Zobrazeno 1 - 7
of 7
pro vyhledávání: '"B W Sigurskjold"'
Autor:
B W Sigurskjold, Bilous D, J. Sadowska, Sharma Vp, Michniewicz J, Dubuc G, N.N. Anand, B. Sinnott, David A. Brummell, C. R. Mackenzie
Publikováno v:
Biochemistry. 32:1180-1187
The carbohydrate-binding site in Fab fragments of an antibody specific for Salmonella serogroup B O-polysaccharide has been probed by site-directed mutagenesis using an Escherichia coli expression system. Of the six hypervariable loops, the CDR3 of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::299fa2fa21ff02eb1310c989ab63d733
https://doi.org/10.1021/bi00055a024
https://doi.org/10.1021/bi00055a024
Autor:
B W Sigurskjold, David R. Bundle
Publikováno v:
Journal of Biological Chemistry. 267:8371-8376
The thermodynamic characteristics of oligosaccharide binding to an antibody binding site that is dominated by aromatic amino acids suggest that the hydrophobic effect contributes substantially to complex formation as well as hydrogen bonding and van
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0cc7fb16e21880881c34741b763af949
https://doi.org/10.1016/s0021-9258(18)42454-4
https://doi.org/10.1016/s0021-9258(18)42454-4
Autor:
S. Mandal, J. Sadowska, N.N. Anand, C. R. Mackenzie, David R. Bundle, Saran A. Narang, B W Sigurskjold, N. M. Young
Publikováno v:
Journal of Biological Chemistry. 266:21874-21879
Active single-chain Fv molecules encoded by synthetic genes have been expressed and secreted to the periplasm of Escherichia coli using the ompA secretory signal. Four different constructs were developed to investigate the effects of peptide linker d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89a92a3f464c645848f77715dd3a65b4
https://doi.org/10.1016/s0021-9258(18)54718-9
https://doi.org/10.1016/s0021-9258(18)54718-9
Autor:
J H, Graversen, C, Jacobsen, B W, Sigurskjold, R H, Lorentsen, S K, Moestrup, H C, Thogersen, M, Etzerodt
Publikováno v:
The Journal of biological chemistry. 275(48)
C-type lectin-like domains are found in many proteins, where they mediate binding to a wide diversity of compounds, including carbohydrates, lipids, and proteins. The binding of a C-type lectin-like domain to a ligand is often influenced by calcium.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::24fbdd96e2189fcc5f20fd79dedf126d
https://pubmed.ncbi.nlm.nih.gov/10964919
https://pubmed.ncbi.nlm.nih.gov/10964919
Autor:
D R, Bundle, B W, Sigurskjold
Publikováno v:
Methods in enzymology. 247
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bf4dbc0aa40909dc7a67b829768200e2
https://pubmed.ncbi.nlm.nih.gov/7898359
https://pubmed.ncbi.nlm.nih.gov/7898359
Autor:
B W, Sigurskjold, D R, Bundle
Publikováno v:
The Journal of biological chemistry. 267(12)
The thermodynamic characteristics of oligosaccharide binding to an antibody binding site that is dominated by aromatic amino acids suggest that the hydrophobic effect contributes substantially to complex formation as well as hydrogen bonding and van
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ecaaf2b5a3e4deb7605c187fb7d087fc
https://pubmed.ncbi.nlm.nih.gov/1373726
https://pubmed.ncbi.nlm.nih.gov/1373726
Publikováno v:
ChemInform. 18
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::166bb778bde24b09097efa62e0e679c4
https://doi.org/10.1002/chin.198714044
https://doi.org/10.1002/chin.198714044