Investigations for the Optimization of Metal Freeforming using the ARBURG freeformer

The ARBURG freeformer represents an additive manufacturing system for producing thermoplastic components using commercially available polymer granulate. This fabrication process offers the potential to use feedstocks known from the metal injection molding (MIM) sector to manufacture so-called green parts. These parts consist of 60 Vol.-% stainless steel powder and 40 Vol-% organic polymer binding system. By debinding and sintering these green parts, it is possible to economically produce full metal components with mechanical properties comparable to metal injection molding. In this publication, the process of producing stainless steel parts with ARBURG plastic freeforming will be presented. The mechanical properties and part density are optimized by varying manufacturing parameters and raw materials. Furthermore, concepts to optimize and increase the service life of the nozzle are shown and discussed. An increase of at least 250% could be achieved by plasma nitriding and coating components of the discharge system

Prospectus, March 12, 1971

PARKLAND LIBRARY IS MEETING NEEDS OF STUDENTS ; Letter To Students; Universities Are Defenseless; Guest Column; Uncle Sam Wants You (a come on); Letter To Editor; Concert Critique; Bull Page: Used Books, Yearbook, Parking Problems, Wit N\u27 Wisdom, Music Minded?, Class Rings, Petitions Due, Gemini House, Final Week Movies, No Paper, Road Rally, Hotline; All Things Must Pass: Reflections On The Frazier-Ali Fight; Baseball Season Underway; Chet Lewis To Nat\u27l.https://spark.parkland.edu/prospectus_1971/1010/thumbnail.jp

Prospectus, February 12, 1971

S.A.S.L.A. IS STARTED FOR STUDENT BENEFIT: ILLIACS TO TAKE ACTION; Veterans Association Co-Sponsors Boy Scouts; Problems Of Our Times: This Business Of Space; Letters To Editor; An Editorial; Bull Page: Coffee House, New Club, Family Night, SASLA, W. I. U. Transfer, SWAMP, Fail Safe, Vets Meeting, Hotline, Gemini House, Wit N\u27 Wisdom, No Paper; Champion Gymnast Teaches At Parkland; Parkland Wins Triangular; Parkland Defeats Lincoln Land; District Playoffs Announced; Mad Dogs Win Green Division; Swim Meet Belley Flops; Intramural Playoffs; Indoor Track Schedule; Intramural Standings; Track Team Shows Strengthhttps://spark.parkland.edu/prospectus_1971/1012/thumbnail.jp

Prevalence of Disorders Recorded in Dogs Attending Primary-Care Veterinary Practices in England

Purebred dog health is thought to be compromised by an increasing occurence of inherited diseases but inadequate prevalence data on common disorders have hampered efforts to prioritise health reforms. Analysis of primary veterinary practice clinical data has been proposed for reliable estimation of disorder prevalence in dogs. Electronic patient record (EPR) data were collected on 148,741 dogs attending 93 clinics across central and south-eastern England. Analysis in detail of a random sample of EPRs relating to 3,884 dogs from 89 clinics identified the most frequently recorded disorders as otitis externa (prevalence 10.2%, 95% CI: 9.1-11.3), periodontal disease (9.3%, 95% CI: 8.3-10.3) and anal sac impaction (7.1%, 95% CI: 6.1-8.1). Using syndromic classification, the most prevalent body location affected was the head-and-neck (32.8%, 95% CI: 30.7-34.9), the most prevalent organ system affected was the integument (36.3%, 95% CI: 33.9-38.6) and the most prevalent pathophysiologic process diagnosed was inflammation (32.1%, 95% CI: 29.8-34.3). Among the twenty most-frequently recorded disorders, purebred dogs had a significantly higher prevalence compared with crossbreds for three: otitis externa (P = 0.001), obesity (P = 0.006) and skin mass lesion (P = 0.033), and popular breeds differed significantly from each other in their prevalence for five: periodontal disease (P = 0.002), overgrown nails (P = 0.004), degenerative joint disease (P = 0.005), obesity (P = 0.001) and lipoma (P = 0.003). These results fill a crucial data gap in disorder prevalence information and assist with disorder prioritisation. The results suggest that, for maximal impact, breeding reforms should target commonly-diagnosed complex disorders that are amenable to genetic improvement and should place special focus on at-risk breeds. Future studies evaluating disorder severity and duration will augment the usefulness of the disorder prevalence information reported herein

Highly active and stable Pt-Ni/CeO 2 -SiO 2 catalysts for ethanol reforming

<p>Acetylated lysines identified in MAP2c</p

Conserved Lysine Acetylation within the Microtubule-Binding Domain Regulates MAP2/Tau Family Members

<div><p>Lysine acetylation has emerged as a dominant post-translational modification (PTM) regulating tau proteins in Alzheimer’s disease (AD) and related tauopathies. Mass spectrometry studies indicate that tau acetylation sites cluster within the microtubule-binding region (MTBR), a region that is highly conserved among tau, MAP2, and MAP4 family members, implying that acetylation could represent a conserved regulatory mechanism for MAPs beyond tau. Here, we combined mass spectrometry, biochemical assays, and cell-based approaches to demonstrate that the tau family members MAP2 and MAP4 are also subject to reversible acetylation. We identify a cluster of lysines in the MAP2 and MAP4 MTBR that undergo CBP-catalyzed acetylation, many of which are conserved in tau. Similar to tau, MAP2 acetylation can occur in a cysteine-dependent auto-regulatory manner in the presence of acetyl-CoA. Furthermore, tubulin reduced MAP2 acetylation, suggesting tubulin binding dictates MAP acetylation status. Taken together, these results uncover a striking conservation of MAP2/Tau family post-translational modifications that could expand our understanding of the dynamic mechanisms regulating microtubules.</p></div

Tau, MAP2c, and MAP4 sequence alignments illustrate extensive MTBR homology and conservation of critical lysines

<p>The microtubule-binding repeats 1–4 from tau, MAP2c, and MAP4 were aligned and exact amino acid homology among the MAPs is depicted with red shading. Solid black lines identify two putative MAP acetylation motifs (see Tables <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0168913#pone.0168913.t001" target="_blank">1</a> and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0168913#pone.0168913.t002" target="_blank">2</a> for all identified acetylated residues), and specific acetylated lysines that are enriched within the identified motifs are highlighted above the indicated lysine residues with filled black circles.</p

MAPs are subject to auto-acetylation within the MTBR domain

<p><b>A)</b> Recombinant tau-K18 (residues 244–372) or MAP2c (residues 280–388) fragments were incubated in acetylation reactions containing [¹⁴C]-labeled acetyl-CoA followed by SDS-PAGE and phosphorimaging using Storm software to detect radiolabeled MAPs. <b>B)</b> Immunoprecipitated 2N4R tau (lane 1), 2N4R-2CA mutant tau (lane 2), or MAP2c proteins (lane 6) derived from QBI-293 lysates were immobilized on agarose beads, incubated with [¹⁴C]-Acetyl-CoA, and analyzed by SDS-PAGE and Coomassie staining followed by phosphorimaging analysis. Replicate IgG control samples (lanes 3–5) were used to clearly separate signal intensities from tau and MAP2c sample lanes. <b>C)</b> Purified MTBR fragments from wild-type MAP2c (280–388), a comparable MAP2c fragment containing a cysteine→alanine substitution (C348A), or MAP4 (925–1102) were incubated in acetylation reactions and direct incorporation of radiolabeled acetyl groups was quantified using a liquid scintillation analyzer. Shown are representative analysis using N = 3 technical replicates from N = 3 independent experiments.</p

MAP interactions with tubulin impair MAP acetylation

<p><b>A)</b> Bovine brain derived MAP-rich fractions were incubated in the absence or presence of increasing concentrations of tubulin (1–10 μM), and analyzed in auto-acetylation reactions containing [¹⁴C]-acetyl-CoA. <b>B)</b> Reactions similar to <b>(A)</b> above were incubated with unlabeled acetyl-CoA in the presence of tubulin and analyzed by immunoblotting using acetylated lysine (Acetyl-Lys), acetylated tau (Ac-K280), and total tau (T46) antibodies. We note that the addition of tubulin progressively inhibited tau and MAP2 acetylation. Shown are representative gels and immunoblots from N = 3 independent experiments.</p