Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Michael, Rheinnecker"'
Autor:
Henning Hanken, Max Heiland, Andreas Kolk, Michael Rheinnecker, Manuela Sachse, Michael Wöltje, Christian Große-Siestrup, Christine Knabe, Alexander Gröbe, Ralf Smeets, Rolf Zehbe
Publikováno v:
Journal of Biomedical Materials Research Part B: Applied Biomaterials. 105:2603-2611
This study assesses the biocompatibility of novel silk protein membranes with and without modification, and evaluates their effect on facilitating bone formation and defect repair in guided bone regeneration. Two calvarian bone defects 12 mm in diame
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f169d275195a3b4ef7c179a7569ec22a
https://doi.org/10.1002/jbm.b.33795
https://doi.org/10.1002/jbm.b.33795
Autor:
Ralf, Smeets, Christine, Knabe, Andreas, Kolk, Michael, Rheinnecker, Alexander, Gröbe, Max, Heiland, Rolf, Zehbe, Manuela, Sachse, Christian, Große-Siestrup, Michael, Wöltje, Henning, Hanken
Publikováno v:
Journal of biomedical materials research. Part B, Applied biomaterials. 105(8)
This study assesses the biocompatibility of novel silk protein membranes with and without modification, and evaluates their effect on facilitating bone formation and defect repair in guided bone regeneration. Two calvarian bone defects 12 mm in diame
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b30c954157d98e8ed759e8a3c069fb80
https://pubmed.ncbi.nlm.nih.gov/27731930
https://pubmed.ncbi.nlm.nih.gov/27731930
Autor:
Henning Hanken, Andreas M. Luebke, Robert Gaudin, Ralf Smeets, Max Heiland, Katharina Grupp, Michael Rheinnecker, Oliver Vorwig, Benedicta Beck-Broichsitter, Michael Wöltje, Alexander Gröbe
Publikováno v:
Oral surgery, oral medicine, oral pathology and oral radiology. 121(5)
To evaluate a novel microvascular anastomosis technique using N-fibroin stents.Cylinder stents of 1 mm diameter and 5 mm length were fabricated using N-fibroin from silkworms. In 22 rats, aortas were dissected, and the stent was inserted into the two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5b6306a5c843749694c1ec0f4eba24f
https://pubmed.ncbi.nlm.nih.gov/27765339
https://pubmed.ncbi.nlm.nih.gov/27765339
Autor:
Melanie Böbel, Silvia Cappellozza, Alessio Saviane, Gianluca Tettamanti, Michael Wöltje, Eleonora Franzetti, Michael Rheinnecker
Publikováno v:
Applied microbiology and biotechnology. 98(10)
The silkworm Bombyx mori represents an established in vivo system for the production of recombinant proteins. Baculoviruses have been extensively investigated and optimised for the expression of high protein levels inside the haemolymph of larvae and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3159d28f296bf776e70d50b5bfc627a3
https://pubmed.ncbi.nlm.nih.gov/24477386
https://pubmed.ncbi.nlm.nih.gov/24477386
Publikováno v:
Biochemistry. 34:13051-13058
The structural basis for the stability of a partly solvent-exposed hydrophobic minicore, formed by the residues Leu51, Val57, and Phe69 in the reactive loop of the serine protease inhibitor chymotrypsin inhibitor 2 (CI2), was analyzed from the stabil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::677928ecb2b00ca95c73800567d3e96a
https://doi.org/10.1021/bi00040a016
https://doi.org/10.1021/bi00040a016
Publikováno v:
Biochemistry. 33:221-225
A strategy for increasing the size of the S4 binding pocket was used to improve the specificity of subtilisin BPN' toward substrates with large hydrophobic P4 side chains. This approach involves single and double amino acid replacements at positions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1af0e5865fbc85973613639be44c6f79
https://doi.org/10.1021/bi00167a029
https://doi.org/10.1021/bi00167a029
Publikováno v:
Biochemistry. 32:18-26
Subtilisin BPN', an extracellular serine protease from Bacillus amyloliquefaciens, requires a 77 amino acid pro-sequence for correct folding in vivo. We report the observation of a metastable folding intermediate during the refolding of wild-type and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd804310e7aa70b594f857695e25a268
https://doi.org/10.1021/bi00052a004
https://doi.org/10.1021/bi00052a004
Publikováno v:
Journal of molecular biology. 233(2)
Subtilisin BPN' is an extracellular serine protease from Bacillus amyloliquefaciens that requires an N-terminal 77 amino acid pro-sequence for correct folding of the catalytic domain. We have expressed an inactive, stable pro-subtilisin variant in Es
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87094e35d4d483058cc9575a1ea93301
https://pubmed.ncbi.nlm.nih.gov/8377204
https://pubmed.ncbi.nlm.nih.gov/8377204
Publikováno v:
Biochemistry. 32(5)
The specificity of subtilisin BPN' toward substrates with large hydrophobic P4 residues has been improved by single amino acid replacements at positions 104 and 107. Mutations were designed to (i) increase the size of the P4 binding pocket by replaci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::008eaa4794f8ef60dcef1685b75387ed
https://pubmed.ncbi.nlm.nih.gov/8448130
https://pubmed.ncbi.nlm.nih.gov/8448130
Publikováno v:
FEBS Letters. (3):349-352
Variants of subtilisin BPN' that possess improved specificity towards isoleucine compared with alanine at the P4 position of small peptide substrates, were analysed for their ability to bind chymotrypsin inhibitor 2. The binding of the inhibitor with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b7298335917288c0e7b7811281cb471