Full Lensing Analysis of Abell 1703: Comparison of Independent Lens-Modelling Techniques

The inner mass-profile of the relaxed cluster Abell 1703 is analysed by two very different strong-lensing techniques applied to deep ACS and WFC3 imaging. Our parametric method has the accuracy required to reproduce the many sets of multiple images, based on the assumption that mass approximately traces light. We test this assumption with a fully non-parametric, adaptive grid method, with no knowledge of the galaxy distribution. Differences between the methods are seen on fine scales due to member galaxies which must be included in models designed to search for lensed images, but on the larger scale the general distribution of dark matter is in good agreement, with very similar radial mass profiles. We add undiluted weak-lensing measurements from deep multi-colour Subaru imaging to obtain a fully model-independent mass profile out to the virial radius and beyond. Consistency is found in the region of overlap between the weak and strong lensing, and the full mass profile is well-described by an NFW model of a concentration parameter, $c_{\rm vir}\simeq 7.15\pm0.5$ (and $M_{vir}\simeq 1.22\pm0.15 \times 10^{15}M_{\odot}/h$). Abell 1703 lies above the standard $c$--$M$ relation predicted for the standard $\Lambda$CDM model, similar to other massive relaxed clusters with accurately determined lensing-based profiles.Comment: 12 pages, 17 figures, 1 table, accepted for publication in MNRAS. V2 includes minor changes and revised figure

Larry Bade Interview for the Veterans\u27 Voices Project

Larry Bade (DOB: May 2, 1965) enlisted in the United States Air Force in February 1984. He served as part of Air Force Security Forces with the 379th Bomb Wing, the 487th Missile Wing, 4th Tactical Fighter Wing and 1st Tactical Fighter Wing. He served in many locations including Italy, Korea and the Middle East during Operation Just Cause, Operation Desert Storm and Operation Enduring Freedom. He retired from the Air Force in January 2011 with the rank of E-7 Master Sergeant.https://corescholar.libraries.wright.edu/veterans_voices/1122/thumbnail.jp

A Dileucine in the Protease of Botulinum Toxin A Underlies Its Long-lived Neuroparalysis: TRANSFER OF LONGEVITY TO A NOVEL POTENTIAL THERAPEUTIC*

Blockade of neurotransmitter release by botulinum neurotoxin type A (BoNTA) underlies the severe neuroparalytic symptoms of human botulism, which can last a few years. The structural basis for this remarkable persistence remains unclear. Herein, recombinant BoNTA was found to match the neurotoxicity of that from Clostridium botulinum, producing persistent cleavage of synaptosomal-associated protein of 25 kDa (SNAP-25) and neuromuscular paralysis. When two leucines near the C terminus of the protease light chain of A (LCA) were mutated, its inhibition of exocytosis was followed by fast recovery of intact SNAP-25 in cerebellar neurons and neuromuscular transmission in vivo. Deletion of 6–7 N terminus residues diminished BoNTA activity but did not alter the longevity of its SNAP-25 cleavage and neuromuscular paralysis. Furthermore, genetically fusing LCE to a BoNTA enzymically inactive mutant (BoTIMA) yielded a novel LCE-BoTIMA protein that targets neurons, and the BoTIMA moiety also delivers and stabilizes the inhibitory LCE, giving a potent and persistent cleavage of SNAP-25 with associated neuromuscular paralysis. Moreover, its neurotropism was extended to sensory neurons normally insensitive to BoNTE. LCE-BoTIMA(AA) with the above-identified dileucine mutated gave transient neuromuscular paralysis similar to BoNTE, reaffirming that these residues are critical for the persistent action of LCE-BoTIMA as well as BoNTA. LCE-BoTIMA inhibited release of calcitonin gene-related peptide from sensory neurons mediated by transient receptor potential vanilloid type 1 and attenuated capsaicin-evoked nociceptive behavior in rats, following intraplantar injection. Thus, a long acting, versatile composite toxin has been developed with therapeutic potential for pain and conditions caused by overactive cholinergic nerves