A Rigorous Computational Approach to Linear Response

We present a general setting in which the formula describing the linear response of the physical measure of a perturbed system can be obtained. In this general setting we obtain an algorithm to rigorously compute the linear response. We apply our results to expanding circle maps. In particular, we present examples where we compute, up to a pre-specified error in the $L^{\infty}$-norm, the response of expanding circle maps under stochastic and deterministic perturbations. Moreover, we present an example where we compute, up to a pre-specified error in the $L^1$-norm, the response of the intermittent family at the boundary; i.e., when the unperturbed system is the doubling map.Comment: Revised version following reports. A new example which contains the computation of the linear response at the boundary of the intermittent family has been adde

An elementary way to rigorously estimate convergence to equilibrium and escape rates

We show an elementary method to have (finite time and asymptotic) computer assisted explicit upper bounds on convergence to equilibrium (decay of correlations) and escape rate for systems satisfying a Lasota Yorke inequality. The bounds are deduced by the ones of suitable approximations of the system's transfer operator. We also present some rigorous experiment showing the approach and some concrete result.Comment: 14 pages, 6 figure

Partial holomorphic connections and extension of foliations

This paper stresses the strong link between the existence of partial holomorphic connections on the normal bundle of a foliation seen as a quotient of the ambient tangent bundle and the extendability of a foliation to an infinitesimal neighborhood of a submanifold. We find the obstructions to extendability and thanks to the theory developed we obtain some new Khanedani-Lehmann-Suwa type index theorems

Search and Discovery Tools for Astronomical On-line Resources and Services

A growing number of astronomical resources and data or information services are made available through the Internet. However valuable information is frequently hidden in a deluge of non-pertinent or non up-to-date documents. At a first level, compilations of astronomical resources provide help for selecting relevant sites. Combining yellow-page services and meta-databases of active pointers may be an efficient solution to the data retrieval problem. Responses generated by submission of queries to a set of heterogeneous resources are difficult to merge or cross-match, because different data providers generally use different data formats: new endeavors are under way to tackle this problem. We review the technical challenges involved in trying to provide general search and discovery tools, and to integrate them through upper level interfaces.Comment: 7 pages, 2 Postscript figures; to be published in A&A

Zinc(II)-methimazole complexes: synthesis and reactivity

The tetrahedral S-coordinated complex [Zn(MeImHS)(4)](ClO4)(2), synthesised from the reaction of [Zn(ClO4)(2)] with methimazole (1-methyl-3H-imidazole-2-thione, MeImHS), reacts with triethylamine to yield the homoleptic complex [Zn(MeImS)(2)] (MeImS = anion methimazole). ESI-MS and MAS C-13-NMR experiments supported MeImS acting as a (N, S)-chelating ligand. The DFT-optimised structure of [Zn(MeImS)(2)] is also reported and the main bond lengths compared to those of related Zn-methimazole complexes. The complex [Zn(MeImS)(2)] reacts under mild conditions with methyl iodide and separates the novel complex [Zn(MeImSMe)(2)I-2] (MeImSMe = S-methylmethimazole). X-ray diffraction analysis of the complex shows a ZnI2N2 core, with the methyl thioethers uncoordinated to zinc. Conversely, the reaction of [Zn( MeImS)(2)] with hydroiodic acid led to the formation of the complex [Zn(MeImHS)(2)I-2] having a ZnI2S2 core with the neutral methimazole units S-coordinating the metal centre. The Zn-coordinated methimazole can markedly modify the coordination environment when changing from its thione to thionate form and vice versa. The study of the interaction of the drug methimazole with the complex [Zn(MeIm)(4)](2+) (MeIm = 1-methylimidazole) - as a model for Zn-enzymes containing a N-4 donor set from histidine residues shows that methimazole displaces only one of the coordinated MeIm molecules; the formation constant of the mixed complex [Zn(MeIm)(3)(MeImHS)](2+) was determined

\u3cem\u3eN\u3c/em\u3e-Methylbenzothiazole-2(3\u3cem\u3eH\u3c/em\u3e)-selone, C\u3csub\u3e8\u3c/sub\u3eH\u3csub\u3e7\u3c/sub\u3eNSSe

The crystal structure of N-methyl1,3-benzothiazole-2(3H)-selone, (mbts) has been studied to estimate the changes in the molecular geometry of the mbts ligand upon coordination. Hypervalent complexes of mbts with TeII and II have been studied by us previously. A significant elongation of the Se=C bond [from 1.817 (7) in mbts to 1.85-1.88 Å in the complexes] was found, but there were no significant changes in the other geometric parameters of the ligand. The only other bond-length decrease of note was for SeC-NMe [from 1.35 (1) in mbts to 1.32-1.34 Å in the complexes]. Thus, only the amino group takes part in electron redistribution upon coordination

Source and dynamics of a volcanic caldera unrest : Campi Flegrei, 1983–84

Acknowledgements We thank Tiziana Vanorio, Antonella Amoruso, Luca Crescentini, Nicholas Rawlinson, Yasuko Takei, and David Cornwell for the valuable suggestions regarding the methodology and interpretation. Reviews from Tim Greenfield and two anonymous reviewers helped improving both clarity of the manuscript and interpretation. The Royal Society of Edinburgh - Accademia dei Lincei Bilateral Agreement, the Santander Mobility Award of the College of Physical Sciences, University of Aberdeen, and the TIDES EU COST action granted L.D.S. travel grants for the realisation of this study. E.D.P. has been supported by the EPHESTO and KNOWAVES projects, funded by the Spanish Ministry of Education and Science.Peer reviewedPublisher PD

Brucella and Osteoarticular Cell Activation: Partners in Crime

Osteoarticular brucellosis is the most common presentation of human active disease although its prevalence varies widely. The three most common forms of osteoarticular involvement are sacroiliitis, spondylitis, and peripheral arthritis. The molecular mechanisms implicated in bone damage have been recently elucidated. B. abortus induces bone damage through diverse mechanisms in which TNF-α and the receptor activator of nuclear factor kappa-B ligand (RANKL)-the natural modulator of bone homeostasis are involved. These processes are driven by inflammatory cells, like monocytes/macrophages, neutrophils, Th17 CD4+ T, and B cells. In addition, Brucella abortus has a direct effect on osteoarticular cells and tilts homeostatic bone remodeling. These bacteria inhibit bone matrix deposition by osteoblasts (the only bone cells involved in bone deposition), and modify the phenotype of these cells to produce matrix metalloproteinases (MMPs) and cytokine secretion, contributing to bone matrix degradation. B. abortus also affects osteoclasts (cells naturally involved in bone resorption) by inducing an increase in osteoclastogenesis and osteoclast activation; thus, increasing mineral and organic bone matrix resorption, contributing to bone damage. Given that the pathology induced by Brucella species involved joint tissue, experiments conducted on synoviocytes revealed that besides inducing the activation of these cells to secrete chemokines, proinflammatory cytokines and MMPS, the infection also inhibits synoviocyte apoptosis. Brucella is an intracellular bacterium that replicates preferentially in the endoplasmic reticulum of macrophages. The analysis of B. abortus-infected synoviocytes indicated that bacteria also replicate in their reticulum suggesting that they could use this cell type for intracellular replication during the osteoarticular localization of the disease. Finally, the molecular mechanisms of osteoarticular brucellosis discovered recently shed light on how the interaction between B. abortus and immune and osteoarticular cells may play an important role in producing damage in joint and bone.Fil: Giambartolomei, Guillermo Hernan. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Inmunología, Genética y Metabolismo. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Inmunología, Genética y Metabolismo; ArgentinaFil: Arriola Benitez, Paula Constanza. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Inmunología, Genética y Metabolismo. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Inmunología, Genética y Metabolismo; ArgentinaFil: Delpino, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Inmunología, Genética y Metabolismo. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Inmunología, Genética y Metabolismo; Argentin