Zobrazeno 1 - 10
of 30
pro vyhledávání: '"H P, Bächinger"'
Publikováno v:
The EMBO Journal. 14:3687-3695
Nitric oxide synthases (NOSs), which catalyze the formation of the ubiquitous biological messenger molecule nitric oxide, represent unique cytochrome P-450s, containing reductase and mono-oxygenase domains within one polypeptide and requiring tetrahy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::520c0656e000ae58d8692bb75802a43b
https://doi.org/10.1002/j.1460-2075.1995.tb00038.x
https://doi.org/10.1002/j.1460-2075.1995.tb00038.x
Publikováno v:
The Journal of Immunology. 148:339-346
Anti-phosphocholine (PC)-keyhole limpet hemacyanin hybridomas representative of a memory response that express the lambda 1 L chain isotype have a high reactivity to PC-protein. A common feature of these hybridomas possessing high affinity for PC-pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c5b2ce9f23d68446292c62071db54fcc
https://doi.org/10.4049/jimmunol.148.2.339
https://doi.org/10.4049/jimmunol.148.2.339
Autor:
J G, Bann, H P, Bächinger
Publikováno v:
The Journal of biological chemistry. 275(32)
We have shown recently that glycosylation of threonine in the peptide Ac-(Gly-Pro-Thr)(10)-NH(2) with beta-d-galactose induces the formation of a collagen triple helix, whereas the nonglycosylated peptide does not. In this report, we present evidence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6cdcb061423f36961b865e6e5acb3485
https://pubmed.ncbi.nlm.nih.gov/10827193
https://pubmed.ncbi.nlm.nih.gov/10827193
Publikováno v:
The Journal of biological chemistry. 275(16)
Most extracellular proteins consist of various modules with distinct functions. Mutations in one common type, the calcium-binding epidermal growth factor-like module (cbEGF), can lead to a variety of genetic disorders. Here, we describe as a model sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::203199f8443927b53f858c740d907406
https://pubmed.ncbi.nlm.nih.gov/10766875
https://pubmed.ncbi.nlm.nih.gov/10766875
Publikováno v:
The Journal of biological chemistry. 275(3)
Fibrillins are the major constituents of extracellular microfibrils. How fibrillin molecules assemble into microfibrils is not known. Sequential extractions and pulse-chase labeling of organ cultures of embryonic chick aortae revealed rapid formation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9beea67236421841f2b1aaa4cd065e73
https://pubmed.ncbi.nlm.nih.gov/10636927
https://pubmed.ncbi.nlm.nih.gov/10636927
Autor:
J M, Davis, H P, Bächinger
Publikováno v:
The Journal of biological chemistry. 268(34)
A hysteresis is observed in the triple helix-coil transition of type III collagen. This hysteresis appears in the thermal transition, where it is not solvent-dependent, and also in the transition induced by guanidinium hydrochloride. The transitions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::907660144806f51db2acd02b095dde96
https://pubmed.ncbi.nlm.nih.gov/8245030
https://pubmed.ncbi.nlm.nih.gov/8245030
Publikováno v:
The Journal of biological chemistry. 266(22)
Fibrillin, a connective tissue macromolecule (Mr = 350,000) which is normally insoluble in its tissue form, has been purified from the medium of human skin fibroblast and ligament cells in culture. Analysis of the amino acid composition indicates tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a4def5bccee04cf8b3e74454c3725715
https://pubmed.ncbi.nlm.nih.gov/1860873
https://pubmed.ncbi.nlm.nih.gov/1860873
Autor:
H P, Bächinger, N P, Morris, G P, Lunstrum, D R, Keene, L M, Rosenbaum, L A, Compton, R E, Burgeson
Publikováno v:
The Journal of biological chemistry. 265(17)
Type VII collagen is a major component of anchoring fibrils, which are 800-nm-long centrosymmetrically cross-banded fibrils that are believed to secure the attachment of certain epithelial basement membranes to the underlying stromal matrix. The ultr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::50728635194bd75603421088df3f58ff
https://pubmed.ncbi.nlm.nih.gov/2112541
https://pubmed.ncbi.nlm.nih.gov/2112541
Publikováno v:
Journal of Biological Chemistry. 258:5869-5877
Procollagen IV was isolated from culture media of the mouse endodermal cell line PF-HR9. Some of the triple helical procollagen IV molecules were associated at their NH2 ends to tetramers which were identified by electron microscopy, velocity sedimen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::80263acd6a8a33ebf2ee7576d3c24634
https://doi.org/10.1016/s0021-9258(20)81976-0
https://doi.org/10.1016/s0021-9258(20)81976-0
Autor:
H P Bächinger, N P Morris
Publikováno v:
Journal of Biological Chemistry. 262:11345-11350
Three collagen chains, 1 alpha, 2 alpha, and 3 alpha, have previously been identified in the cartilaginous extracellular matrix and have been referred to collectively as type XI collagen. The structure of type XI is poorly defined. Neither the organi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2d7afe2a364af25b13153080b01e6256
https://doi.org/10.1016/s0021-9258(18)60965-2
https://doi.org/10.1016/s0021-9258(18)60965-2