Elaine D Collins

Summary

Affiliation: San Jose State University
Country: USA

Publications

  1. doi request reprint Cloning the human vitamin D receptor into the pTwin-1 expression vector
    Elaine D Collins
    Department of Chemistry, San Jose State University, One Washington Square, San Jose, CA 95192 0101, USA
    J Steroid Biochem Mol Biol 121:121-3. 2010
  2. ncbi request reprint Residues of the human nuclear vitamin D receptor that form hydrogen bonding interactions with the three hydroxyl groups of 1alpha,25-dihydroxyvitamin D3
    Madhuri D Reddy
    Department of Chemistry, San Jose State University, San Jose, CA 95192 0101, USA
    J Steroid Biochem Mol Biol 103:347-51. 2007
  3. ncbi request reprint Role of residues 143 and 278 of the human nuclear Vitamin D receptor in the full-length and Delta165-215 deletion mutant
    Alejandra Acevedo
    Department of Chemistry, San Jose State University, San Jose, CA 95192 0101, USA
    J Steroid Biochem Mol Biol 89:83-7. 2004
  4. ncbi request reprint Generation of large deletion mutants from plasmid DNA
    Ludmila Stoynova
    San Jose State University, San Jose, CA, USA
    Biotechniques 36:402-4, 406. 2004
  5. ncbi request reprint Effect of 25-hydroxyl group orientation on biological activity and binding to the 1alpha,25-dihydroxy vitamin D3 receptor
    Elaine D Collins
    Department of Chemistry, San Jose State University, San Jose, CA 95192, USA
    J Steroid Biochem Mol Biol 94:279-88. 2005
  6. ncbi request reprint Flexibility of BIV TAR-Tat: models of peptide binding
    Mark Hsieh
    Department of Chemistry, San Jose State University, CA 95192 0101, USA
    J Biomol Struct Dyn 20:243-51. 2002

Collaborators

Detail Information

Publications6

  1. doi request reprint Cloning the human vitamin D receptor into the pTwin-1 expression vector
    Elaine D Collins
    Department of Chemistry, San Jose State University, One Washington Square, San Jose, CA 95192 0101, USA
    J Steroid Biochem Mol Biol 121:121-3. 2010
    ..Western blot analysis of the VDR-fusion protein indicates that a protein of approximately 75 kDA was obtained as expected...
  2. ncbi request reprint Residues of the human nuclear vitamin D receptor that form hydrogen bonding interactions with the three hydroxyl groups of 1alpha,25-dihydroxyvitamin D3
    Madhuri D Reddy
    Department of Chemistry, San Jose State University, San Jose, CA 95192 0101, USA
    J Steroid Biochem Mol Biol 103:347-51. 2007
    ..Defining the role of hormone D-VDR binding will lead to a better understanding of the vitamin D signal transduction pathway...
  3. ncbi request reprint Role of residues 143 and 278 of the human nuclear Vitamin D receptor in the full-length and Delta165-215 deletion mutant
    Alejandra Acevedo
    Department of Chemistry, San Jose State University, San Jose, CA 95192 0101, USA
    J Steroid Biochem Mol Biol 89:83-7. 2004
    ..This suggests that there are some minor structural and functional differences between the wild-type VDR and the Delta165-215 deletion mutant and that Y143 residue is more important for receptor function than residue S278...
  4. ncbi request reprint Generation of large deletion mutants from plasmid DNA
    Ludmila Stoynova
    San Jose State University, San Jose, CA, USA
    Biotechniques 36:402-4, 406. 2004
  5. ncbi request reprint Effect of 25-hydroxyl group orientation on biological activity and binding to the 1alpha,25-dihydroxy vitamin D3 receptor
    Elaine D Collins
    Department of Chemistry, San Jose State University, San Jose, CA 95192, USA
    J Steroid Biochem Mol Biol 94:279-88. 2005
    ..The 25-hydroxyl orientation combined with the 16,17-ene functionality of analog LA enhances its ability to interact with VDR and induce biological actions...
  6. ncbi request reprint Flexibility of BIV TAR-Tat: models of peptide binding
    Mark Hsieh
    Department of Chemistry, San Jose State University, CA 95192 0101, USA
    J Biomol Struct Dyn 20:243-51. 2002
    ..This approach for identifying potential sites amenable to substitution of more flexible residues to enhance peptide binding to RNA targets could be a useful design tool...