Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Åsa Frostell-Karlsson"'
Publikováno v:
Journal of the Renin-Angiotensin-Aldosterone System, Vol 2 (2001)
Introduction Angiotensin II AT 1-receptor antagonists are highly bound to plasma proteins (≥ 99%). With some antagonists, such as DuP-532, the protein binding was such that no efficacy of the drug could be demonstrated clinically. Whether protein b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57aa48303660b372d29d065b0cf693a4
https://pubmed.ncbi.nlm.nih.gov/28095232
https://pubmed.ncbi.nlm.nih.gov/28095232
Autor:
Anita Larsson, Markku Hämäläinen, S. Abbas, Mia Bennemo, Åsa Frostell-Karlsson, C. Estmer Nilsson
Publikováno v:
Vaccine. 28:759-766
Quantification of hemagglutinin (HA) by single-radial immuno diffusion (SRID) is the predominant method to ensure product potency in seasonal influenza vaccines. Here a new method for quantification of influenza virus using biosensor technology is pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07b63b6a253d4b2f69d030c1b3ab81d3
https://doi.org/10.1016/j.vaccine.2009.10.070
https://doi.org/10.1016/j.vaccine.2009.10.070
Publikováno v:
Analytical Biochemistry. 353:217-225
Reversible protein phosphorylation of serine, threonine, and tyrosine residues by protein kinases and phosphatases is important for the regulation of cellular signal transduction and controls many cellular functions. Disturbances in this regulation h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f969b4c81e286c9d97cee6ca733afa1
https://doi.org/10.1016/j.ab.2006.03.004
https://doi.org/10.1016/j.ab.2006.03.004
Autor:
Markku Hämäläinen, Robert Karlsson, Katherine S. Fenner, Åsa Frostell-Karlsson, Helena Widegren, Lena Westerlund, Han van de Waterbeemd, Caroline E Green
Publikováno v:
Journal of Pharmaceutical Sciences. 94:25-37
The interactions between 78 drug compounds and immobilised liposomes were investigated using an assay based on surface plasmon resonance technology. The drugs were screened at a single concentration and allowed to interact simultaneously with two dif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4274ca7ce53b8dd476ab069922c550fa
https://doi.org/10.1002/jps.20215
https://doi.org/10.1002/jps.20215
Autor:
Markku Hämäläinen, Robert Karlsson, Annika Remaeus, Karl Andersson, Åsa Frostell-Karlsson, Peter Borg, Håkan Roos
Publikováno v:
Journal of Medicinal Chemistry. 43:1986-1992
The interactions between a set of drugs, selected on the basis of reported human serum albumin (HSA) binding levels, and immobilized HSA were investigated using surface plasmon resonance technology. Major HSA binding sites were available after immobi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d827d3f5c829077b4374b51451c2306
https://doi.org/10.1021/jm991174y
https://doi.org/10.1021/jm991174y
Publikováno v:
Journal of Chromatography A. 597:397-410
A system for real-time biospecific interaction analysis using biosensor technology based on the optical phenomenon surface plasmon resonance is described. The biospecific interface is a sensor chip covered with a hydrogel matrix. One component of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e689e85c9d2dd520796969e7ff40f31
https://doi.org/10.1016/0021-9673(92)80137-j
https://doi.org/10.1016/0021-9673(92)80137-j
Autor:
Anna Hansson, Kjell Magnusson, Jonas Lidholm, Fredrik Edebratt, Lars Nieba, Åsa Frostell Karlsson, Andreas Plückthun, Sabine E. Nieba-Axmann, Anette Persson, Markku Hämäläinen
Publikováno v:
Analytical biochemistry. 252(2)
While BIACORE instruments are routinely used for kinetic measurements and for the determination of binding constants, the immobilization of a ligand onto the sensor chip surface has to be individually optimized for every system. We show here that the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d4715097de2f588dfca991028520ad3
https://pubmed.ncbi.nlm.nih.gov/9344407
https://pubmed.ncbi.nlm.nih.gov/9344407