Inner metric properties of 2-dimensional semi-algebraic sets

Sin resume

Carthaginians, Romans and Americans: overseas with the 355th AAA SLT BN

While the title 355th AAA Searchlight Battalion dates back to May of 1942, the actual history of the unit, and the personnel in it, dates back to fifteen months before that -- February, 1941. At this time there were four coast artillery regiments in training at Camp Stewart, Georgia. The 207th and 212th were from New York City, the 209th from Western New York State, and the 214th from Georgia. These units had been sent to Camp Stewart for one year of basic training. The A batteries, or searchlight batteries, of these regiments were the units which later formed the First Provisional Searchlight Battalion. Such terms as DEC, azimuth, elevation, orientation, and slant range, soon became familiar to the men of these batteries. In addition to their specialized training in searchlights and searchlight tactics, the men received regular basic military training. The study of subjects, such as convoy discipline, first aid, communications, map reading and aircraft recognition, became a part of the daily routine. The men were also given calisthenics, infantry drill and manual of arms to build their bodies.https://digicom.bpl.lib.me.us/ww_reg_his/1056/thumbnail.jp

Developing innovative systems for reinforced masonry walls

The Commission of the European Communities has recently funded a CRAFT research project aimed at developing innovative systems for load and non-load-bearing reinforced masonry walls. The project involves twelve partners coming from four different European countries, among which there are universities and research centres, small and medium enterprises for the production of clay and concrete units and mortars, a company for advanced metal products and industrial associations of brick and block producers. The development of the reinforced masonry walls is based on the advancement of vertical reinforcement and fastenings, of mortar and concrete and on their integration with special clay and concrete blocks for the definition of new construction systems. The foreseen advantages are: new possibilities for masonry; more economical construction; quality increase for masonry walls; crack-free and earthquake resistant construction. The project follows three steps: assessment of the technical and economical feasibility of the envisaged construction technologies by means of extensive experimental and numerical activities; construction of prototypes as demonstration of the proposed technologies and materials; in situ testing to completely validate the systems. In the present contribution, an overview of the main objectives and steps of the project is given. Furthermore, the different construction systems that are being developed and designed are described. The main fields of application and the main technical problems encountered for the different construction systems is described, together with the experimental program outlined in order to characterize their mechanical behaviour under different serviceability and ultimate conditions

Bi-allelic mutations in uncoordinated mutant number-45 myosin chaperone B are a cause for congenital myopathy

Congenital myopathies (CM) form a genetically heterogeneous group of disorders characterized by perinatal muscle weakness. Here, we report an 11-year old male offspring of consanguineous parents of Lebanese origin. He presented with proximal weakness including Gower's sign, and skeletal muscle biopsy revealed myopathic changes with core-like structures. Whole exome sequencing of this index patient lead to the discovery of a novel genetically defined CM subtype based on bi-allelic mutations in the uncoordinated mutant number-45 myosin chaperone B (UNC45B) NM_173167:c.2261G > A, p.Arg754Gln. The mutation is conserved in evolution and co-segregates within the pedigree with the phenotype, and located in the myosin binding armadillo repeat domain 3 (ARM3), and has a CADD Score of 35. On a multimeric level, UNC45B aggregates to a chain which serves as an assembly line and functions as a template defining the geometry, regularity, and periodicity of myosin arranged into muscle thick filaments. Our discovery is in line with the previously described myopathological phenotypes in C. elegans and in vertebrate mutants and knockdown-models. In conclusion, we here report for the first time a patient with an UNC45B mutation causing a novel genetically defined congenital myopathy disease entity

Structure of the TPR Domain of AIP: Lack of Client Protein Interaction with the C-Terminal alpha-7 Helix of the TPR Domain of AIP Is Sufficient for Pituitary Adenoma Predisposition

PMCID: PMC3534021This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited

Unc45b Forms a Cytosolic Complex with Hsp90 and Targets the Unfolded Myosin Motor Domain

Myosin folding and assembly in striated muscle is mediated by the general chaperones Hsc70 and Hsp90 and a myosin specific co-chaperone, UNC45. Two UNC45 genes are found in vertebrates, including a striated muscle specific form, Unc45b. We have investigated the role of Unc45b in myosin folding. Epitope tagged murine Unc45b (Unc45bFlag) was expressed in muscle and non-muscle cells and bacteria, isolated and characterized. The protein is a soluble monomer in solution with a compact folded rod-shaped structure of ∼19 nm length by electron microscopy. When over-expressed in striated muscle cells, Unc45bFlag fractionates as a cytosolic protein and isolates as a stable complex with Hsp90. Purified Unc45bFlag re-binds Hsp90 and forms a stable complex in solution. The endogenous Unc45b in muscle cell lysates is also found associated with Hsp90. The Unc45bFlag/Hsp90 complex binds the partially folded myosin motor domain when incubated with myosin subfragments synthesized in a reticulocyte lysate. This binding is independent of the myosin rod or light chains. Unc45bFlag does not bind native myosin subfragments consistent with a chaperone function. More importantly, Unc45bFlag enhances myosin motor domain folding during de novo motor domain synthesis indicating that it has a direct role in myosin maturation. Thus, mammalian Unc45b is a cytosolic protein that forms a stable complex with Hsp90, selectively binds the unfolded conformation of the myosin motor domain, and promotes motor domain folding

Secondary structure of rhBMP-2 in a protective biopolymeric carrier material

Efficient delivery of growth factors is one of the great challenges of tissue engineering. Polyelectrolyte multilayer films (PEM) made of biopolymers have recently emerged as an interesting carrier for delivering recombinant human bone morphogenetic protein 2 (rhBMP-2 noted here BMP-2) to cells in a matrix-bound manner. We recently showed that PEM made of poly(l-lysine) and hyaluronan (PLL/HA) can retain high and tunable quantities of BMP-2 and can deliver it to cells to induce their differentiation in osteoblasts. Here, we investigate quantitatively by Fourier transform infrared spectroscopy (FTIR) the secondary structure of BMP-2 in solution as well as trapped in a biopolymeric thin film. We reveal that the major structural elements of BMP-2 in solution are intramolecular β-sheets and unordered structures as well as α-helices. Furthermore, we studied the secondary structure of rhBMP-2 trapped in hydrated films and in dry films since drying is an important step for future applications of these bioactive films onto orthopedic biomaterials. We demonstrate that the structural elements were preserved when BMP-2 was trapped in the biopolymeric film in hydrated conditions and, to a lesser extent, in dry state. Importantly, its bioactivity was maintained after drying of the film. Our results appear highly promising for future applications of these films as coatings of biomedical materials, to deliver bioactive proteins while preserving their bioactivity upon storage in dry state.This work was supported by the French Ministry of Research through an ANR-EmergenceBIO grant (ANR-09-EBIO-012-01), by the European Commission (FP7 program) via a European Research Council starting grant (BIOMIM, GA 259370), and by GRAVIT (081012_FIBIOS). C.P. is grafetul to IUF for financial support

The role of FKBP5 in cancer aetiology and chemoresistance

FK506 binding protein 51 (FKBP51, also called FKBP5) belongs to a family of immunophilins, FK506 binding proteins (FKBPs). Members of this family are targets for drugs such as rapamycin and cyclosporine. Although FKBP5 shares characteristics with other FKBPs, it also has unique features, especially its role in the regulation of multiple signalling pathways and in tumourigenesis and chemoresistance. In this review, we will focus on the recently discovered role of FKBP5 in cancer aetiology and response to antineoplastic therapy

Timing and minimal access surgery for sciatica: a summary of two randomized trials

Scientific Assessment and Innovation in Neurosurgical Treatment Strategie

Hsp70 chaperones: Cellular functions and molecular mechanism

Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short hydrophobic peptide segments within their substrate proteins. The substrate binding and release cycle is driven by the switching of Hsp70 between the low-affinity ATP bound state and the high-affinity ADP bound state. Thus, ATP binding and hydrolysis are essential in vitro and in vivo for the chaperone activity of Hsp70 proteins. This ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target Hsp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the Hsp70-substrate complex. Additional co-chaperones fine-tune this chaperone cycle. For specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100