Labor Law - National Labor Relations Board - Effect of the NLRB\u27s Refusal to Take Jurisdiction

Appellant corporation was charged by the United Steelworkers of America with unfair labor practices in violation of sections 8(a)(1), (3) and (5) of the National Labor Relations Act. Although appellant\u27s business affected commerce within the meaning of the act, the acting regional director of the NLRB declined to issue a complaint because the company\u27s volume of business did not meet the Board\u27s revised minimum jurisdictional standards. The union then filed substantially the same charges with the Utah Labor Relations Board. The Utah Board\u27s determination that it had jurisdiction was affirmed by the Utah Supreme Court. On certiorari to the Supreme Court of the United States, held, reversed, two justices dissenting. The proviso to section 10(a) of the NLRA offers the exclusive means whereby states may assume jurisdiction over matters which Congress has entrusted to the NLRB. Guss v. Utah Labor Board, 353 U.S. I (1957)

The Physics of the B Factories

This work is on the Physics of the B Factories. Part A of this book contains a brief description of the SLAC and KEK B Factories as well as their detectors, BaBar and Belle, and data taking related issues. Part B discusses tools and methods used by the experiments in order to obtain results. The results themselves can be found in Part C

Labor Law - National Labor Relations Board - Effect of the NLRB\u27s Refusal to Take Jurisdiction

Appellant corporation was charged by the United Steelworkers of America with unfair labor practices in violation of sections 8(a)(1), (3) and (5) of the National Labor Relations Act. Although appellant\u27s business affected commerce within the meaning of the act, the acting regional director of the NLRB declined to issue a complaint because the company\u27s volume of business did not meet the Board\u27s revised minimum jurisdictional standards. The union then filed substantially the same charges with the Utah Labor Relations Board. The Utah Board\u27s determination that it had jurisdiction was affirmed by the Utah Supreme Court. On certiorari to the Supreme Court of the United States, held, reversed, two justices dissenting. The proviso to section 10(a) of the NLRA offers the exclusive means whereby states may assume jurisdiction over matters which Congress has entrusted to the NLRB. Guss v. Utah Labor Board, 353 U.S. I (1957)

Potent, specific MEPicides for treatment of zoonotic staphylococci

Coagulase-positive staphylococci, which frequently colonize the mucosal surfaces of animals, also cause a spectrum of opportunistic infections including skin and soft tissue infections, urinary tract infections, pneumonia, and bacteremia. However, recent advances in bacterial identification have revealed that these common veterinary pathogens are in fact zoonoses that cause serious infections in human patients. The global spread of multidrug-resistant zoonotic staphylococci, in particular the emergence of methicillin-resistant organisms, is now a serious threat to both animal and human welfare. Accordingly, new therapeutic targets that can be exploited to combat staphylococcal infections are urgently needed. Enzymes of the methylerythritol phosphate pathway (MEP) of isoprenoid biosynthesis represent potential targets for treating zoonotic staphylococci. Here we demonstrate that fosmidomycin (FSM) inhibits the first step of the isoprenoid biosynthetic pathway catalyzed by deoxyxylulose phosphate reductoisomerase (DXR) in staphylococci. In addition, we have both enzymatically and structurally determined the mechanism by which FSM elicits its effect. Using a forward genetic screen, the glycerol-3-phosphate transporter GlpT that facilitates FSM uptake was identified in two zoonotic staphylococci, Staphylococcus schleiferi and Staphylococcus pseudintermedius. A series of lipophilic ester prodrugs (termed MEPicides) structurally related to FSM were synthesized, and data indicate that the presence of the prodrug moiety not only substantially increased potency of the inhibitors against staphylococci but also bypassed the need for GlpT-mediated cellular transport. Collectively, our data indicate that the prodrug MEPicides selectively and robustly inhibit DXR in zoonotic staphylococci, and further, that DXR represents a promising, druggable target for future development

<i>Fasciola hepatica</i> cathepsin L-like proteases: biology, function and potential in the development of first generation liver fluke vaccines.

Fasciola hepatica secretes cathepsin L proteases that facilitate the penetration of the parasite through the tissues of its host, and also participate in functions such as feeding and immune evasion. The major proteases, cathepsin L1 (FheCL1) and cathepsin L2 (FheCL2) are members of a lineage that gave rise to the human cathepsin Ls, Ks and Ss, but while they exhibit similarities in their substrate specificities to these enzymes they differ in having a wider pH range for activity and an enhanced stability at neutral pH. There are presently 13 Fasciola cathepsin L cDNAs deposited in the public databases representing a gene family of at least seven distinct members, although the temporal and spatial expression of each of these members in the developmental stage of F. hepatica remains unclear. Immunolocalisation and in situ hybridisation studies, using antibody and DNA probes, respectively, show that the vast majority of cathepsin L gene expression is carried out in the epithelial cells lining the parasite gut. Within these cells the enzyme is packaged into secretory vesicles that release their contents into the gut lumen for the purpose of degrading ingested host tissue and blood. Liver flukes also express a novel multi-domain cystatin that may be involved in the regulation of cathepsin L activity. Vaccine trials in both sheep and cattle with purified native FheCL1 and FheCL2 have shown that these enzymes can induce protection, ranging from 33 to 79%, to experimental challenge with metacercariae of F. hepatica, and very potent anti-embryonation/hatch rate effects that would block parasite transmission. In this article we review the vaccine trials carried out over the past 8 years, the role of antibody and T cell responses in mediating protection and discuss the prospects of the cathepsin Ls in the development of first generation recombinant liver fluke vaccines. © 2003 Australian Society for Parasitology Inc. Published by Elsevier Ltd. All rights reserved

A comparison of individual and combined L-phenylalanine ammonia lyase and cationic peroxidase transgenes for engineering resistance in tobacco to necrotrophic pathogens

This study tested the relative and combined efficacy of ShPx2 and ShPAL transgenes by comparing Nicotianatabacum hybrids with enhanced levels of l-phenylalanine ammonia lyase (PAL) activity and cationic peroxidase (Prx) activity with transgenic parental lines that overexpress either transgene. The PAL/Prx hybrids expressed both transgenes driven by the 35S CaMV promoter, and leaf PAL and Prx enzyme activities were similar to those of the relevant transgenic parent and seven- to tenfold higher than nontransgenic controls. Lignin levels in the PAL/Prx hybrids were higher than the PAL parent and nontransgenic controls, but not significantly higher than the Prx parent. All transgenic plants showed increased resistance to the necrotrophs Phytophthora parasitica pv. nicotianae and Cercospora nicotianae compared to nontransgenic controls, with a preponderance of smaller lesion categories produced in Prx-expressing lines. However, the PAL/Prx hybrids showed no significant increase in resistance to either pathogen relative to the Prx parental line. These data indicate that, in tobacco, the PAL and Prx transgenes do not act additively in disease resistance. Stacking with Prx did not prevent a visible growth inhibition from PAL overexpression. Practical use of ShPAL will likely require more sophisticated developmental control, and we conclude that ShPx2 is a preferred candidate for development as a resistance transgene