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1.  Feasibility and marketing studies of health sciences librarianship education programs. 
The University of North Carolina at Chapel Hill evaluated five curricular models designed to improve education for health sciences librarianship. Three of the models enhanced existing degree and certificate programs, and two were new programs for working information professionals. Models were developed with input from experts and a Delphi study; the marketability of the models was tested through surveys of potential students and employers; and recommendations were made as a guide to implementation. The results demonstrated a demand for more specialized curricula and for retraining opportunities. Marketing data showed a strong interest from potential students in a specialized master's degree, and mid-career professionals indicated an interest in postmaster's programs that provided the ability to maintain employment. The study pointed to the opportunity for a center of excellence in health sciences information education to enable health sciences librarians to respond to their evolving roles.
PMCID: PMC226522  PMID: 9934529
2.  Preparing tomorrow's health sciences librarians: feasibility and marketing studies. 
The University of North Carolina at Chapel Hill is devising and evaluating five curricular models designed to improve education for health sciences librarianship. These models fit into a continual learning process from the initial professional preparation to lifelong learning opportunities. Three of them enhance existing degree and certificate programs in the School of Information and Library Science (SILS) with a health sciences specialization, and two are new programs for working information professionals. The approaches involve partnerships among SILS, the Health Sciences Library, and the program in Medical Informatics. The planning process will study the feasibility of the proposed programs, test the marketability of the models to potential students and employers, and make recommendations about implementation.
PMCID: PMC226194  PMID: 8913557
3.  A longitudinal study of Sin Nombre virus prevalence in rodents, southeastern Arizona. 
Emerging Infectious Diseases  1999;5(1):113-117.
We determined the prevalence of Sin Nombre virus antibodies in small mammals in southeastern Arizona. Of 1,234 rodents (from 13 species) captured each month from May through December 1995, only mice in the genus Peromyscus were seropositive. Antibody prevalence was 14.3% in 21 white-footed mice (P. leucopus), 13.3% in 98 brush mice (P. boylii), 0.8% in 118 cactus mice (P. eremicus), and 0% in 2 deer mice (P. maniculatus). Most antibody-positive mice were adult male Peromyscus captured close to one another early in the study. Population dynamics of brush mice suggest a correlation between population size and hantavirus-antibody prevalence.
PMCID: PMC2627683  PMID: 10081678
4.  Mutations in the zinc fingers of ADR1 that change the specificity of DNA binding and transactivation. 
Molecular and Cellular Biology  1992;12(6):2784-2792.
ADR1 is a yeast transcription factor that contains two zinc fingers of the Cys-2-His-2 (C2H2) class. Mutations that change the specificity of DNA binding of ADR1 to its target site, upstream activation sequence 1 (UAS1), have been identified at three positions in the first zinc finger. Mutations Arg-115 to Gln, His-118 to Thr, and Arg-121 to Asn led to new specificities of DNA binding at adjacent positions 10, 9, and 8 (3'-GAG-5') in UAS1. Arg-115 is at the finger tip, and His-118 and Arg-121 are at positions 3 and 6, respectively, in the alpha helix of finger 1. One double mutant displayed the binding specificity expected from the properties of its constituent new-specificity mutations. Mutations in the second finger that allowed its binding site to be identified through loss-of-contact phenotypes were made. These mutations imply a tail-to-tail orientation of the two ADR1 monomers on their adjacent binding sites. Finger 1 is aligned on UAS1 in an amino-to-carboxyl-terminal orientation along the guanine-rich strand in a 3'-to-5' direction. One of the ADR1 mutants was functional in vivo with both its cognate binding site and wild-type UAS1, but the other two mutants were defective in transactivation despite their ability to bind with high affinity to their cognate binding sites.
PMCID: PMC364473  PMID: 1588970

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