306 research outputs found

    SLIDES: Shale and Air Quality: The View from the Other Side

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    Presenter: Jeremy Nichols, Climate & Energy Program Director, WildEarth Guardians, Denver, CO 18 slide

    SLIDES: Shale and Air Quality: The View from the Other Side

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    Presenter: Jeremy Nichols, Climate & Energy Program Director, WildEarth Guardians, Denver, CO 18 slide

    The Vaccinia-related Kinases Phosphorylate the N\u27 Terminus of BAF, Regulating Its Interaction with DNA and Its Retention in the Nucleus

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    The vaccinia-related kinases (VRKs) comprise a branch of the casein kinase family whose members are characterized by homology to the vaccinia virus B1 kinase. The VRK orthologues encoded by Caenorhabditis elegans and Drosophila melanogaster play an essential role in cell division; however, substrates that mediate this role have yet to be elucidated. VRK1 can complement the temperature sensitivity of a vaccinia B1 mutant, implying that VRK1 and B1 have overlapping substrate specificity. Herein, we demonstrate that B1, VRK1, and VRK2 efficiently phosphorylate the extreme N\u27 terminus of the BAF protein (Barrier to Autointegration Factor). BAF binds to both DNA and LEM domain–containing proteins of the inner nuclear membrane; in lower eukaryotes, BAF has been shown to play an important role during the reassembly of the nuclear envelope at the end of mitosis. We demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of BAF with DNA and reduces its interaction with the LEM domain. Coexpression of VRK1 and GFP-BAF greatly diminishes the association of BAF with the nuclear chromatin/matrix and leads to its dispersal throughout the cell. Cumulatively, our data suggest that the VRKs may modulate the association of BAF with nuclear components and hence play a role in maintaining appropriate nuclear architecture

    The Vaccinia-related Kinases Phosphorylate the N\u27 Terminus of BAF, Regulating Its Interaction with DNA and Its Retention in the Nucleus

    Get PDF
    The vaccinia-related kinases (VRKs) comprise a branch of the casein kinase family whose members are characterized by homology to the vaccinia virus B1 kinase. The VRK orthologues encoded by Caenorhabditis elegans and Drosophila melanogaster play an essential role in cell division; however, substrates that mediate this role have yet to be elucidated. VRK1 can complement the temperature sensitivity of a vaccinia B1 mutant, implying that VRK1 and B1 have overlapping substrate specificity. Herein, we demonstrate that B1, VRK1, and VRK2 efficiently phosphorylate the extreme N\u27 terminus of the BAF protein (Barrier to Autointegration Factor). BAF binds to both DNA and LEM domain–containing proteins of the inner nuclear membrane; in lower eukaryotes, BAF has been shown to play an important role during the reassembly of the nuclear envelope at the end of mitosis. We demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of BAF with DNA and reduces its interaction with the LEM domain. Coexpression of VRK1 and GFP-BAF greatly diminishes the association of BAF with the nuclear chromatin/matrix and leads to its dispersal throughout the cell. Cumulatively, our data suggest that the VRKs may modulate the association of BAF with nuclear components and hence play a role in maintaining appropriate nuclear architecture

    Wildcat Bridge - I-65 Artesion Well/Geotechnical/Structural

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    In this session we will discuss the emergency design and repair of the I-65 bridge over Wildcat Creek in Tippecanoe County during the summer of 2015 that closed I-65 northbound

    Editorial:LRRK2-Fifteen Years From Cloning to the Clinic

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    none4noneRideout, Hardy; Greggio, Elisa; Kortholt, Arjan; Nichols, R JeremyRideout, Hardy; Greggio, Elisa; Kortholt, Arjan; Nichols, R Jerem

    Functional characterization of the vaccinia virus I5 protein

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    The I5L gene is one of ~90 genes that are conserved throughout the chordopoxvirus family, and hence are presumed to play vital roles in the poxvirus life cycle. Previous work had indicated that the VP13 protein, a component of the virion membrane, was encoded by the I5L gene, but no additional studies had been reported. Using a recombinant virus that encodes an I5 protein fused to a V5 epitope tag at the endogenous locus (vI5V5), we show here that the I5 protein is expressed as a post-replicative gene and that the ~9 kDa protein does not appear to be phosphorylated in vivo. I5 does not appear to traffic to any cellular organelle, but ultrastructural and biochemical analyses indicate that I5 is associated with the membranous components of assembling and mature virions. Intact virions can be labeled with anti-V5 antibody as assessed by immunoelectron microscopy, indicating that the C' terminus of the protein is exposed on the virion surface. Using a recombinant virus which encodes only a TET-regulated copy of the I5V5 gene (vΔindI5V5), or one in which the I5 locus has been deleted (vΔI5), we also show that I5 is dispensable for replication in tissue culture. Neither plaque size nor the viral yield produced in BSC40 cells or primary human fibroblasts are affected by the absence of I5 expression

    Numerical Evaluation of Micro-Pocket Fission Detectors

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    Micro-pocket fission detectors (MPFDs) are miniature fission chambers suitable for in-core neutron measurement that have been under development at Kansas State University for over one decade. Current-generation devices have been used at a number of university reactors (Kansas State, Wisconsin, and MIT) and as part of the first experiments performed during the recent restart of TREAT. Ongoing research aims to improve understanding of the existing MPFDs and to optimize designs for future deployment. To aid in this development, the dynamic response of a prototypic MPFD was evaluated using Garfield++, Elmer, Gmsh, and Stopping and Range of Ions in Matter (SRIM). Specifically, the finite-element code Elmer was used to calculate the electric field on a mesh generated by Gmsh. SRIM was used to compute the energy loss tables of the fission fragments in the gas. With output from Elmer and SRIM, Garfield++ was used to simulate the ionization process, the resulting electron drift, and the induced signal. This particular Garfield++ application was developed with hybrid parallelization based MPI and OpenMP. The performance of the MPFDs subjected to different temperatures and applied voltages was evaluated. The preliminary results indicate the fission fragment deposits a few MeV of energy in the gas, consistent with previous estimates. The pulses in the MPFDs can be formed in the nanosecond scale, thus accommodating high count rates and, hence, high neutron-flux levels. Ongoing work aims to extend this model and validate it against existing and planned experimental data

    Chronic Exertional Compartment Syndrome: A Case Report about Claudication in a Healthy Adult

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    Claudication occurs when the blood supply is insufficient to service the musculature in the body with oxygen and metabolic waste management. A clinical complaint of claudication is commonly seen in primary care among older patients with vascular risk factors. A young and healthy patient presenting with claudication is less common and often results in delayed diagnosis with numerous extraneous diagnostic studies. This case discusses a young, healthy male patient with lower extremity symptoms that got worse with exercise and better with rest. He had normal physical exam findings leading to multiple diagnostic studies and over 12 months between the onset of symptoms and his return to full activity. Claudication can result from rare conditions, such as chronic exertional compartment syndrome, popliteal artery entrapment syndrome, fibromuscular dysplasia, and cystic adventitial disease. Symptomatic individuals with chronic exertional compartment syndrome experience reversible muscular pain from exercise-induced pressure, which increases within the finite spaces of any muscular compartment. Understanding the pathophysiology of exertional compartment syndrome and its related diagnoses allows for an organized diagnostic approach to young, healthy patients with claudication symptoms. This organized approach allows timely care, which is imperative for primary care physicians to reduce the number of tests performed, decrease the time to diagnosis, and reduce both the anxiety and cost for the patient. The approach presented herein can serve as a reminder of a proper work-up in similar patients and allow practitioners to identify the conditions that require intervention to improve outcomes
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