2-bromostearic acid

2-bromostearic acid is a lipid of Fatty Acyls (FA) class.

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There are no associated biomedical information in the current reference collection.

Current reference collection contains 55 references associated with 2-bromostearic acid in LipidPedia. Due to lack of full text of references or no associated biomedical terms are recognized in our current text-mining method, we cannot extract any biomedical terms related to diseases, pathways, locations, functions, genes, lipids, and animal models from the associated reference collection.

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All references with 2-bromostearic acid

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Authors Title Published Journal PubMed Link
pmid:
Suter D and Weidemann MJ Regulation of carbohydrate metabolism in lymphoid tissue. Nature of the endogenous substrates and their contribution to the respiratory fuel of the sliced rat spleen in vitro. 1976 Biochem. J. pmid:182138
Cuendet GS et al. Decreased basal, noninsulin-stimulated glucose uptake and metabolism by skeletal soleus muscle isolated from obese-hyperglycemic (ob/ob) mice. 1976 J. Clin. Invest. pmid:993331
Isenberg H et al. Binding of hydrophobic ligands to spectrin. 1981 FEBS Lett. pmid:7274462
Tamarit-Rodriguez J et al. Starvation-induced secretory changes of insulin, somatostatin, and glucagon and their modification by 2-bromostearate. 1984 Horm. Metab. Res. pmid:6143716
Bedoya FJ et al. Effect of 2-bromostearate on glucose-phosphorylating activities and the dynamics of insulin secretion in islets of Langerhans during fasting. 1984 Diabetes pmid:6381181
Tamarit-Rodríguez J et al. Starvation-induced changes of palmitate metabolism and insulin secretion in isolated rat islets stimulated by glucose. 1984 Biochem. J. pmid:6383345
Bihler I et al. Regulation of glucose transport in Ca2+-tolerant myocytes from adult rat heart. 1985 Biochim. Biophys. Acta pmid:2411296
Vara E et al. Palmitate dependence of insulin secretion, "de novo" phospholipid synthesis and 45Ca2+-turnover in glucose stimulated rat islets. 1988 Diabetologia pmid:3069535
Kahana E et al. Fluorescence quenching of spectrin and other red cell membrane cytoskeletal proteins. Relation to hydrophobic binding sites. 1992 Biochem. J. pmid:1540147

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