Changes in the size of the thyroid in patients with benign non-toxic multinodular goiter after radioactive iodine therapy.

Multinodular goiter (MNG) is regarded as one of the most common causes of hyperthyroidism, particularly in areas of mild-to-moderate iodine deficiency. The present study aims to explore the effects of the radioactive iodine (RAI) therapy on benign non-toxic MNG and evaluate its side effects. Patients with benign non-toxic MNG entered the study.

A patient education program is cost-effective for preventing failure of endoscopic procedures in a gastroenterology department.

Objective: The growing use and complexity of endoscopy procedures in GI units has increased the need for good patient preparation. Earlier studies in this area have focused on the psychological benefits of patient education programs. The present study was directed at determining cost-effectiveness of a patient education program.

Detection of anticodon nuclease residues involved in tRNALys cleavage specificity.

The tRNALys-specific anticodon nuclease exists in latent form in Escherichia coli strains containing the optional prr locus. The latency is a result of a masking interaction between the anticodon nuclease core-polypeptide PrrC and the Type IC DNA restriction-modification enzyme EcoprrI. Activation of the latent enzyme by phage T4-infection elicits cleavage of tRNALys 5' to the wobble base, yielding 5'-OH and 2', 3'-cyclic phosphate termini.

Phage T4-coded Stp: double-edged effector of coupled DNA and tRNA-restriction systems.

The optional Escherichia coli prr locus encodes two physically associated restriction systems: the type IC DNA restriction-modification enzyme EcoprrI and the tRNA(Lys)-specific anticodon nuclease, specified by the PrrC polypeptide. Anticodon nuclease is kept latent as a result of this interaction. The activation of anticodon nuclease, upon infection by phage T4, may cause depletion of tRNA(Lys) and, consequently, abolition of T4 protein synthesis.

Cleavage of the HIV replication primer tRNALys,3 in human cells expressing bacterial anticodon nuclease.

Anticodon nuclease is a bacterial restriction enzyme directed against tRNA(Lys). We report that anticodon nuclease also cleaves mammalian tRNA(Lys) molecules, with preference and site specificity shown towards the natural substrate. Expression of the anticodon nuclease core polypeptide PrrC in HeLa cells from a recombinant vaccinia virus elicited cleavage of intracellular tRNA(Lys),3.