Domino tilings and related models: space of configurations of domains with holes

We first prove that the set of domino tilings of a fixed finite figure is a distributive lattice, even in the case when the figure has holes. We then give a geometrical interpretation of the order given by this lattice, using (not necessarily local) transformations called {\em flips}. This study allows us to formulate an exhaustive generation algorithm and a uniform random sampling algorithm. We finally extend these results to other types of tilings (calisson tilings, tilings with bicolored Wang tiles).Comment: 17 pages, 11 figure

Communication Complexity and Intrinsic Universality in Cellular Automata

The notions of universality and completeness are central in the theories of computation and computational complexity. However, proving lower bounds and necessary conditions remains hard in most of the cases. In this article, we introduce necessary conditions for a cellular automaton to be "universal", according to a precise notion of simulation, related both to the dynamics of cellular automata and to their computational power. This notion of simulation relies on simple operations of space-time rescaling and it is intrinsic to the model of cellular automata. Intrinsinc universality, the derived notion, is stronger than Turing universality, but more uniform, and easier to define and study. Our approach builds upon the notion of communication complexity, which was primarily designed to study parallel programs, and thus is, as we show in this article, particulary well suited to the study of cellular automata: it allowed to show, by studying natural problems on the dynamics of cellular automata, that several classes of cellular automata, as well as many natural (elementary) examples, could not be intrinsically universal

Traced communication complexity of cellular automata

We study cellular automata with respect to a new communication complexity problem: each of two players know half of some finite word, and must be able to tell whether the state of the central cell will follow a given evolution, by communicating as little as possible between each other. We present some links with classical dynamical concepts, especially equicontinuity, expansiveness, entropy and give the asymptotic communication complexity of most elementary cellular automata.Comment: submitted to TC

Chiasma

Newspaper reporting on events at the Boston University School of Medicine in the 1960s

Proceedings of AUTOMATA 2011 : 17th International Workshop on Cellular Automata and Discrete Complex Systems

International audienceThe proceedings contain full (reviewed) papers and short (non reviewed) papers that were presented at the workshop

Communications in cellular automata

The goal of this paper is to show why the framework of communication complexity seems suitable for the study of cellular automata. Researchers have tackled different algorithmic problems ranging from the complexity of predicting to the decidability of different dynamical properties of cellular automata. But the difference here is that we look for communication protocols arising in the dynamics itself. Our work is guided by the following idea: if we are able to give a protocol describing a cellular automaton, then we can understand its behavior

Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex

<p>Abstract</p> <p>Background</p> <p>To study the organization and interaction with the fusion domain (or fusion peptide, FP) of the transmembrane domain (TMD) of influenza virus envelope glycoprotein for its role in membrane fusion which is also essential in the cellular trafficking of biomolecules and sperm-egg fusion.</p> <p>Results</p> <p>The fluorescence and gel electrophoresis experiments revealed a tight self-assembly of TMD in the model membrane. A weak but non-random interaction between TMD and FP in the membrane was found. In the complex, the central TMD oligomer was packed by FP in an antiparallel fashion. FP insertion into the membrane was altered by binding to TMD. An infrared study exhibited an enhanced membrane perturbation by the complex formation. A model was built to illustrate the role of TMD in the late stages of influenza virus-mediated membrane fusion reaction.</p> <p>Conclusion</p> <p>The TMD oligomer anchors the fusion protein in the membrane with minimal destabilization to the membrane. Upon associating with FP, the complex exerts a synergistic effect on the membrane perturbation. This effect is likely to contribute to the complete membrane fusion during the late phase of fusion protein-induced fusion cascade. The results presented in the work characterize the nature of the interaction of TMD with the membrane and TMD in a complex with FP in the steps leading to pore initiation and dilation during virus-induced fusion. Our data and proposed fusion model highlight the key role of TMD-FP interaction and have implications on the fusion reaction mediated by other type I viral fusion proteins. Understanding the molecular mechanism of membrane fusion may assist in the design of anti-viral drugs.</p

Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex

<p>Abstract</p> <p>Background</p> <p>To study the organization and interaction with the fusion domain (or fusion peptide, FP) of the transmembrane domain (TMD) of influenza virus envelope glycoprotein for its role in membrane fusion which is also essential in the cellular trafficking of biomolecules and sperm-egg fusion.</p> <p>Results</p> <p>The fluorescence and gel electrophoresis experiments revealed a tight self-assembly of TMD in the model membrane. A weak but non-random interaction between TMD and FP in the membrane was found. In the complex, the central TMD oligomer was packed by FP in an antiparallel fashion. FP insertion into the membrane was altered by binding to TMD. An infrared study exhibited an enhanced membrane perturbation by the complex formation. A model was built to illustrate the role of TMD in the late stages of influenza virus-mediated membrane fusion reaction.</p> <p>Conclusion</p> <p>The TMD oligomer anchors the fusion protein in the membrane with minimal destabilization to the membrane. Upon associating with FP, the complex exerts a synergistic effect on the membrane perturbation. This effect is likely to contribute to the complete membrane fusion during the late phase of fusion protein-induced fusion cascade. The results presented in the work characterize the nature of the interaction of TMD with the membrane and TMD in a complex with FP in the steps leading to pore initiation and dilation during virus-induced fusion. Our data and proposed fusion model highlight the key role of TMD-FP interaction and have implications on the fusion reaction mediated by other type I viral fusion proteins. Understanding the molecular mechanism of membrane fusion may assist in the design of anti-viral drugs.</p

Blacklisting variants common in private cohorts but not in public databases optimizes human exome analysis

Computational analyses of human patient exomes aim to filter out as many nonpathogenic genetic variants (NPVs) as possible, without removing the true disease-causing mutations. This involves comparing the patient's exome with public databases to remove reported variants inconsistent with disease prevalence, mode of inheritance, or clinical penetrance. However, variants frequent in a given exome cohort, but absent or rare in public databases, have also been reported and treated as NPVs, without rigorous exploration. We report the generation of a blacklist of variants frequent within an in-house cohort of 3,104 exomes. This blacklist did not remove known pathogenic mutations from the exomes of 129 patients and decreased the number of NPVs remaining in the 3,104 individual exomes by a median of 62%. We validated this approach by testing three other independent cohorts of 400, 902, and 3,869 exomes. The blacklist generated from any given cohort removed a substantial proportion of NPVs (11-65%). We analyzed the blacklisted variants computationally and experimentally. Most of the blacklisted variants corresponded to false signals generated by incomplete reference genome assembly, location in low-complexity regions, bioinformatic misprocessing, or limitations inherent to cohort-specific private alleles (e.g., due to sequencing kits, and genetic ancestries). Finally, we provide our precalculated blacklists, together with ReFiNE, a program for generating customized blacklists from any medium-sized or large in-house cohort of exome (or other next-generation sequencing) data via a user-friendly public web server. This work demonstrates the power of extracting variant blacklists from private databases as a specific in-house but broadly applicable tool for optimizing exome analysis