Pull-down of Biotinylated RNA and Associated Proteins.

Mapping networks of RNA-protein interactions in cells is essential for understanding the inner workings of many biological processes, including RNA processing, trafficking, and translation. Current methods for studying protein-RNA interactions rely mostly on purification of poly(A) transcripts, which represent only ~2-3% of total RNAs (). Alternate robust methods for tagging RNA molecules with an RNA aptamer (, MS2-, U1A- and biotin-RNA aptamer) and capturing the RNA-protein complex by the respective aptamer-specific partner are not extensively studied.

Phosphorylation of Pal2 by the protein kinases Kin1 and Kin2 modulates mRNA splicing in the unfolded protein response in yeast.

During cellular stress in the budding yeast , an endoplasmic reticulum (ER)-resident dual kinase and RNase Ire1 splices an intron from mRNA in the cytosol, thereby releasing its translational block. Hac1 protein then activates an adaptive cellular stress response called the unfolded protein response (UPR) that maintains ER homeostasis. The polarity-inducing protein kinases Kin1 and Kin2 contribute to mRNA processing.

Legal support to gain access to medical treatment in the current healthcare system is unproductive.

The National Health Service in UK is facing grave financial crisis. Recently, 65% of Acute Trusts have reported a collective deficit of £2.5 billion.

Adaptation to Endoplasmic Reticulum Stress Requires Transphosphorylation within the Activation Loop of Protein Kinases Kin1 and Kin2, Orthologs of Human Microtubule Affinity-Regulating Kinase.

Perturbations in endoplasmic reticulum (ER) homeostasis, a condition termed ER stress, activate the unfolded protein response (UPR), an intracellular network of signaling pathways. Recently, we have shown that protein kinase Kin1 and its paralog, Kin2, in the budding yeast (orthologs of microtubule affinity-regulating kinase in humans) contribute to the UPR function. These Kin kinases contain a conserved kinase domain and an autoinhibitory kinase-associated 1 (KA1) domain separated by a long undefined domain.

Phosphorylation of translation initiation factor eIF2α at Ser51 depends on site- and context-specific information.

Protein kinases phosphorylate specific amino acid residues of substrate proteins and regulate many cellular processes. Specificity for phosphorylation depends on the accessibility of these residues, and more importantly, kinases have preferences for certain residues flanking the phospho-acceptor site. Translation initiation factor 2α [eukaryotic translation initiation factor 2α (eIF2α)] kinase phosphorylates serine51 (Ser51) of eIF2α and downregulates cellular protein synthesis.

Financial implications of laparoscopic hot gallbladder service in a nontertiary District General Hospital.

Introduction: The service of providing index admission laparoscopic cholecystectomy (IALC), as recommended by NIC guidelines, often falls short in nontertiary centres because of a combination of limited resources and financial constraints.

Methods: This retrospective study in a single-centre District General Hospital included 50 patients, eligible to undergo IALC, and calculated potential savings from performing IALC on the day of admission by considering admission tariffs, bed, and operating costs.

Results: The IALC was provided in 19 patients (38%), with a mean delay from admission to operation of (median) 3 days.