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Autor:
W. Göhring
Publikováno v:
HTM Journal of Heat Treatment and Materials. 51:170-175
Carburizing in gas atmospheres generated in situ by introducing a fuel-air mixture into the furnace, results in uniform and reproducible carburized layers with reduced internal oxidation. The reasons for this gas properties are investigated. The domi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d39cc7ec7f190bddd521926b8c5160c
https://doi.org/10.1515/htm-1996-510308
https://doi.org/10.1515/htm-1996-510308
Publikováno v:
HTM Journal of Heat Treatment and Materials. 49:296-305
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2635ebfe77ba7264b02cdbbe6bad2e64
https://doi.org/10.1515/htm-1994-490507
https://doi.org/10.1515/htm-1994-490507
Autor:
B. Edenhofer, W. Göhring
Publikováno v:
HTM Journal of Heat Treatment and Materials. 46:259-268
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c3e5c20ee8a4ec6304d9e2fb975ac06e
https://doi.org/10.1515/htm-1991-460503
https://doi.org/10.1515/htm-1991-460503
Publikováno v:
Journal of molecular biology. 314(4)
Laminin-5 is a typical component of several epithelial tissues and contains a unique gamma2 chain which can be proteolytically processed by BMP-1. This occurs in the N-terminal half of the gamma2 chain (606 residues), which consists of two rod-like t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5069e02d1a847958d880771061333476
https://pubmed.ncbi.nlm.nih.gov/11733994
https://pubmed.ncbi.nlm.nih.gov/11733994
Publikováno v:
European journal of biochemistry. 268(19)
The basement membrane protein, nidogen-1, was previously shown to consist of three globular domains, G1 to G3, and two connecting segments. Nidogen-1 is a major mediator in the formation of ternary complexes with laminins, collagen IV, perlecan and f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::979389f976aaf7be118e912603ea0ce1
https://pubmed.ncbi.nlm.nih.gov/11589703
https://pubmed.ncbi.nlm.nih.gov/11589703
Publikováno v:
Journal of molecular biology. 311(3)
Perlecan, a major basement membrane proteoglycan, has a complex modular structure designed for the binding of many cellular and extracellular ligands. Its domain IV, which consists of a tandem of immunoglobulin-like modules (IG2-IG15), is rich in suc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::daffaa56a9c40aba7daec24a8683cf0a
https://pubmed.ncbi.nlm.nih.gov/11493006
https://pubmed.ncbi.nlm.nih.gov/11493006
Publikováno v:
Nature structural biology. 8(7)
Nidogen, an invariant component of basement membranes, is a multifunctional protein that interacts with most other major basement membrane proteins. Here, we report the crystal structure of the mouse nidogen-1 G2 fragment, which contains binding site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ed4dbf200d9d4fb93de8ffe0efa07582
https://pubmed.ncbi.nlm.nih.gov/11427880
https://pubmed.ncbi.nlm.nih.gov/11427880
Publikováno v:
European journal of biochemistry. 259(3)
Domain IV of mouse perlecan, which consists of 14 immunoglobulin superfamily (IG) modules, was prepared from recombinant human cell culture medium in the form of two fragments, IV-1 (IG2-9, 100 kDa) and IV-2 (IG10-15, 66 kDa). Both fragments bound to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::77cc8f0d1ac31e2d46957db24aa50885
https://pubmed.ncbi.nlm.nih.gov/10092882
https://pubmed.ncbi.nlm.nih.gov/10092882
Publikováno v:
FEBS letters. 430(3)
The N-terminal domains VI plus V (62 kDa) and V alone (43 kDa) of the laminin alpha1 chain were obtained as recombinant products and shown to be folded into a native form by electron microscopy and immunological assays. Domain VI alone, which corresp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::20a4690174061278f9b2104d3628ae96
https://pubmed.ncbi.nlm.nih.gov/9688542
https://pubmed.ncbi.nlm.nih.gov/9688542