University of Paris

About: University of Paris is a education organization based out in Paris, France. It is known for research contribution in the topics: Population & Transplantation. The organization has 102426 authors who have published 174180 publications receiving 5041753 citations. The organization is also known as: Sorbonne.

FETI‐DP: a dual–primal unified FETI method—part I: A faster alternative to the two‐level FETI method

Abstract: The FETI method and its two-level extension (FETI-2) are two numerically scalable domain decomposition methods with Lagrange multipliers for the iterative solution of second-order solid mechanics and fourth-order beam, plate and shell structural problems, respectively.The FETI-2 method distinguishes itself from the basic or one-level FETI method by a second set of Lagrange multipliers that are introduced at the subdomain cross-points to enforce at each iteration the exact continuity of a subset of the displacement field at these specific locations. In this paper, we present a dual–primal formulation of the FETI-2 concept that eliminates the need for that second set of Lagrange multipliers, and unifies all previously developed one-level and two-level FETI algorithms into a single dual–primal FETI-DP method. We show that this new FETI-DP method is numerically scalable for both second-order and fourth-order problems. We also show that it is more robust and more computationally efficient than existing FETI solvers, particularly when the number of subdomains and/or processors is very large. Copyright © 2001 John Wiley & Sons, Ltd.

Polarity of oxide surfaces and nanostructures

Abstract: Whenever a compound crystal is cut normal to a randomly chosen direction, there is an overwhelming probability that the resulting surface corresponds to a polar termination and is highly unstable. Indeed, polar oxide surfaces are subject to complex stabilization processes that ultimately determine their physical and chemical properties. However, owing to recent advances in their preparation under controlled conditions and to improvements in the experimental techniques for their characterization, an impressive variety of structures have been investigated in the last few years. Recent progress in the fabrication of oxide nano-objects, which have been largely stimulated by a growing demand for new materials for applications ranging from micro-electronics to heterogeneous catalysis, also offer interesting examples of exotic polar structures. At odds with polar orientations of macroscopic samples, some smaller size polar nano-structures turn out to be perfectly stable. Others are subject to unusual processes of stabilization, which are absent or not effective in their extended counterparts. In this context, a thorough and comprehensive reflexion on the role that polarity plays at oxide surfaces, interfaces and in nano-objects seems timely.This review includes a first section which presents the theoretical concepts at the root of the polar electrostatic instability and its compensation and introduces a rigorous definition of polar terminations that encompasses previous theoretical treatments; a second section devoted to a summary of all experimental and theoretical results obtained since the first review paper by Noguera (2000 J. Phys.: Condens. Matter 12 R367); and finally a discussion section focusing on the relative strength of the stabilization mechanisms, with special emphasis on ternary compound surfaces and on polarity effects in ultra-thin films.

Global protein function prediction from protein-protein interaction networks

Abstract: Determining protein function is one of the most challenging problems of the post-genomic era. The availability of entire genome sequences and of high-throughput capabilities to determine gene coexpression patterns has shifted the research focus from the study of single proteins or small complexes to that of the entire proteome 1 . In this context, the search for reliable methods for assigning protein function is of primary importance. There are various approaches available for deducing the function of proteins of unknown function using information derived from sequence similarity or clustering patterns of coregulated genes 2,3 , phylogenetic profiles 4 , protein-protein interactions (refs. 5‐8 and Samanta, M.P. and Liang, S., unpublished data), and protein complexes 9,10 . Here we propose the assignment of proteins to functional classes on the basis of their network of physical interactions as determined by minimizing the number of protein interactions among different functional categories. Function assignment is proteome-wide and is determined by the global connectivity pattern of the protein network. The approach results in multiple functional assignments, a consequence of the existence of multiple equivalent solutions. We apply the method to analyze the yeast Saccharomyces cerevisiae protein-protein interaction network 5 .