of S, N, and C assimilation are not known. O-acetylserine, a precursor of cysteine, was proposed to be the signal regulating sulphate assimilation, but most probably is not the outgoing signal to N and C metabolism. cDNA arrays revealed the induction of genes involved in auxin synthesis upon S-starvation, pointing to a possible role of phytohormones. Clearly, despite significant progress in understanding the regulation of sulphate assimilation and glutathione synthesis, their co-ordination with N and C metabolism achieved, and several potential signal molecules identified, present knowledge is still far from being sufficient.
Regulation of calcium signalling and gene expression by glutathione
The glutathione redox couple is an information-rich redox buffer that interacts with numerous cellular components. To explore the role of glutathione in redox signalling, leaf contents were increased either chemically, by feeding reduced glutathione (GSH), or genetically, by over-expressing the first enzyme of the GSH biosynthetic pathway, γ-glutamylcysteine synthetase (γ-ECS). Leaf discs were also fed glutathione disulphide (GSSG), leading to increases in both GSH and GSSG. The effects of increases in GSH were compared with non-specific changes in leaf thiol status induced by feeding dithiothreitol (DTT) or the monothiol β-mercaptoethanol (β-ME). Photosynthesis measurements showed that none of the feeding treatments greatly disrupted leaf physiology. Transgenic plants expressing aequorin were used to analyse calcium signatures during the feeding treatments. Calcium release occurred soon after the onset of GSH or GSSG feeding, but was unaffected by DTT or β-ME. Pathogenesis-related protein 1 (PR-1) was induced both in the γ-ECS overexpressors and by feeding GSH, but not GSSG. Feeding DTT also induced PR-1. Key transcripts encoding antioxidative enzymes were much less affected, although glutathione synthetase was suppressed by feeding thiols or GSSG. It is concluded that modulation of glutathione contents transmits information through diverse signalling mechanisms, including (i) the establishment of an appropriate redox potential for thiol/disulphide exchange and (ii) the release of calcium to the cytosol.
Regulation of high-affinity sulphate transporters in plants: towards systematic analysis of sulphur signalling and regulation
Plants require the function of plasma membrane-bound sulphate transporters for the initial uptake of inorganic sulphate. Part of this fundamental process is the energy-dependent proton/sulphate co-transport systems that are located in the surface cell layers of roots. During sulphur limitation, plants are able to activate the expression of sulphate transporters that facilitate the uptake of sulphate in roots. SULTR1;1 and SULTR1;2 are suggested to be the essential components of the sulphate uptake system in Arabidopsis roots. The physiological importance of SULTR1;1 and SULTR1;2 is supported by characteristics that can cope with sulphur deficiency: they were (i) functional high-affinity sulphate transporters; (ii) induced by sulphur limitation at the mRNA levels; and (iii) predominantly localized in the root hairs, epidermis, and cortex. The expression of high-affinity sulphate transporters was primarily regulated by sulphur in a promoter-dependent manner. Aside from the sulphur-specific regulation, the induction of SULTR1;1 and SULTR1;2 high-affinity sulphate transporters by sulphur limitation was dependent on the supply of carbon and nitrogen. In this review, the application of SULTR promoter–GFP systems for the analysis of regulatory pathways of sulphate acquisition in plants is described.
Impact of pedospheric and atmospheric sulphur nutrition on sulphur metabolism of Allium cepa L., a species with a potential sink capacity for secondary sulphur compounds
Onion (Allium cepa L.) was able to use atmospheric H2S as sole sulphur source for growth. The foliarly absorbed H2S was rapidly metabolized into water-soluble, non-protein thiol compounds, including cysteine, and subsequently into other sulphur compounds in the shoots. In H2S-exposed plants, the accumulation of sulphur compounds in the shoots was nearly linear with the concentration (0.15–0.6 μl l−1) and duration of the exposure. Exposure of onion to H2S for up to 1 week did not affect the sulphur content of the roots. Secondary sulphur compounds formed a sink for the foliarly absorbed sulphide, and the sulphur accumulation upon H2S exposure could, for a great part, be ascribed to enhancement of the content of γ-glutamyl peptides and/or alliins. Furthermore, there was a substantial increase in the sulphate content in the shoots upon H2S exposure. The accumulation of sulphate originated both from the pedosphere and from the oxidation of absorbed atmospheric sulphide, and/or from the degradation of accumulated secondary sulphur compounds. From studies on the interaction between atmospheric and pedospheric sulphur nutrition it was evident that H2S exposure did not result in a down-regulation of the sulphate uptake by the roots.
Structure, function and regulation of the hsp90 machinery
Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone which is essential in eukaryotes. It is required for the activation and stabilization of a wide variety of client proteins and many of them are involved in important cellular pathways. Since Hsp90 affects numerous physiological processes such as signal transduction, intracellular transport, and protein degradation, it became an interesting target for cancer therapy. Structurally, Hsp90 is a flexible dimeric protein composed of three different domains which adopt structurally distinct conformations. ATP binding triggers directionality in these conformational changes and leads to a more compact state. To achieve its function, Hsp90 works together with a large group of cofactors, termed co-chaperones. Co-chaperones form defined binary or ternary complexes with Hsp90, which facilitate the maturation of client proteins. In addition, posttranslational modifications of Hsp90, such as phosphorylation and acetylation, provide another level of regulation. They influence the conformational cycle, co-chaperone interaction, and inter-domain communications. In this review, we discuss the recent progress made in understanding the Hsp90 machinery.
From a Liberal Occupation to an Occupation of the Welfare State: Norwegian Physiotherapy 1960-2000
This article demonstrates how Norwegian physiotherapy has developed as part of the state apparatus over the past decades. From the state's point of view, the methods and skills of physiotherapy are deemed valuable because they are designed to encourage people to take an active part in constructing and reconstructing their own health. From the physiotherapists' point of view, the state is an attractive ally in their seemingly endless struggle to escape from the shadow of medicine. The occupation was drawn into the public domain and given a wider mandate as part of a bio-political strategy. In return, it has experienced growth, gained nationwide representation, and obtained greater autonomy vis-à-vis the law. The case illustrates the larger issues of how modern welfare states expand and contribute to the regulation of complex societies.
The Telomerase Complex: An Overview
This chapter contains sections titled: Conservation of Telomere Function and the Discovery of Telomerase The Discovery of the Two Minimal Telomerase Components Telomerase Beyond the Minimal Components: Associated Proteins Regulation of Telomerase by Telomeric Proteins and RNAS Telomerase, Telomere Maintenance, Cancer, and Aging Telomerase Beyond Telomere Synthesis Telomere Maintenance Without Telomerase Conclusion Acknowledgment References