Current Role at Stanford


I consult with all members of the Stanford scientific research community on issues surrounding data management, including understanding and creating data management plans, organizing and backing up your research data, acquiring and analyzing data, assigning metadata to enable future discovery, and preserving your data for long-term access in the Stanford Digital Repository. Visit the Data Management Services web site to find out more.

Education & Certifications


  • PhD, Yale University, Molecular Biophysics and Biochemistry
  • MPhil, Yale University, Molecular Biophysics and Biochemistry
  • BS, Centre College of Kentucky, Biochemistry and Molecular Biology
  • Certified Instructor, Software Carpentry (2015)

All Publications


  • The PharmGKB: integration, aggregation, and annotation of pharmacogenomic data and knowledge CLINICAL PHARMACOLOGY & THERAPEUTICS Hodge, A. E., Altman, R. B., Klein, T. E. 2007; 81 (1): 21-24

    Abstract

    The Pharmacogenetics and Pharmacogenomics Knowledge Base, PharmGKB (http://www.pharmgkb.org), curates pharmacogenetic and pharmacogenomic information to generate knowledge concerning the relationships among genes, drugs, and diseases, and the effects of gene variation on these relationships. PharmGKB curators collect information on genotype-phenotype relationships both from the literature and from the deposition of primary research data into our database. Their goal is to catalyze pharmacogenetic and pharmacogenomic research.

    View details for DOI 10.1038/sj.clpt.6100048

    View details for Web of Science ID 000242874200010

    View details for PubMedID 17185992

  • The cyclin-dependent kinase inhibitory domain of the yeast Sic1 protein is contained within the C-terminal 70 amino acids MOLECULAR AND GENERAL GENETICS Hodge, A., Mendenhall, M. 1999; 262 (1): 55-64

    Abstract

    By inhibiting the activity of Cdc28/Clb cyclin-dependent protein kinase (CDK) complexes, Sic1 prevents the premature initiation of S phase in the yeast Saccharomyces cerevisiae. By testing a series of Sic1 truncation mutants, we have mapped the minimal domain necessary for Cdc28/Clb inhibition in vivo to the C-terminal 70 amino acids of Sic1. Site-directed mutagenesis was used to show that a sequence that matches the zRxL motif found in mammalian CDK inhibitors is essential for Sicl function. This motif is not found in the Schizosaccharomyces CDK inhibitor p25rum1, which appears to be a structural and functional homolog of Sicl. Based on the mutational data and sequence comparisons, we argue that Sic1 and p25rum1 are structurally distinct from the known mammalian CDK inhibitors, but may bind CDK complexes in a manner more closely resembling CDK substrates like the retinoblastoma and E2F proteins.

    View details for Web of Science ID 000082577300007

    View details for PubMedID 10503536

  • Regulation of cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS Mendenhall, M. D., Hodge, A. E. 1998; 62 (4): 1191-?

    Abstract

    The cyclin-dependent protein kinase (CDK) encoded by CDC28 is the master regulator of cell division in the budding yeast Saccharomyces cerevisiae. By mechanisms that, for the most part, remain to be delineated, Cdc28 activity controls the timing of mitotic commitment, bud initiation, DNA replication, spindle formation, and chromosome separation. Environmental stimuli and progress through the cell cycle are monitored through checkpoint mechanisms that influence Cdc28 activity at key cell cycle stages. A vast body of information concerning how Cdc28 activity is timed and coordinated with various mitotic events has accrued. This article reviews that literature. Following an introduction to the properties of CDKs common to many eukaryotic species, the key influences on Cdc28 activity-cyclin-CKI binding and phosphorylation-dephosphorylation events-are examined. The processes controlling the abundance and activity of key Cdc28 regulators, especially transcriptional and proteolytic mechanisms, are then discussed in detail. Finally, the mechanisms by which environmental stimuli influence Cdc28 activity are summarized.

    View details for Web of Science ID 000077376400007

    View details for PubMedID 9841670