oratorySelected Recent Publications
Original articles
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. 282:11805-11816, 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. 368:718-728, 2007.
Kuo, C.L., Isogai, Z., Keene, D.R., Hazeki, N., Ono, R.N., Sengle, G., Bächinger, H.P. and Sakai, L.Y. Effects of fibrillin-1 degradation on microfibril ultrastructure. J. Biol. Chem. 282:4007-4020, 2007.
Knosp, W.M., Saneyoshi, C., Shou, S., Bächinger, H.P. and Stadler, H.S. Elucidation, quantitative refinement and in vivo utilization of the hoxa13 DNA biding site. J. Biol. Chem. 282:6843-6853, 2007.
Jiravanichanun, N., Mizuno, K., Bächinger, H.P. and Okuyama, K. Threonine in collagen triple-helical structure. Polymer Journal 38:400-4003, 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.
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. 281:27566-27574, 2006.
Ishida, Y., Kubota, H., Yamamoto, A., Kitamura, A., Bächinger, H.P. and Nagata, K. Type I collagen in HSP47-null cells is aggregated in ER and deficient in N-propeptide processing and fibrillogenesis. Mol. Biol. Cell 17:2346-2355,. 2006
Whittaker, M.M., Mizuno, K., Bächinger, H.P. and Whittaker, J.W. Kinetic analysis of the metal binding mechanism of E. coli. Manganese superoxide dismutase. Biophys. J. 90:598-607, 2006.
Bachmann A., Kiefhaber, T., Boudko, S., Engel, J. and Bächinger, H.P. Collagen triple helix formation in all-trans chains proceeds by a nucleation/growth mechanism with a purely entropic barrier. Proc. Natl. Acad. Sci. USA 102:13897-13902, 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. 280:27970-27980, 2005.
Schumacher, M., Mizuno, K., and Bächinger, H.P. The crystal structure of the collagen-like polypeptide (Glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)9 at 1.55 Å resolution shows up-puckering of the proline ring in the Xaa position. J. Biol. Chem. 280:20397-20403, 2005.
Huan, J.Y., Meza-Romero, R., Mooney, J.L., 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. J. Chem. Tech. and Biotech. 80:2-12, 2005
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. 2005 Mar 3. PMID: 15749701