The Bethe ansatz approach for factorizable centrally extended S-matrices

We consider the Bethe ansatz solution of integrable models interacting through factorized $S$-matrices based on the central extention of the $\bf{su}(2|2)$ symmetry. The respective $\bf{su}(2|2)$ $R$-matrix is explicitly related to that of the covering Hubbard model through a spectral parameter dependent transformation. This mapping allows us to diagonalize inhomogeneous transfer matrices whose statistical weights are given in terms of $\bf{su}(2|2)$ $S$-matrices by the algebraic Bethe ansatz. As a consequence of that we derive the quantization condition on the circle for the asymptotic momenta of particles scattering by the $\bf{su}(2|2) \otimes \bf{su}(2|2)$ $S$-matrix. The result for the quantization rule may be of relevance in the study of the energy spectrum of the $AdS_5 \times S^{5}$ string sigma model in the thermodynamic limit. \Comment: 22 pages, published versio

Improving Supervisor Evaluations Through the Use of Self Determination Contracts

Supervisor perceptions of employee competence in areas of work, social, and personal demands of the job often determine success or failure for the supported employee. This study involved three workers with disabilities who participated in a supported employment program. After being successfully hired in a job of their choosing, problems arose that jeopardized the successful completion of the placement phase. The workers used individualized self-determination contracts to improve supervisor evaluations. Specifically, they completed daily self-determination contracts to plan their work outcomes, manage their tasks, evaluate their performance, and make adjustments for their next opportunity to work. Results indicated that all three workers used self-determination strategies to improve their performance and meet the expectations of their respective employers.Yeshttps://us.sagepub.com/en-us/nam/manuscript-submission-guideline

The Snf1-related protein kinases SnRK2.4 and SnRK2.10 are involved in maintenance of root system architecture during salt stress

The Sucrose non-fermenting-1 related protein kinase 2 (SnRK2) family represents a unique family of plant specific-protein kinases implicated in cellular signalling in response to osmotic stress. In our studies, we observed that two class 1 SnRK2 kinases, SnRK2.4 and SnRK2.10, are rapidly and transiently activated in Arabidopsis roots after exposure to salt. Under saline conditions, snrk2.4 knockout mutants had a reduced primary root length, while snrk2.10 mutants exhibited a reduction in the number of lateral roots. The reduced lateral root density was found to be a combinatory effect of a decrease in the amount of lateral root primordia and an increase in the amount of arrested lateral root primordia. The phenotypes were in agreement with the observed expression patterns of genomic YFP-fusions of SnRK2.10 and 2.4, under control of their native promoter sequences. SnRK2.10 was found to be expressed in the vascular tissue at the base of a developing lateral root, whereas SnRK2.4 was expressed throughout the root, with higher expression in the vascular system. Salt stress triggered a rapid re-localization of SnRK2.4-YFP from the cytosol to punctate structures in root epidermal cells. Differential centrifugation experiments of isolated Arabidopsis root proteins, confirmed recruitment of endogenous SnRK2.4/2.10 to membranes upon exposure to salt, supporting their observed binding affinity for the phospholipid phosphatidic acid. Together, our results reveal a role for SnRK2.4 and 2.10 in root growth and architecture in saline conditions. (c) 2012 The Authors. The Plant Journal (c) 2012 Blackwell Publishing Ltd

Identification and functional characterization of the Arabidopsis Snf1-related protein kinase SnRK2.4 phosphatidic acid-binding domain

Phosphatidic acid (PA) is an important signalling lipid involved in various stress-induced signalling cascades. Two SnRK2 protein kinases (SnRK2.4 and SnRK2.10), previously identified as PA-binding proteins, are shown here to prefer binding to PA over other anionic phospholipids and to associate with cellular membranes in response to salt stress in Arabidopsis roots. A 42 amino acid sequence was identified as the primary PA-binding domain (PABD) of SnRK2.4. Unlike the full-length SnRK2.4, neither the PABD-YFP fusion protein nor the SnRK2.10 re-localized into punctate structures upon salt stress treatment, showing that additional domains of the SnRK2.4 protein are required for its re-localization during salt stress. Within the PABD, five basic amino acids, conserved in class 1 SnRK2s, were found to be necessary for PA binding. Remarkably, plants overexpressing the PABD, but not a non-PA-binding mutant version, showed a severe reduction in root growth. Together, this study biochemically characterizes the PA-SnRK2.4 interaction and shows that functionality of the SnRK2.4 PABD affects root development