Correction. In the article "Molecular determinants of immunogenicity: The immunon model of immune response" by H.

No abstract

Team-based virtual microscopy and on-line learning were used to transform the first-year Physiology/Histology course at The Johns Hopkins School of Medicine into a student-centered learning environment. Prior to each laboratory session, students were required to view prelaboratory virtual lectures and examine digital slides that had been enhanced with annotations and 2-min microlectures. The laboratory classroom was then used for team-based learning exercises including student presentations and small-group discussions designed to integrate histology and physiology. The results of quantitative assessments indicated an 8- to 14-point increase over the identical final exams given over the past 5 yr. Means (+/-SD) of percent correct answers on the final exam were found to be 75.2% (11.1%), 72.5% (12.6%), 70.5% (12.6%), 73.6% (11.3%), 73.1% (12.2%), and 84.1% (9.1%) for years 2001-2006, respectively. The mean test scores for all other years were statistically lower compared with 2006, as determined by the Bonferroni post hoc multiple-comparison test (P < 0.001 for all years).

The immunogenicity of a folded, all D-amino acid protein, rubredoxin, has been compared with that for the corresponding L-protein enantiomer. Following multiple administrations with alum adjuvant, the L-protein induced a strong, specific IgG antibody response, whereas the D-protein did not. This relative lack of responsiveness to the D-protein cannot be attributed to rapid excretion, since it is retained at least 4 times longer than the natural L-protein. These observations provide the first direct evidence that a folded D-amino acid protein has low immunogenicity and is long lived in vivo. Proteins with such properties may be useful as molecular platforms in a variety of chemical and pharmacological applications.