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	1.	Kinetic characterization of [125I] iodo-prolactin in binding to primary monolayer cultures of rabbit mammary epithelium. [electronic resource] by Soltysiak, R M Fellows, R E Producer: 19820917 In: Journal of receptor research vol. 2 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	2.	The effect of cyclic nucleotides on virus infection. [electronic resource] by Maassab, H F Soltysiak, R M Producer: 19781227 In: Annals of the New York Academy of Sciences vol. 284 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	3.	Prolactin receptor expression in monolayer cultures of rabbit mammary epithelial cells: pre- and postpartum [125I]-prolactin binding activity. [electronic resource] by Soltysiak, R M Fellows, R E Producer: 19840511 In: Journal of cellular biochemistry vol. 22 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	4.	Regulation of membrane-bound enzymes of glycosphingolipid biosynthesis. [electronic resource] by Burczak, J D Soltysiak, R M Sweeley, C C Producer: 19850521 In: Journal of lipid research vol. 25 Availability: No items available. Save to lists Add to cart (remove)
	5.	Glycolipid N-acetylgalactosaminyltransferase activities in normal and Kirsten murine sarcoma virus transformed BALB/c 3T3 cells. [electronic resource] by Lockney, M W Soltysiak, R M Sweeley, C C Producer: 19821218 In: Advances in experimental medicine and biology vol. 152 Availability: No items available. Save to lists Add to cart (remove)
	6.	D,L-alpha-Fluoropalmitic acid inhibits sphingosine base formation and accumulates in membrane lipids of cultured mammalian cells. [electronic resource] by Soltysiak, R M Matsuura, F Bloomer, D Sweeley, C C Producer: 19840404 In: Biochimica et biophysica acta vol. 792 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)