The compatibility of modern slaughter techniques with Halal slaughter:A review of the aspects of “modern” slaughter methods that divide scholarly opinion within the Muslim community

AbstractThe continuous expansion of the global halal meat market has attracted interest from governments, food business operators and the animal and meat science research fraternity. Despite this growing trend, and the enormous economic benefits associated with it, there is a lack of clarity regarding what is ‘authentic’ halal. Many Islamic jurists are reluctant to approve animal slaughter methods that were not practiced at the time of the Prophet of Islam, Mohammed. Others insist that since Islam holds animal welfare in high regard, any modern method of slaughter that is shown to improve animal welfare without compromising on the basic requirements of halal slaughter can be approved for halal production. This paper highlights the aspects of modern slaughter that continues to divide scholarly opinion among Islamic jurists. It also examines the arguments put forward by opponents and proponents regarding the acceptability of modern slaughter techniques for halal slaughter.</jats:p

Oncogenic RET Kinase domain mutations perturb the autophosphorylation trajectory by enhancing substrate presentation in trans

To decipher the molecular basis for RET kinase activation and oncogenic deregulation, we defined the temporal sequence of RET autophosphorylation by label-free quantitative mass spectrometry. Early autophosphorylation sites map to regions flanking the kinase domain core, while sites within the activation loop only form at later time points. Comparison with oncogenic RET kinase revealed that late autophosphorylation sites become phosphorylated much earlier than wild-type RET, which is due to a combination of an enhanced enzymatic activity, increased ATP affinity, and surprisingly, by providing a better intermolecular substrate. Structural analysis of oncogenic M918T and wild-type RET kinase domains reveal a cis-inhibitory mechanism involving tethering contacts between the glycine-rich loop, activation loop, and αC-helix. Tether mutations only affected substrate presentation but perturbed the autophosphorylation trajectory similar to oncogenic mutations. This study reveals an unappreciated role for oncogenic RET kinase mutations in promoting intermolecular autophosphorylation by enhancing substrate presentation

Concern for the ingroup and opposition to affirmative action.

The present experiments suggest that the desire to benefit the in-group drives dominant-group members&apos; policy preferences, independent of concern for out-groups&apos; outcomes. In Experiment 1, the effect of a manipulation of affirmative action procedures on policy support was mediated by how Whites expected the policy to affect fellow Whites, but not by the expected effect on minorities. In Experiments 2 and 3, when focused on losses for the White in-group, Whites&apos; racial identity was negatively related to support for affirmative action. However, when focused on gains for the Black out-group or when participants were told that Whites were not affected by the policy, racial identity did not predict attitudes toward the policy. In Experiments 2 and 3, perceived fairness mediated these effects

Structure and Chemical Inhibition of the Ret Tyrosine Kinase Domain.

The RET proto-oncogene encodes a receptor tyrosine kinase for the glial cell line-derived neurotrophic factor family of ligands. Loss-of-function mutations in RET are implicated in Hirschsprung disease, whereas activating mutations in RET are found in human cancers, including familial medullar thyroid carcinoma and multiple endocrine neoplasias 2A and 2B. We report here the biochemical characterization of the human RET tyrosine kinase domain and the structure determination of the non-phosphorylated and phosphorylated forms. Both structures adopt the same active kinase conformation competent to bind ATP and substrate and have a pre-organized activation loop conformation that is independent of phosphorylation status. In agreement with the structural data, enzyme kinetic data show that autophosphorylation produces only a modest increase in activity. Longer forms of RET containing the juxtamembrane domain and C-terminal tail exhibited similar kinetic behavior, implying that there is no cis-inhibitory mechanism within the RET intracellular domain. Our results suggest the existence of alternative inhibitory mechanisms, possibly in trans, for the autoregulation of RET kinase activity. We also present the structures of the RET tyrosine kinase domain bound to two inhibitors, the pyrazolopyrimidine PP1 and the clinically relevant 4-anilinoquinazoline ZD6474. These structures explain why certain multiple endocrine neoplasia 2-associated RET mutants found in patients are resistant to inhibition and form the basis for design of more effective inhibitors

Mechanistic insight into RET kinase inhibitors targeting the DFG-out conformation in RET-rearranged cancer

Oncogenic fusion events have been identified in a broad range of tumors. Among them, RET rearrangements represent distinct and potentially druggable targets that are recurrently found in lung adenocarcinomas. Here, we provide further evidence that current anti-RET drugs may not be potent enough to induce durable responses in such tumors. We report that potent inhibitors such as AD80 or ponatinib that stably bind in the DFG-out conformation of RET may overcome these limitations and selectively kill RET-rearranged tumors. Using chemical genomics in conjunction with phosphoproteomic analyses in RET-rearranged cells we identify the CCDC6-RETI788N mutation and drug-induced MAPK pathway reactivation as possible mechanisms, by which tumors may escape the activity of RET inhibitors. Our data provide mechanistic insight into the druggability of RET kinase fusions that may be of help for the development of effective therapies targeting such tumors

Low-altitude, high-resolution aerial imaging systems for row and field crop phenotyping: A review

Global plant genetics research efforts have focused on developing high yielding, stress tolerant, and disease resistant row and field crop varieties that are more efficient in their use of agronomic inputs (water, nutrients, pesticides, etc.). Until recently, a key bottleneck in such research was the lack of high-throughput sensing technologies for effective and rapid evaluation of expressed phenotypes under field conditions for holistic data-driven decision making and variety selection. This review focuses on technological aspects of integrating unmanned aerial vehicles with imaging systems to enhance field phenotyping capabilities. The state-of-the-art of unmanned aerial vehicle technology for various applications including crop emergence, vigor, and characterization of yield potential of row and field crops has been reviewed. The potential of using aerial imaging to evaluate resistance/susceptibility to biotic and abiotic stress for crop breeding and precision production management has been discussed along with future perspectives and developments.Keywords: High-throughput field phenomics, Aerial imaging, Crop breeding, Data minin

Structural basis of outer membrane protein insertion by the BAM complex

All Gram-negative bacteria, mitochondria and chloroplasts have outer membrane proteins (OMPs) that perform many fundamental biological processes. The OMPs in Gram-negative bacteria are inserted and folded into the outer membrane by the β-barrel assembly machinery (BAM). The mechanism involved is poorly understood, owing to the absence of a structure of the entire BAM complex. Here we report two crystal structures of the Escherichia coli BAM complex in two distinct states: an inward-open state and a lateral-open state. Our structures reveal that the five polypeptide transport-associated domains of BamA form a ring architecture with four associated lipoproteins, BamB–BamE, in the periplasm. Our structural, functional studies and molecular dynamics simulations indicate that these subunits rotate with respect to the integral membrane β-barrel of BamA to induce movement of the β-strands of the barrel and promote insertion of the nascent OMP