The purpose of this application, under Articles 78.1 and 81.1 of the Code, is to replace Diplodocus longus Marsh, 1878 as the type species of the sauropod dinosaur genus Diplodocus by the much better represented D. carnegii Hatcher, 1901, due to the undiagnosable state of the holotype of D. longus (YPM 1920, a partial tail and a chevron). The holotype of D. carnegii, CM 84, is a well-preserved and mostly articulated specimen. Casts of it are on display in various museums around the world, and the species has generally been used as the main reference for studies of comparative anatomy or phylogeny of the genus. Both species are known from the Upper Jurassic Morrison Formation of the western United States. The genus Diplodocus is the basis for the family-level taxa diplodocinae Marsh, 1884, diplodocidae Marsh, 1884, diplodocimorpha Marsh, 1884 (Calvo & Salgado, 1995) and diplodocoidea Marsh, 1884 (Upchurch, 1995). It is also a specifier of at least 10 phylogenetic clades. With the replacement of D. longus by D. carnegii as type species, Diplodocus could be preserved as a taxonomic name with generally accepted content. Taxonomic stability of the entire clade diplodocoidea, and the proposed definitions of several clades within Sauropoda, could be maintained.

{We consider stochastic Navier-Stokes equations in a 2D-bounded domain with the Navier with friction boundary condition. We establish the existence and the uniqueness of the solutions and study the vanishing viscosity limit. More precisely, we prove that solutions of stochastic Navier Stokes equations converge, as the viscosity goes to zero, to solutions of the corresponding stochastic Euler equations. (C) 2015 Elsevier B.V. All rights reserved.}

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Molybdenum is found in the active site of enzymes usually coordinated by one or two pyranopterin molecules. Here, we mimic an enzyme with a mononuclear molybdenum-bis pyranopterin center by incorporating molybdenum in rubredoxin. In the molybdenum-substituted rubredoxin, the metal ion is coordinated by four sulfurs from conserved cysteine residues of the apo-rubredoxin and two other exogenous ligands, oxygen and thiol, forming a Mo((VI))-(S-Cys)4(O)(X) complex, where X represents -OH or -SR. The rubredoxin molybdenum center is stabilized in a Mo(VI) oxidation state, but can be reduced to Mo(IV) via Mo(V) by dithionite, being a suitable model for the spectroscopic properties of resting and reduced forms of molybdenum-bis pyranopterin-containing enzymes. Preliminary experiments indicate that the molybdenum site built in rubredoxin can promote oxo transfer reactions, as exemplified with the oxidation of arsenite to arsenate.