Featured Publications
The hemerythrin-like domain within F-box and leucine-rich repeat protein 5 communicates cellular iron and oxygen availability by distinct mechanisms.
Chollangi S, Thompson JW, Ruiz JC, Gardner KH, Bruick RK The Journal of biological chemistry 2012 May
Structural and molecular characterization of iron-sensing hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5).
Thompson JW, Salahudeen AA, Chollangi S, Ruiz JC, Brautigam CA, Makris TM, Lipscomb JD, Tomchick DR, Bruick RK J. Biol. Chem. 2012 Mar 287 10 7357-65
An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis.
Salahudeen AA, Thompson JW, Ruiz JC, Ma HW, Kinch LN, Li Q, Grishin NV, Bruick RK Science 2009 Oct 326 5953 722-6
Artificial Ligand Binding within the HIF2α PAS-B Domain of the HIF2 Transcription Factor
Scheuermann, T.H., Tomchick, D.R., Machius, M., Guo, Y., Bruick, R.K., and Gardner, K.H. Proc. Natl. Acad. Sci. USA. 2009 106 450-455
Functions of the Per/ARNT/Sim (PAS) Domains of the Hypoxia Inducible Factor (HIF)
Yang, J., Zhang, L., Erbel, P.J.A., Gardner, K.H., Ding, K., Garcia, J.A., and Bruick, R.K. J. Biol. Chem. 2005 280 36047-36054
FIH-1 is an asparaginyl hydroxylase that regulates HIF transcriptional activity
Peet, D.J., Lando, D., Whelan, D.A., Gorman, J.J., Whitelaw, M.L. and Bruick, R.K. Genes & Dev. 2002 16 1466-1471
A conserved family of prolyl-4-hydroxylases that modify HIF
Bruick, R.K. and McKnight, S.L. Science 2001 294 1337-1340
Protein degradation and iron homeostasis.
Thompson JW, Bruick RK Biochimica et biophysica acta 2012 Feb
Activation of the HIF prolyl hydroxylase by the iron chaperones PCBP1 and PCBP2.
Nandal A, Ruiz JC, Subramanian P, Ghimire-Rijal S, Sinnamon RA, Stemmler TL, Bruick RK, Philpott CC Cell Metab. 2011 Nov 14 5 647-57
Conditional HIF-1alpha expression produces a reversible cardiomyopathy.
Bekeredjian R, Walton CB, MacCannell KA, Ecker J, Kruse F, Outten JT, Sutcliffe D, Gerard RD, Bruick RK, Shohet RV PLoS ONE 2010 5 7 e11693
