Recent Publications

2005

Huan, J.; Meza-Romero, R.; Mooney, J.; Chou, Y.K.; Edwards, D.M.; Rich, C.; Link, J.M.; Vandenbark, A.A.; Bourdette, D.N.; Bächinger, H.P.; and Burrows, G.G. Rationally Designed Mutations Convert Complexes of Human Recombinant T Cell Receptor Ligands Into Monomers that Retain Biological Activity. Journal of Chemical Technology and Biotechnology. Vol 80 (1):pgs 2-12, 2005.

Burrows, G.G.; Chang, J.W.; Huan, J.; Meza-Romero, R.; Mooney, J.; and Bächinger, H.P. Design, Engineering and Characterization of Human Recombinant T Cell Receptor Ligands Derived from Human Leukocyte Antigens DP2 and DP4. Journal of Chemical Technology and Biotechnology. Vol 247, April 2005.

Gregory, K.E., Ono, R.N., Charbonneau, N.L., Kuo, C.-L., Keene, D.R., Bächinger, H.P., and Sakai, L.Y. The prodomain of BMP-7 targets the BMP-7 complex to the extracellular matrix.
J Biol Chem. 2005 Jul 29;280(30):27970-80.

Holden, P., Keene, DR., Lunstrum, GP., Bächinger, HP., Horton, WA. Secretion of cartilage oligomeric matrix protein is affected by the signal peptide. J. Biol. Chem. 280: 17172-17179, 2005.

Bachmann A, Kiefhaber T, Boudko S, Engel J, Bächinger, HP. Collagen triple-helix formation in all-trans chains proceeds by a nucleation/growth mechanism with a purely entropic barrier. Proc Natl Acad Sci USA. 2005 Sep 27;102(39):13897-902.

Schumacher, M., Mizuno, K., and Bächinger, HP. The crystal structure of the collagen-like polypeptide (Glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)9 at 1.55 A resolution shows up-puckering of the praline ring in the Xaa position. J Biol Chem, 280:20397-20403, 2005.

Walker, W., Z., Zhou, Z.Q., Ota, S., Wynshow-Boris, A., and Hurlin, P.J. J. Cell Biol. 169(3):405-13, 2005.

2006

Whittaker MM, Mizuno K, Bächinger HP, Whittaker JW. Kinetic analysis of the metal binding mechanism of Escherichia coli manganese superoxide dismutase. Biophys J. 2006 Jan 15;90(2):598-607.

Ishida Y, Kubota H, Yamamoto A, Kitamura A, Bächinger HP, Nagata K. Type I Collagen in Hsp47-null Cells Is Aggregated in ER and Deficient in N-Propeptide Processing and Fibrillogenesis. Mol Biol Cell. 2006 Mar 8.

Jiravanichanun, N., Mizuno, K., Bächinger, H.P. and Okuyama, K. Threonine in collagen triple-helical structure. Polymer Journal 38:400-4003, 2006.

Schumacher, M.A., Mizuno, K. and Bächinger, H.P. The crystal structure of a collagen-like polypeptide with 3(S)-hydroxyproline residues in the Xaa position forms a standard 7/2 collagen triple helix. J. Biol. Chem. 281:27566-74, 2006.

Morello, R., Bertin, T., Chen, Y., Hicks, J., Tonachini, L., Monticone, M., Castagnola, P., Rauch, F., Glorieux, F.H., Vranka, J., Bächinger, H.P., Pace, J.M., Schwarze, U., Byers, P., Weis, M.A., Fernandes, R.J., Eyre, D.R., Yao. Z., Boyce, B.F. and Lee, B. CRTAP is required for prolyl 3-hydroxylation and loss of its function causes recessive osteogenesis imperfecta. Cell 127:291-304, 2006.

2007

Kuo CL, Isogai Z, Keene DR, Hazaki N, Ono RN, Sengle G, Bächinger, HP, Sakai LY, Effects of fibrillin-1 degradation on microfibril ultrastructure. J. Biol. Chem. 282:4007-4020, 2007.

Knosp, WM., Saneyoshi, C., Shou, S., Bächinger, H.P., Stadler, H.S., Elucidation, Quantitative Refinement, and In Vivo Utilization of the Hoxa13 DNA Binding Site., J Biol Chem. 2007 Mar 2;282(9):6843-53. Epub 2007 Jan 1.
PMID: 17200107 [PubMed - in process]

Guo C, Degnin CR, Laederich MB, Lunstrum GP, Holden P, Bihlmaier J, Krakow D, Cho JY, Horton WA: Sprouty 2 disturbs FGFR3 degradation in the achondroplasia group of human skeletal dysplasias. (Submitted to JBC) 2007.

Meier, S., Jensen, P.R., Adamczyk, P., Bächinger, H.P., Holstein, T.W., Engel, J., Ozbek, S. and Grzesiek, S. Sequence-structure and structure-function analysis in cystein-rich domains forming the ultrastable nematocyst wall. J. Mol. Biol. in press, 2007.

Kobayashi, N., Kostka, G. Garbe, J.H., Keene, D.R., Bächinger, H.P., Hanisch, F.G., Markova, D., Tsuda, T., Timpl, R. Chu, M.L. and Sasaki, T. A comparative analysis of the fibulin protein family: Biochemical characterization, binding interactions and tissue localization. J. Biol. Chem. in press, 2007.

Bachmann, A., Bächinger, H.P. and Engel, J. The model peptide [(GER)15GPCCG]3 folds into a collagen triple helix several orders of magnitude faster than collagens. J. Mol. Biol. submitted, 2007.

Vranka, J.A., H. Scott Stadler and Bächinger, H.P. Patterns of expression of prolyl 3-hydroxylases in mouse tissues. Submitted, 2007.

Shriners Research Center, Portland OR

Recent Publications