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Uppsala, Sweden

Andersson K.,Uppsala University | Andersson K.,Ridgeview Diagnostics AB | Andersson K.,Ridgeview Instruments AB
Journal of Analytical Oncology | Year: 2013

In conjunction with the defense of a doctoral thesis on the deciphering of complex protein interactions on living cells, six scientists shared their view on time in molecular and cellular biology. This brief review takes the form of a conference report and summarizes the contributions of the speakers and the defense. Opportunities and challenges for time resolved assays in molecular and cellular biology were vividly discussed during two days with a pan-European audience. Awareness of biological timeframes and understanding the temporal aspects were claimed critical for analytical applications in biology. © 2013 Lifescience Global. Source


Patent
Ridgeview Diagnostics Ab | Date: 2013-05-30

A method for assessing if an individual or an animal has a selected condition includes: obtaining a biological sample from the individual or animal; detecting in a time-resolved manner the presence of a disease related target through use of a probe (


Altschuh D.,University of Strasbourg | Bjorkelund H.,Ridgeview Instruments AB | Bjorkelund H.,Uppsala University | Strandgard J.,Ridgeview Instruments AB | And 7 more authors.
Biochemical and Biophysical Research Communications | Year: 2012

Cellular receptor systems are expected to present complex ligand interaction patterns that cannot be evaluated assuming a simple one ligand:one receptor interaction model. We have previously evaluated heterogeneous interactions using an alternative method to regression analysis, called Interaction Map (IM). IM decomposes a time-resolved binding curve into its separate components. By replacing the reductionistic, scalar kinetic association rate constant ka and dissociation rate constant kd with a two-dimensional distribution of ka and kd, it is possible to display heterogeneous data as a map where each peak corresponds to one of the components that contribute to the cumulative binding curve. Here we challenge the Interaction Map approach by artificially generating heterogeneous data from two known interactions, on either LigandTracer or Surface Plasmon Resonance devices. We prove the ability of IM to accurately decompose these man-made heterogeneous binding curves composed of two different interactions. We conclude that the Interaction Map approach is well suited for the analysis of complex binding data and forecast that it has a potential to resolve previously uninterpretable data, in particular those generated in cell-based assays. © 2012 Elsevier Inc. Source


Gedda L.,Oncology and Radiation Science | Bjorkelund H.,Oncology and Radiation Science | Lebel L.,Ridgeview Diagnostics AB | Asplund A.,Uppsala University | And 7 more authors.
Applied Immunohistochemistry and Molecular Morphology | Year: 2013

Immunohistochemical study (IHC) is a critical tool in the clinical diagnosis of breast cancer. One common assessment is the expression level of the HER2 receptor in breast cancer tissue samples with the aim of stratifying patients for applicability of the therapeutic antibody Herceptin. In this study, we aimed to investigate whether a novel assay, real-time IHC combined with Interaction Map analysis, offers the possibility of objective assessment of HER2 expression. Interaction Map presents real-time interaction data as a collection of peaks on a surface, and it was performed on 20 patient tissue samples previously scored for HER2 expression. The result shows that the relative weight of the peaks in the maps contains novel information that could discriminate between high and low HER2 expression in an operator-independent manner (P<0.001). We conclude that the real-time IHC assay has a promising potential to complement conventional IHC and may improve the precision in the future clinical diagnostics of breast cancer.©2013 by Lippincott Williams& Wilkins. Source


Peess C.,Roche Holding AG | Von Proff L.,Roche Holding AG | Goller S.,Roche Holding AG | Andersson K.,Ridgeview Diagnostics AB | And 4 more authors.
PLoS ONE | Year: 2015

For the development of efficient anti-cancer therapeutics against the HER receptor family it is indispensable to understand the mechanistic model of the HER receptor activation upon ligand binding. Due to its high complexity the binding mode of Heregulin 1 beta (HRG1β) with its receptor HER3 is so far not understood. Analysis of the interaction of HRG1β with surface immobilized HER3 extracellular domain by time-resolved Surface Plasmon Resonance (SPR) was so far not interpretable using any regular analysis method as the interaction was highly complex. Here, we show that Interaction Map (IM) made it possible to shed light on this interaction. IM allowed deciphering the rate limiting kinetic contributions from complex SPR sensorgrams and thereby enabling the extraction of discrete kinetic rate components from the apparently heterogeneous interactions. We could resolve details from the complex avidity-driven binding mode of HRG1β with HER3 by using a combination of SPR and IM data. Our findings contribute to the general understanding that a major conformational change of HER3 during its activation is induced by a complex sequential HRG1β docking mode. © 2015 Peess et al. Source

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