Zobrazeno 1 - 10
of 88
pro vyhledávání: '"F C, Wiberg"'
Publikováno v:
Biochemistry. 32:114-119
Previous studies have identified a putative calcium binding site involving two glutamic acid residues located in the protease domain of coagulation factor IX. Amino acid sequence homology considerations suggest that factor VII (FVII) possesses a simi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16b74d7351d1be5d5685c8f82cf4715b
https://doi.org/10.1021/bi00052a016
https://doi.org/10.1021/bi00052a016
Autor:
P M Christensen, Anders H. Pedersen, T C Beck, K B Moeller, F Norris, F C Wiberg, U Hedner, O. Nordfang, K Norris, J Meidahl-Pedersen
Publikováno v:
Journal of Biological Chemistry. 265:16786-16793
Previous studies have shown that extrinsic pathway inhibitor (EPI) is an effective inhibitor of factor Xa alone or factor VIIa-tissue factor complex in the presence of factor Xa. Since tissue factor exposure is implicated in thrombogenesis, we hypoth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d9316afedad0c439e172f9d66f3e8044
https://doi.org/10.1016/s0021-9258(17)44829-0
https://doi.org/10.1016/s0021-9258(17)44829-0
Publikováno v:
The Journal of biological chemistry. 274(52)
We have investigated the role of the C-terminal of the alpha-subunit in the insulin receptor family by characterizing chimeric mini-receptor constructs comprising the first three domains (468 amino acids) of insulin receptor (IR) or insulin-like grow
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::42e8268d685e9b3ff786bad5cd9033cd
https://pubmed.ncbi.nlm.nih.gov/10601304
https://pubmed.ncbi.nlm.nih.gov/10601304
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 54(Pt 1)
Crystals of the monomeric and dimeric forms of human neutrophil gelatinase associated lipocalin have been grown in hanging-drop vapor-diffusion trials using PEG as a precipitating agent with recombinant protein expressed in a baculovirus-based system
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c94ab3d292656651ce23d9dbf83adfc3
https://pubmed.ncbi.nlm.nih.gov/9761822
https://pubmed.ncbi.nlm.nih.gov/9761822
Publikováno v:
The Journal of biological chemistry. 273(28)
In order to characterize regions of the insulin receptor that are essential for ligand binding and possibly identify a smaller insulin-binding fragment of the receptor, we have used site-directed mutagenesis to construct a series of insulin receptor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::39c8cfa6ad851ac378577a22194f882c
https://pubmed.ncbi.nlm.nih.gov/9651379
https://pubmed.ncbi.nlm.nih.gov/9651379
Autor:
N P, Møller, K B, Møller, R, Lammers, A, Kharitonenkov, E, Hoppe, F C, Wiberg, I, Sures, A, Ullrich
Publikováno v:
The Journal of biological chemistry. 270(39)
Binding of insulin to its receptor (IR) causes rapid autophosphorylation with concomitant activation of its tyrosine kinase which transmits the signal by phosphorylating cellular substrates. The IR activity is controlled by protein-tyrosine phosphata
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3a5b9b4cabef635b7f618f9878380eb3
https://pubmed.ncbi.nlm.nih.gov/7559456
https://pubmed.ncbi.nlm.nih.gov/7559456
Publikováno v:
The Journal of biological chemistry. 269(52)
The exact nature of how the insulin molecule interacts with the insulin receptor is obscure although chimeric receptors have shown that the ligand specificity of the insulin receptor and the IGF-I receptor (i.e. the sequences that discriminate betwee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2544b00439ddde97fa139f9307445baa
https://pubmed.ncbi.nlm.nih.gov/7806523
https://pubmed.ncbi.nlm.nih.gov/7806523
Autor:
L, Schäffer, T, Kjeldsen, A S, Andersen, F C, Wiberg, U D, Larsen, J F, Cara, R G, Mirmira, S H, Nakagawa, H S, Tager
Publikováno v:
The Journal of biological chemistry. 268(5)
We have examined, by use of a hybrid insulin/insulin-like growth factor-I analog and chimeric insulin/type I insulin-like growth factor receptors, the interplay between ligand and receptor structure in determining the affinity and specificity of horm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d04a5ee09f6d12d8ad6b645349094474
https://pubmed.ncbi.nlm.nih.gov/8428981
https://pubmed.ncbi.nlm.nih.gov/8428981
Autor:
A S, Andersen, T, Kjeldsen, F C, Wiberg, H, Vissing, L, Schäffer, J S, Rasmussen, P, De Meyts, N P, Møller
Publikováno v:
The Journal of biological chemistry. 267(19)
We have previously shown, using truncated soluble recombinant receptors, that substituting the 62 N-terminal amino acids of the alpha subunit from the insulin-like growth factor I receptor (IGFIR) with the corresponding 68 amino acids from the insuli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e60fc85c8c547fe682ce5117ccb9b1d3
https://pubmed.ncbi.nlm.nih.gov/1320025
https://pubmed.ncbi.nlm.nih.gov/1320025
Publikováno v:
The Journal of biological chemistry. 266(28)
Insulin receptors can be purified by affinity chromatography on immobilized insulin, but published methods all suffer from a rather low capacity of the affinity columns. By using insulin that has been protected in positions A1 and B29, we have been a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::88a4da5a9479c7ca016b6a881e27f02e
https://pubmed.ncbi.nlm.nih.gov/1918001
https://pubmed.ncbi.nlm.nih.gov/1918001