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The Journal of Biological Chemistry|May 25, 1989
Thermal stability and folding of type IV procollagen and effect of peptidyl-prolyl cis-trans-isomerase on the folding of the triple helixJ M Davis, B A Boswell, H P Bächinger
The Journal of Biological Chemistry|August 25, 1982
Mouse procollagen IV. Characterization and supramolecular associationH P Bächinger, L I Fessler, J H Fessler
FEBS Letters|May 17, 2000
Sweet is stable: glycosylation stabilizes collagenJ G Bann, D H Peyton, H P Bächinger
European Journal of Biochemistry|December 1, 1978
Physical evidence for the assembly of A and B chains of human placental collagen in a single triple helixH Bentz, H P Bächinger, R Glanville, et al.
American Journal of Medical Genetics|January 15, 1993
Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type I collagenH P Bächinger, N P Morris, J M Davis
The EMBO Journal|July 1, 1997
A single amino acid can switch the oligomerization state of the alpha-helical coiled-coil domain of cartilage matrix proteinK Beck, J E Gambee, A Kamawal, et al.
The Journal of Biological Chemistry|August 30, 1996
Triple helix formation of procollagen type I can occur at the rough endoplasmic reticulum membraneK Beck, B A Boswell, C C Ridgway, et al.
The Journal of Biological Chemistry|August 15, 2001
The basic helix-loop-helix domain of the aryl hydrocarbon receptor nuclear transporter (ARNT) can oligomerize and bind E-box DNA specificallyJ L Huffman, A Mokashi, H P Bächinger, et al.
The Journal of Biological Chemistry|February 7, 2001
A cartilage oligomeric matrix protein mutation associated with pseudoachondroplasia changes the structural and functional properties of the type 3 domainB K Maddox, A Mokashi, D R Keene, et al.
The Journal of Biological Chemistry|December 25, 1981
Chain assembly intermediate in the biosynthesis of type III procollagen in chick embryo blood vesselsH P Bächinger, L I Fessler, R Timpl, et al.
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