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Wiesmann, U. N., S. DiDonato, and N. N. Herschkowitz, "Effect of chloroquine on cultured fibroblasts: release of lysosomal hydrolases and inhibition of their uptake.", Biochemical and biophysical research communications, vol. 66, issue 4, pp. 1338-43, 1975 Oct 27. Abstract
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Poole-Wilson, P. A., and G. A. Langer, "Effect of pH on ionic exchange and function in rat and rabbit myocardium.", The American journal of physiology, vol. 229, issue 3, pp. 570-81, 1975 Sep. Abstract

The effects of pH variation on ionic exchange and mechanical function were studied in the arterially perfused rat and rabbit septa. The pH and PCO2 of the control perfusate were 7.40 and 39 mmHg, respectively. In the rabbit septum a metabolic acidosis (pH equals 6.82, PCO2 equals 39 mmHg) caused a loss of 16% of control tension in 12 min. Na+ and K+ exchange were unaltered. A comparable respiratory acidosis (pH equals 6.81, PCO2 equals 159 mmHg) caused a 51% loss of tension in 2 min. Na+ exchange was unaltered but K+ efflux fell from 8.9 +/- 0.6 (mean +/- SE) to 4.9 +/- 0.3 mmol/kg dry wt per min (P less than 0.001, n equals 10). A net gain of K+ of 16.9 +/- 1.7 (n equals 14) mmol/kg dry wt occurred and was attributable to a delayed fall in K+ influx relative to efflux over 15 min. The net gain could not be mimicked by epinephrine administration or blocked by propranolol and was absent in the beating rat septum and the quiescent rabbit septum. These results suggest that the net uptake of K+, which appears to be dependent on a period of depolarization, and the changes of contractility are controlled by the H+ ion concentration at a cellular site whose exchange with the extracellular space is characterized by a considerable restriction of diffusion. Changes of contractility are not related to the net uptake of K+.

Elkhadem, A., and P. Nagi, "Effectiveness of MTA pulpotomy in primary molars: a critical assessment of relevant studies.", Evidence-based dentistry, vol. 14, issue 2, pp. 46, 2013. Abstract

DATA SOURCES: Medline.

STUDY SELECTION: Studies that evaluated the efficacy of MTA as a pulpotomy medicament in primary teeth were included, abstracts, observational studies and case reports were excluded. Only English language studies were considered.

DATA EXTRACTION AND SYNTHESIS: Studies were assessed and graded by two reviewers using a weighted criteria based system and a qualitative summary of the evidence provided.

RESULTS: Twenty-two studies were included, 17 studies compared MTA with formocresol, four studies compared MTA with calcium hydroxide, ferric sulphate, Portland cement, calcium-enriched mixture cement (CEM) and one study compared white MTA with grey MTA.

CONCLUSIONS: Based on the assessment criteria employed, there was no evidence that MTA was better than present materials and techniques as a pulpotomy medicament.

Fahnestock, S. R., "Evidence of the involvement of a 50S ribosomal protein in several active sites.", Biochemistry, vol. 14, issue 24, pp. 5321-7, 1975 Dec 2. Abstract

The functional role of the Bacillus stearothermophilus 50S ribosomal protein B-L3 (probably homologous to the Escherichia coli protein L2) was examined by chemical modification. The complex [B-L3-23S RNA] was photooxidized in the presence of rose bengal and the modified protein incorporated by reconstitution into 50S ribosomal subunits containing all other unmodified components. Particles containing photooxidized B-L3 are defective in several functional assays, including (1) poly(U)-directed poly(Phe) synthesis, (2) peptidyltransferase activity, (3) ability to associate with a [30S-poly(U)-Phe-tRNA] complex, and (4) binding of elongation factor G and GTP. The rates of loss of the partial functional activities during photooxidation of B-L3 indicate that at least two independent inactivating events are occurring, a faster one, involving oxidation of one or more histidine residues, affecting peptidyltransferase and subunit association activities and a slower one affecting EF-G binding. Therefore the protein B-L3 has one or more histidine residues which are essential for peptidyltransferase and subunit association, and another residue which is essential for EF-G-GTP binding. B-L3 may be the ribosomal peptidyltransferase protein, or a part of the active site, and may contribute functional groups to the other active sites as well.