We initiate the representation theory of restricted Lie superalgebras over an algebraically closed field of characteristic p > 2. A superalgebra generalization of the celebrated Kac-Weisfeiler Conjecture is formulated, which exhibits a mixture of p-power and 2-power divisibilities of dimensions of modules. We establish the Conjecture for basic classical Lie superalgebras.

We report preliminary results on the analysis of the three-body Υ( 10860) → B Bπ, Υ(10860) → [B B * + c.c.]π and Υ(10860) → B * B * π decays including an observation of the Υ(10860) → Z ± b (10610)π ∓ → [B B * + c.c.] ± π ∓ and Υ(10860) → Z ± b (10650)π ∓ → [B * B * ] ± π ∓ decays as intermediate channels. We measure branching fractions of the three-body decays to be B(Υ(10860) → [B B * + c.c.] ± π ∓ ) = (28.3 ± 2.9 ± 4.6) × 10 −3 and B(Υ(10860) → [B * B * ] ± π ∓ ) = (14.1 ± 1.9 ± 2.4) × 10 −3 and set 90% C.L. upper limit B(Υ(10860) → [B B] ± π ∓ ) < 4.0 × 10 −3 . We also report results on the amplitude analysis of the three-body Υ(10860) → Υ(nS)π + π − , n = 1, 2, 3 decays and the analysis of the internal structure of the three-body Υ(10860) → h b (mP )π + π − , m = 1, 2 decays. The results are based on a 121.4 fb −1 data sample collected with the Belle detector at a center-of-mass energy near the Υ(10860).

A series of vanillin derivatives incorporating a bis(2-hydroxyethyl)dithioacetal moiety was designed and synthesized via a facile method. A plausible reaction pathway was proposed and verified by computational studies. Bioassay results demonstrated that target compounds possessed good to excellent activities against potato virus Y (PVY) and cucumber mosaic virus (CMV), of which, compound 6f incorporating a bis(2-hydroxyethyl)dithioacetal moiety, exhibited the best curative and protection activities against PVY and CMV in vivo, with 50% effective concentration values of 217.6, 205.7 μg/mL and 206.3, 186.2 μg/mL, respectively, better than those of ribavirin (848.0, 808.1 μg/mL and 858.2, 766.5 μg/mL, respectively), dufulin (462.6, 454.8 μg/mL and 471.2, 465.4 μg/mL, respectively), and ningnanmycin (440.5, 425.3 μg/mL and 426.1, 405.3 μg/mL, respectively). Current studies provide support for the application of vanillin derivatives incorporating bis(2-hydroxyethyl)dithioacetal as new antiviral agents.

The lymphoid tyrosine phosphatase LYP, encoded by the PTPN22 gene, recently emerged as an important risk factor and drug target for human autoimmunity. Here we solved the structure of the catalytic domain of LYP, which revealed noticeable differences with previously published structures. The active center with a semi-closed conformation binds phosphate ion, which may represent an intermediate conformation after de-phosphorylation of the substrate but before release of the phosphate product. The structure also revealed an unusual disulfide bond formed between the catalytic Cys and one of the two Cys residues nearby, which is not observed in previously determined structures. Our structural and mutagenesis data suggest that the disulfide bond may play a role in protecting the enzyme from irreversible oxidation. Surprisingly, we found that the two non-catalytic Cys around the active center exert an opposite yin-yang regulation on the catalytic Cys activity. These detailed structure and functional characterizations have provided new insight into auto-regulatory mechanisms of LYP function.Regulating tyrosine phosphorylation level is a fundamental mechanism for numerous important aspects of eukaryote physiology, as well as human health and disease (1-3). Cellular tyrosine phosphorylation levels are regulated by the antagonistic activities of two classes of enzymes, the protein tyrosine kinases (PTKs) 1 and the protein tyrosine phosphatases (PTPs). Recent findings have led to the emerging recognition that PTPs play specific and even dominant roles in setting the levels of tyrosine phosphorylation in cells and in the regulation of many physiological processes (2-7). Disruption of the equilibrium maintained by PTPs and PTKs causes a range of human disease, including cancer, diabetes, and autoimmunity (8-16).A major class of PTPs, known as classical PTPs, include transmembrane PTPs and nonreceptor PTPs (NRPTP), which are then further sub-classified based on their sequence similarities and non-catalytic domain structural motifs (4,8). NRPTPs display various ‖ The coordinates and structure factors for the disulfide structure of PTPN22 (PDB ID: 3H2X) The importance of LYP in immune system regulation has been recently demonstrated by the finding that a human variant W620, caused by a single nucleotide polymorphism in PTPN22 at nucleotide 1858, leads to a significantly increased risk for autoimmune diseases including type-1 diabetes, rheumatoid arthritis and systemic lupus erythematosus (11,16,18,19). Since the autoimmune-predisposing LYP-W620 variant is a gain-of-function mutation and shows increased phosphatase activity (20), LYP is currently considered a promising drug target for autoimmunity. Elucidation of the structure and regulation of LYP is important in order to understand its mechanism of action in autoimmunity and to develop innovative approaches to the pharmacological inhibition of the enzyme for therapeutic purposes.One possible mechanism of regulating cysteine-based PTP activity is through oxidation of t...

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