oratoryCURRICULUM VITAE
Hans Peter Bächinger
Senior Investigator, Research Center
Shriners Hospital for Children,
Portland Hospital
Professor of Biochemistry and Molecular Biology
Oregon Health & Science University.
INSTITUTION AND LOCATION DEGREE STUDY
University of Basel, Switzerland, Diploma 1975 Chemistry
Biocenter, University of Basel, Switzerland, Ph.D. 1979
Biophysics; Molecular Biology Institute, UCLA Postdoctoral 1981
HONORS
Fellowship from the Swiss National Science Foundation, January-December, 1980
First Place, Young Investigators Forum, American Heart Association, Greater Los Angeles Affiliate, May, 1981.
RESEARCH AND/OR PROFESSIONAL EXPERIENCE
1998-Present Portland Research Unit, Shriners Hospitals for Children, Senior Investigator; Department of Biochemistry and Molecular Biology, Oregon Health & Science University, Professor
1989-1998 Portland Research Unit, Shriners Hospitals for Children, Investigator; Department of Biochemistry and Molecular Biology, Oregon Health & Science University, Associate Professor
1984-1989 Portland Research Unit, Shriners Hospitals for Children, Investigator; Department of Biochemistry, Oregon Health & Science University, Assistant Professor
1982-1984 Medical University of South Carolina, Assistant Professor of Medicine and Biochemistry
1981-1982 Assistant Research Molecular Biologist, UCLA
1980-1981 Postdoctoral Fellow, Molecular Biology Institute, UCLA
1979-1980 Postdoctoral Fellow, Biozentrum der Universität Basel, Department of Biophysical Chemistry
PROFESSIONAL ORGANIZATIONS
Schweizerische Gesellschaft für Biochemie, USGEB, Sektion Biophysik
American Society for Biochemistry and Molecular Biology
American Chemical Society; Protein Society
PUBLICATIONS - Original Articles
1. Bruckner, P., Bächinger, H.P., Timpl, R., and Engel, J.: Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix coil transition. Eur. J. Biochem., 90:595-603, 1978.
2. Bächinger, H.P., Bruckner, P., Timpl, R., and Engel, J.: The role of cis-trans isomerization of peptide bonds in the coil triple helix conversion of collagen. Eur. J. Biochem., 90:605-613, 1978.
3. Bentz, H., Bächinger, H.P., Glanville, R.W., and Kühn, K.: Physical evidence for the assembly of chains of human placental collagen in a single triple helix. Eur. J. Biochem., 92:563-567, 1978.
4. Bächinger, H.P., Eggenberger, H.P., and Hänisch, G.: Conversion of a Cary 60 spectropolarimeter into a fast circular dichroism instrument for use with standard rapid reaction techniques. Rev. Sci. Instrum., 50:1367-1372, 1979.
5. Timpl, R., Ristell, J., and Bächinger, H.P.: Identification of a new basement membrane collagen by the aid of a large fragment resistant to bacterial collagenase. FEBS Lett., 101:265-268, 1979.
6. Timpl, R., Rhode, H., Ott-Ullbricht, U., Risteli, J., and Bächinger, H.P.: Chemical characterization of laminin, a major glycoprotein of basement membranes. Proc. Vth Intern. Symp. Glycoconjugates, G. Thieme Stuttgart, pp. 145-146, 1979.
7. Engel, J., Bächinger, H.P., Bruckner, P., and Timpl, R.: The role of disulfide bridges and cis-trans isomerization of peptide bonds in collagen folding. In Protein Folding, (R. Jaenicke, Ed.), Elsevier/North Holland Biomedical Press, pp. 345-368, 1980.
8. Bächinger, H.P., Bruckner, P., Timpl, R., Prockop, D.J., and Engel, J.: Folding mechanism of the triple helix in type III collagen and type III pN-collagen. Role of disulfide bridges and peptide bond isomerization. Eur. J. Biochem., 106:619-632, 1980.
9. Risteli, J., Bächinger, H.P., Engel, J., Furthmayr, H., and Timpl, R.: 7S collagen: Characterization of an unusual basement membrane structure. Eur. J. Biochem., 108: 239-250, 1980.
10. Rhode, H., Bächinger, H.P., and Timpl, R.: Characterization of pepsin fragments of laminin in a tumor basement membrane. Evidence for the existence of related proteins. Hoppe Seyler's Z. Phys. Chem., 361:1651-1660, 1980.
11. Bächinger, H.P., Fessler, L.I., Timpl, R., and Fessler, J.H.: Chain assembly intermediate in the biosynthesis of type III procollagen in chick embryo blood vessel. J. Biol. Chem., 256:13193-13199, 1981.
12. Fessler, J.H., Bächinger, H.P., Doege, K.J., and Fessler, L.I.: Biosynthesis and processing of procollagens. In Chemistry and Biology of Mineralized Connective Tissue, (A. Veis, Ed.), Elsevier North Holland, Inc., NY, pp. 137-141, 1981.
13. Fessler, J.H., Bächinger, H.P., Lunstrum, G., and Fessler, L.I.: Biosynthesis and processing of some procollagens. In New Trends in Basement Membrane Research (K. Kuhn and R. Timpl, Eds.), Raven, NY, pp. 145-153, 1982.
14. Imber, R., Bächinger, H.P., and Bickle, T.A.: Purification and characterization of a small DNA binding protein Hb from Bacillus Globigii. Eur. J. Biochem., 122:627-632, 1982.
15. Bächinger, H.P., Fessler, L.I., and Fessler, J.H.: Mouse procollagen IV: Characterization and supramolecular association. J. Biol. Chem., 257:9796-9803, 1982.
16. Bächinger, H.P., Doege, K.J., Petschek, J.P., Fessler, L.I., and Fessler, J.H.: Structural implications from an EM comparison of procollagen V with procollagen I, pC (I), procollagen IV and a Drosophila procollagen. J. Biol. Chem., 257:14590-14592, 1982.
17. Duncan, K.G., Fessler, L.I., Bächinger, H.P., and Fessler, J.H.: Procollagen IV: Association to tetramers. J. Biol. Chem., 258:5869-5877, 1983.
18. Fessler, J.H., Lunstrum, G., Duncan, K.A., Campbell, A.G., Stone, R., Bächinger, H.P., and Fessler, L.I.: Evolutionary constancy of basement membrane components. In The Role of Extracellular Matrix in Development, Alan R. Liss, Inc., New York, pp. 207-219, 1984.
19. Bächinger, H.P., and LeRoy, E.C.: Connective tissue in scleroderma (systemic sclerosis). A vascular emphasis. Rheumatology, 10:430-450, 1986.
20. Keene, D.R., Sakai, L.Y., Burgeson, R.E., and Bächinger, H.P.: Direct visualization of IgM antibodies to tissue antigens utilizing a monoclonal anti type III collagen IgM as a model system. J. Histochem. Cytochem., 35:311-318, 1987.
21. Keene, D.R., Sakai, L.Y., Bächinger, H.P., and Burgeson, R.E.: Type III collagen is present on banded collagen fibrils regardless of fibril diameter. J. Cell Biol., 105:2393-2402, 1987.
22. Morris, N.P., and Bächinger, H.P.: Type XI collagen is a heterotrimer with a composition retaining non-triple helical domains. J. Biol. Chem., 262:11345-11350, 1987.
23. Bächinger, H.P.: The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen. J. Biol. Chem., 262:17144-17148, 1987.
24. Lunstrum, G.P., Bächinger, H.P., Fessler, L.I., Duncan, K.G., Nelson, R.E., and Fessler, J.H.: Drosophila basement membrane procollagen IV: Protein characterization and distribution. J. Biol. Chem., 263:18318-18327, 1988.
25. Bruderer, U., Stenzel-Poore, M.P., Bächinger, H.P., Fellman, J.H., and Rittenberg, M.B.: Antibody combining site heterogeneity within the response to phosphocholine-keyhole limpit hemocyanin. Molecular Immunology, 26:63-71, 1989.
26. Davis, J.M., Boswell, B.A., and Bächinger, H.P.: Thermal stability and folding of type IV procollagen and effect of peptidyl-prolyl cis-trans isomerase on the folding of the triple helix. J. Biol. Chem., 264:8956-8962, 1989.
27. Bächinger, H.P., Morris, N.P., and Davis, J.M.: Thermal stability and folding of interstitial and basement membrane collagens. In Springer Series in Biophysics (Bayley, P.M., Ed.), pp. 171-181, 1989.
28. Bächinger, H.P., Morris, N.P., Lunstrum, G.P., Keene, D.R., Rosenbaum, L.M., Compton, L.A., and Burgeson, R.E.: The relationship of the biophysical and biochemical characteristics of type VII collagen to the functioning of anchoring fibrils. J. Biol. Chem., 265:10095-10101, 1990.
29. Morris, N.P., Watt, S.L., Davis, J.M., and Bächinger, H.P.: Unfolding intermediates in the triple helix to coil transition of bovine type XI collagen and human type V collagens. J. Biol. Chem., 265:10081-10087, 1990.
30. Bächinger, H.P., and Morris, N.P.: Analysis of the thermal stability of type II collagen in various solvents. Matrix, 10:331-338, 1990.
31. Bächinger, H.P., and Davis, J.M.: Sequence specific thermal stability of the collagen triple helix. Int. J. Biol. Macromol., 13:152-156, 1991.
32. Sakai, L.Y., Keene, D.R., Glanville, R.W., and Bächinger, H.P.: Purification and partial characterization of fibrillin, a cysteine-rich structural component of connective tissue microfibrils. J. Biol. Chem., 266:14763-14770, 1991.
33. Brown, M., Stenzel-Poore, M., Stevens, S., Kondoleon, S.K., Ng, J., Bächinger, H.P., and Rittenberg, M.B.: Immunologic memory to phosphocholine keyhole limpit hemocyanin. J. Immunol., 148:339-346, 1992.
34. Compton, L.A., Davis, J.M., Macdonald, J.R., and Bächinger, H.P.: Structural and functional characterization of E. coli peptidyl-prolyl cis-trans isomerases. Eur. J. Biochem., 206:927-934, 1992.
35. Hori, H., Keene, D.R., Sakai, L.Y., Wirtz, M.K., Bächinger, H.P., Godfrey, M., and Hollister, D.W.: Repeated helical epitopes of defined amino acid sequence in human type III collagen identified by monoclonal antibodies. Mol. Immunol., 29:759-770, 1992.
36. Bächinger, H.P., Morris, N.P., and Davis, J.M.: The thermal stability and folding of the collagen triple helix and the effects of mutations in Osteogenesis Imperfecta on the triple helix of type I collagen. Am. J. Med. Gen., 45:152-162, 1993.
37. Davis, J.M. and Bächinger, H.P.: Hysteresis in the triple helix-coil transition of type III collagen. J. Biol. Chem., 268:25965-25972, 1993.
38. Kwok, R.P.S., Lundblad, J.R., Chrivia, J.C., Richards, J.P., Bächinger, H.P., Brennan, R.G., Roberts, S.G.E., Green, M.R., and Goodman, R.H.: Nuclear protein CBP is a coactivator for the transcription factor CREB. Nature, 370:223-226, 1994.
39. Klatt, P., Schmidt, K., Lehner, D., Glatter, O., Bächinger, H.P., Mayer, B.: Structural analysis of porcine brain nitric oxide synthase reveals a role of tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer. EMBO Journal, 14:3687-3695, 1995.
40. Reinhardt, D., Keene, D.R., Corson, G.M., Pöschl, E., Bächinger, H.P., Gambee, J.E., Sakai, L.Y.: Fibrillin 1: Organization in microfibrils and structural properties. J. Mol. Biol., 258:104-116, 1996.
41. Beck, K., Gambee, J.E., Bohan, C., Bächinger, H.P.: The C-terminal domain of cartilage matrix protein assembles into a triple stranded a-helical coiled coil structure. J. Mol. Biol., 256:909-923, 1996.
42. Richards, J.R., Bächinger, H.P., Goodman, R.H., Brennan, R.G.: Analysis of the structural properties of CREB and phosphorylated CREB. J. Biol. Chem., 271:13716-13723, 1996.
43. Klatt, P., Pfeiffer, S., List, B.M., Lehner, D., Glatter, O., Bächinger, H.P., Werner, E.R., Schmidt, K., Meyer, B.: Characterization of heme-deficient neuronal nitric oxide synthase reveals a role for heme in subunit dimerization and binding of substrate and tetrahydrobiopterin. J. Biol. Chem., 271:7336-7342 1996.
44. Mechling, D.E., Gambee, J.E., Morris, N.P., Sakai, L.Y., Keene, D.R., Mayne, R., Bächinger, H.P.: Type IX collagen NC1 domain peptides can trimerize in vitro without forming a triple helix. J. Biol. Chem., 271:13781-13785, 1996.
45. Beck, K., Boswell, B.A., Ridgway, C.C., Bächinger, H.P.: Triple helix formation of procollagen type I occurs at the rough endoplasmic reticulum membrane. J. Biol. Chem., 271:21566-21573, 1996.
46. Mann, K., Mechling, D.E., Bächinger, H.P., Eckerskorn, C., Gaill, F., and Timpl, R.. Glycosylated threonine but not 4-hydroxyproline dominates the triple helix stabilizing positions in a sequence of a hydrothermal vent worm cuticle collagen. J. Mol. Biol., 261:255-266, 1996.
47. Reinhardt, D.P., Mechling, D.E., Boswell, B.A., Keene, D.R., Sakai, L.Y., and Bächinger, H.P.: Calcium determines the shape of fibrillin. J. Biol. Chem. 272:7368-7373, 1997.
48. Beck, K., Gambee, J.E., Kamawal, A., and Bächinger, H.P.: A single amino acid can switch the oligomerization state of the a-helical coiled-coil domain of cartilage matrix protein. EMBO J. 16:3767-3777, 1997.
49. Arnold, W. V., Sieron, A. L., Fertala, A., Bächinger, H. P., Mechling, D., and Prockop, D. J.: A cDNA cassette system for the synthesis of recombinant procollagens. Variants of procollagen II lacking a D-period are secreted as triple helical monomers. Matrix Biol. 16:105-116, 1997.
50. Maddox, B. K., Keene, D. R., Sakai, L. Y., Charbonneau, N. L., Morris, N. P., Ridgeway, C. C., Boswell, B. A., Sussman, M. D., Horton, W. A., and Bächinger, H. P., Hecht, J. T. The fate of cartilage oligomeric matrix protein is determined by the cell type in the case of a novel mutation in pseudoachondroplasia. J. Biol. Chem. 272:30993-30997, 1997.
51. Ignatuschenko, M. V., Winter, R. W., Bächinger, H. P., Hinrichs, D. J., and Riscoe, M. K. Xanthones as antimalarial agents; studies of a possible mode of action. FEBS Letters 409:67-73, 1997.
52. Zeng, B., Macdonald, J.R., Bann, J.G., Beck, K., Gambee, J.E., Boswell, B.A., and Bächinger, H.P. Purification and characterization of chicken FKBP65, a peptidyl-prolyl cis-trans isomerase that is only partially inhibited by FK506. Biochem. J. 330:109-114, 1998.
53. Arnold, W. V., Fertala, A., Sieron, A. L., Hattori, H., Mechling, D., Bächinger, H. P., and Prockop, D. J. Recombinant procollagens II: Deletion of D period segments identifies sequences that are required for helix stabilization and generates a temperature sensitive N-proteinase cleavage site. J. Biol. Chem. 273:31822-31828, 1998.
54. Engel, J. and Bächinger, H.P. Collagen-like sequences in phages and bacteria. Proc. Indian Acad. Sci. (Chem. Sci.) 111:81-86, 1999.
55. Burrows, G.G., Chang, J.W., Bächinger, H.P., Bourdette, D.N., Offner, H., and Vandenbark, A.A. Design, engineering and production of functional single-chain T cell receptor ligands. Protein Engineering, 12:771-778, 1999.
56. Reinhardt, D.P., Gambee, J.E., Ono, R.N., Bächinger, H.P., and Sakai, L.Y. Initial steps in assembly of microfibrils require formation of fibrillin intermolecular disulfide crosslinks. J. Biol. Chem., 275:2205-2210, 2000.
57. Reinhardt, D.P., Ono, R.N., Notbohm, H., Müller, P.K., Bächinger, H.P., and Sakai, L.Y. Marfan mutations can render fibrillin-1 more susceptible to proteolysis. J. Biol. Chem. 275:12399-12345, 2000.
58. Maddox, B.K., Mokashi, A., Keene, D.R., and Bächinger, H.P. A cartilage oligomeric matrix protein (COMP) mutation associated with pseudoachondroplasia (PSACH) changes the structural and functional properties of the type 3 domain. J. Biol. Chem. 275:11412-11417, 2000.
59. Engel, J., and Bächinger, H.P. Cooperative equilibrium transitions coupled with a slow annealing step explain the sharpness and hysteresis of collagen folding. Matrix Biology, 19:235-244, 2000.
60. Mechling, D.E., and Bächinger, H.P. The collagen-like peptide (GER)15GPCCG forms pH dependent covalently-linked triple-helical trimers. J. Biol. Chem. 275:14532-14536, 2000.
61. Bann, J.G., Peyton, D.H., and Bächinger, H.P. Sweet is stable: Glycosylation stabilizes collagen. FEBS letters 473:237-240, 2000.
62. Gregory, K.E., Oxford, J.T., Chen, Y., Gambee, J.E., Gygi, S.P., Aebersold, R., Neame, P.J., Mechling, D.E., Bächinger, H.P., and Morris, N.P. Structural organization of distinct domains within the non-collagenous N-terminal region of collagen type XI. J. Biol. Chem. 275:11498-11506, 2000.
63. Bann, J.G., and Bächinger, H.P. Glycosylation/Hydroxylation-induced stabilization of the collagen triple helix: 4 trans-hydroxyproline in the Xaa position can stabilize the triple helix. J. Biol. Chem. 275:24466-24469, 2000.
64. Lampi, K.J., Oxford, J.T., Bächinger, H.P., Shearer, T.R., David, L.L., and Kapfer, D. Deamidation of human b B1 alters the elongated structure of the dimmer. Exp. Eye Res. 72:279-288, 2001.
65. Schumacher, M.A., Rivard, A.F., Bächinger, H.P., and Adelmann, J.P. Structure of the gating domain of a Ca2+ -activated K+ channel complexed with Ca2+ -calmodulin. Nature, 410:1120-1124, 2001.
66. Huffman, J.L., Mokashi, A., Bächinger, H.P., and Brennan, R.G. The basic helix-loop-helix domain of the aryl hydrocarbon receptor nuclear transporter (ARNT) can oligomerize and bind E-box DNA specifically. J. Biol. Chem. 276:40537-40544, 2001.
67. Frank, S., Kammerer, R.A., Mechling, D., Schulthess, T., Landwehr, R., Bann. J., Guo, Y., Lustig, A., Bächinger, H.P., and Engel, J. Stabilization of short collagen-like triple helices by protein engineering. J. Mol. Biol. 308:1081-1089, 2001.
68. Vranka, J., Mokashi, A., Keene, D.R., Tufa, S., Corson, G., Sussman, M., Horton, W.A., Maddox, K., Sakai, L., and Bächinger, H.P. Selective intracellular retention of extracellular matrix proteins and chaperones associated with Pseudoachondroplasia. Matrix Biology, 20:439-450, 2001.
69. Macdonald, J.R. and Bächinger, H.P. HSP47 binds cooperatively to triple helical type I collagen, but has little effect on the thermal stability or the rate of refolding. J. Biol. Chem. 276:25399-25403, 2001.
70. Chang, J.W., Mechling, D.E., Bächinger, H.P., and Burrows, G.G. Design, engineering and production of human recombinant T cell receptor ligands derived from HLA-DR2. J. Biol. Chem., 276:24170-24176, 2001.
71. Bächinger, H.P. and Engel, J. Thermodynamic vs. kinetic stability of collagen triple helices. Matrix Biol., 20:267-269, 2001.
72. Chen, Y., Molloy, S.S., Thomas, L., Gambee, J., Bächinger, H.P., Ferguson, B., Zonana, J., Thomas, G., and Morris, N.P. Mutations within a furin consensus sequence block proteolytic release of Ectodysplasin-A and cause X-linked hypohidrtic ectodermal dysplasia. Proc. Natl. Acad. Sci. USA, 98:7219-7223, 2001.
73. Boudko, S., Frank, S., Kammerer, R.A., Stetefeld, J., Schulthess, T., Landwehr, R., Lustig, A., Bächinger, H.P., and Engel, J. Nucleation and propagation of the collagen triple helix in single-chain and trimerized peptides: transition from 3rd to 1st order kinetics. J. Mol. Biol., 317:459-470, 2002.
74. Moller, T., Franch, T., Hojrup, P., Keene, D.R., Bächinger, H.P., Brennan, R.G., and Valentin-Hansen, P. Hfq: a bacterial Sm-like protein that mediates RNA-RNA interaction. Mol. Cell 9:23-30, 2002.
75. Alfadhli, A., Steel, E., Finlay, L., Bächinger, H.P., and Barklis, E. Hantavirus nucleocapsid protein coiled-coil domains. J. Biol. Chem. 277:27103-27108, 2002.
76. Kapfer, D.M., Kim, Y.H., Bächinger, H.P., Boswell, B.A., Lindner, R.A., Carver, J.A., Shearer, T.R., David, L.L., and Lampi, K.J. Decreased heat stability and increased chaperone requirement of modified human B1-crystallins. Mol Vis. 8:359-366, 2002.
77. Kim, Y.H., Kapfer, D.M., Baekhorst, J., Lubsen, N., Bächinger, H.P., Shearer, T.R., David, L.L., Feix, J.B., and Lampi, K.J. Deamidation, but not truncation, decreases the urea-stability of a lens structural protein, bB1-crystallin. Biochemistry. 26:14076-14084, 2002.
78. Bann, J.G., Bächinger, H.P., and Peyton, D.H. The role of carbohydrate in stabilizing the triple helix in a model for a deep-sea hydrothermal vent worm collagen. Biochemistry 42:4042-4048, 2003.
79. Frank, S., Boudko, S., Mizuno, K., Schulthess, T., Engel. J., and Bächinger, H.P. Collagen triple helix formation can be nucleated at either end. J. Biol. Chem. 278:7747-7750, 2003.
80. Mizuno, K., Hayashi, T., and Bächinger, H.P. Hydroxylation induced stabilization of the collagen triple helix: Further characterization of peptides with 4(R)-hydroxyproline in the Xaa position. J. Biol. Chem. 278:32373-32379, 2003.
81. Mizuno, K. and Bächinger, H. P. Thermal stability and folding of collagen triple helices. Conn. Tissue 35:207-217, 2003.
82. Mizuno, K., Hayashi, T., Peyton, D.H., and Bächinger, H.P. The peptides Ac-(Gly-3(S)Hyp-4(R)Hyp)10-NH2 and Ac-(Gly-Pro-3(S)Hyp)10-NH2 do not form a collagen triple helix. J. Biol. Chem. 279:282-287, 2004.
83. Harms, M. J., Kapfer, D. M., Steel, E., David, L. L., Bächinger, H. P., and Lampi, K. Static and quasi-elastic light scattering determined changes in structure of deamidated BB1-crystallins. Protein Science13:678-686, 2004.
84. Mizuno, K., Whittaker, M. M., Bächinger, H. P., and Whittaker, J. W. Calorimetric studies on the tight-binding metal interactions of E. coli manganese superoxide dismutase. J. Biol. Chem., in press, 2004.
85. Vranka, J., Sakai, L. Y., and Bächinger, H. P. Prolyl 3-hydroxylase 1: Enzyme characterization and identification of a novel family of enzymes. J. Biol. Chem. 279:23615-23621, 2004.
86. Bächinger, H. P. and Engel, J. Thermodynamics and kinetics of collagen folding. Handbook of Protein Folding, Part 1: 1059-1110, 2005. Wiley-VCH (Buchner, J. and Kiefhaber, T., eds.).
87. Engel, J. and Bächinger, H.P. Structure, stability and folding of the collagen triple helix. Topics in Current Chemistry, 247:7-33 ,2005.
88. Mizuno, K., Hayashi, T., Peyton, D., and Bächinger, H.P. Hydroxylation-induced stabilization of the collagen triple helix: Acetyl-(Glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)10-NH2 forms a highly stable triple helix. J. Biol. Chem. 279:38072-38078, 2004.
89. Pokidysheva, E., Milbradt, A., Meier, S., Renner, C., Hässinger, D., Bächinger, H.P., Moroder, L., Grzesiek, S., Holstein, T.W., Özbek, S., and Engel, J. The structure of the Cys-rich terminal domain of Hydra minicollagen, which is invoved in disulfide networks of the nematocyst wall. J. Biol. Chem., 279:30395-30401, 2004.
90. Knosp, W.M., Scott, V., Bächinger, H.P., and Stadler, H.S. HOXA13 directly regulates the expression of bone morphogenetic proteins 2 and 7 to control distal limb morphogenesis. Development 131:4581-4592, 2004.
91. Meier, S., Häussinger, D., Pokidysheva, E., Bächinger, H.P., and Grzesiek, S. Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from <em>Hydra</em> and characterization of its disulfide bond formation. FEBS letters 569:112-116, 2004.
92. 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.
93. 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.
94. 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.
95. 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.
96. 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.
97. 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.
98. 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
99. 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.
100. 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. Biol. Chem., submitted, 2006.
101. 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.
102. Jiravanichanun, N., Mizuno, K., Bächinger, H.P. and Okuyama, K. Threonine in collagen triple-helical structure. Polymer Journal 38:400-4003, 2006.
103. 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.
104. 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.
105. 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.
106. 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.
107. Vranka, J.A., H. Scott Stadler and Bächinger, H.P. Patterns of expression of prolyl 3-hydroxylases in mouse tissues. Submitted, 2007.