Joshua J. Higgin, Ph.D. - Publications
Affiliations: | 2004 | University of Wisconsin, Madison, Madison, WI |
Area:
Chemical biology, protein design and engineering, enzymology, biofuelsYear | Citation | Score | |||
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2013 | Vasta JD, Higgin JJ, Kersteen EA, Raines RT. Bioavailable affinity label for collagen prolyl 4-hydroxylase. Bioorganic & Medicinal Chemistry. 21: 3597-601. PMID 23702396 DOI: 10.1016/J.Bmc.2013.04.057 | 0.486 | |||
2011 | Smith BD, Higgin JJ, Raines RT. Site-specific folate conjugation to a cytotoxic protein. Bioorganic & Medicinal Chemistry Letters. 21: 5029-32. PMID 21570289 DOI: 10.1016/J.Bmcl.2011.04.081 | 0.605 | |||
2004 | Kersteen EA, Higgin JJ, Raines RT. Production of human prolyl 4-hydroxylase in Escherichia coli. Protein Expression and Purification. 38: 279-91. PMID 15555944 DOI: 10.1016/J.Pep.2004.09.008 | 0.584 | |||
2004 | Makarov AA, Yakovlev GI, Mitkevich VA, Higgin JJ, Raines RT. Zinc(II)-mediated inhibition of ribonuclease Sa by an N-hydroxyurea nucleotide and its basis. Biochemical and Biophysical Research Communications. 319: 152-6. PMID 15158454 DOI: 10.1016/J.Bbrc.2004.04.182 | 0.527 | |||
2003 | Wright G, Higgin JJ, Raines RT, Steenbergen C, Murphy E. Activation of the prolyl hydroxylase oxygen-sensor results in induction of GLUT1, heme oxygenase-1, and nitric-oxide synthase proteins and confers protection from metabolic inhibition to cardiomyocytes. The Journal of Biological Chemistry. 278: 20235-9. PMID 12649278 DOI: 10.1074/Jbc.M301391200 | 0.507 | |||
2003 | Higgin JJ, Yakovlev GI, Mitkevich VA, Makarov AA, Raines RT. Zinc(II)-mediated inhibition of a ribonuclease by an N-hydroxyurea nucleotide. Bioorganic & Medicinal Chemistry Letters. 13: 409-12. PMID 12565940 DOI: 10.1016/S0960-894X(02)00929-0 | 0.466 | |||
2000 | Friedman L, Higgin JJ, Moulder G, Barstead R, Raines RT, Kimble J. Prolyl 4-hydroxylase is required for viability and morphogenesis in Caenorhabditis elegans. Proceedings of the National Academy of Sciences of the United States of America. 97: 4736-41. PMID 10781079 DOI: 10.1073/Pnas.97.9.4736 | 0.524 | |||
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