James M Flink
Overview
Explore the profile of James M Flink including associated specialties, affiliations and a list of published articles.
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Articles
6
Citations
225
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Recent Articles
1.
Grohganz H, Gildemyn D, Skibsted E, Flink J, Rantanen J
J Pharm Sci
. 2011 Jan;
100(7):2871-5.
PMID: 21259241
Noninvasive near-infrared (NIR) and Raman spectroscopies were applied to provide a fast and efficient insight into the formation of different mannitol solid forms occurring in freeze-dried formulations. Multivariate data analysis...
2.
Grohganz H, Gildemyn D, Skibsted E, Flink J, Rantanen J
Anal Chim Acta
. 2010 Aug;
676(1-2):34-40.
PMID: 20800739
The possibility for determination of the water content in pharmaceutical samples by near-infrared (NIR) spectroscopy has been more widely investigated in the past few years. However, many studies claim that...
3.
Groenning M, Norrman M, Flink J, van de Weert M, Bukrinsky J, Schluckebier G, et al.
J Struct Biol
. 2007 Aug;
159(3):483-97.
PMID: 17681791
Amyloid fibrils share various common structural features and their presence can be detected by Thioflavin T (ThT). In this paper, the binding mode of ThT to insulin amyloid fibrils was...
4.
Vestergaard B, Groenning M, Roessle M, Kastrup J, van de Weert M, Flink J, et al.
PLoS Biol
. 2007 May;
5(5):e134.
PMID: 17472440
Although amyloid fibrillation is generally believed to be a nucleation-dependent process, the nuclei are largely structurally uncharacterized. This is in part due to the inherent experimental challenge associated with structural...
5.
Groenning M, Olsen L, van de Weert M, Flink J, Frokjaer S, Jorgensen F
J Struct Biol
. 2007 Feb;
158(3):358-69.
PMID: 17289401
Amyloid fibril formation plays a role in more than 20 diseases including Alzheimer's disease. In vitro detection of these fibrils is often performed using Thioflavin T (ThT), though the ThT...
6.
Pedersen J, Flink J, Dikov D, Otzen D
Biophys J
. 2006 Mar;
90(11):4181-94.
PMID: 16533857
Recent work suggests that protein fibrillation mechanisms and the structure of the resulting protein fibrils are very sensitive to environmental conditions such as temperature and ionic strength. Here we report...