Bredo, Eric, and Walter Feinberg, eds., Knowledge and Values in Social and Educational Research . Philadelphia: Temple University Press, 1982.

Presents overviews by the editors of positivistic, interpretive, and critical approaches to research; includes for each approach 6 or 7 chapters by other writers on related topics

Bredo, Eric, and Walter Feinberg, Introduction: Competing Modes of Social and Educational Research, pp. 3-11, The Positivistic Approach to Social and Educational Research, pp. 13-27, The Interpretive Approach to Social and Educational Research, pp. 115-128, The Critical Approach to Social and Educational Research, pp. 271-291, in Eric Bredo and Walter Feinberg, eds., Knowledge and Values in Social and Educational Research . Philadelphia: Temple University Press, 1982.*

Explains three research approaches: positivist, interpretive, and critical

Howe, Kenneth R., Eric Bredo, R. Burke Johnson, and Linda C. Tillman, Epistemology, Methodology, and Education Sciences, Educational Researcher, 38(August/September, 2009), 428-466.

Treats alternatives to positivist views on educational research; a series of scholars comment on these ideas and Howe responds

The GAGOme:a cell-based library of displayed glycosaminoglycans

Glycosaminoglycans (GAGs) are essential polysaccharides in normal physiology and disease. However, understanding of the contribution of specific GAG structures to specific biological functions is limited, largely because of the great structural heterogeneity among GAGs themselves, as well as technical limitations in the structural characterization and chemical synthesis of GAGs. Here we describe a cell-based method to produce and display distinct GAGs with a broad repertoire of modifications, a library we refer to as the GAGOme. By using precise gene editing, we engineered a large panel of Chinese hamster ovary cells with knockout or knock-in of the genes encoding most of the enzymes involved in GAG biosynthesis, to generate a library of isogenic cell lines that differentially display distinct GAG features. We show that this library can be used for cell-based binding assays, recombinant expression of proteoglycans with distinct GAG structures, and production of distinct GAG chains on metabolic primers that may be used for the assembly of GAG glycan microarrays