| 1. |
- Kehoe, Laura, et al.
(författare)
-
Make EU trade with Brazil sustainable
- 2019
-
Ingår i: Science. - : American Association for the Advancement of Science (AAAS). - 0036-8075 .- 1095-9203. ; 364:6438, s. 341-
-
Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)
|
|
| 2. |
- Andersson, Evert, et al.
(författare)
-
How to find a compromise between track friendliness and the ability to run at high speed
- 2012
-
Ingår i: Civil-Comp Proceedings. - Stirlingshire, UK : Civil-Comp Press. - 1759-3433. ; 98
-
Tidskriftsartikel (refereegranskat)abstract
- When designing and optimizing a rail vehicle there is a contradiction between, on the one hand, stability on straight track at high speed and, on the other hand, reasonable wheel and rail wear in small- and medium-radius curves. This paper describes the process of developing and optimizing a track-friendly bogie. A simulation model has been used to investigate dynamic stability on straight track at high speeds along with the wheel and rail wear in sharper curves. The result is a bogie with relatively soft wheelset guidance allowing passive radial self-steering, which in combination with appropriate yaw damping ensures stability on straight track at higher speeds. This bogie has been tested according to EN 14363 at speeds up to about 300 km/h and in curves with radii ranging from 250 m and up.
|
|
| 3. |
|
|
| 4. |
|
|
| 5. |
|
|
| 6. |
-
Bergtagen
- 2020. - 200
-
Editorial collection (pop. science, debate, etc.)
|
|
| 7. |
- Braam, Svenja, 1989, et al.
(author)
-
Exploring carbon source related localization and phosphorylation in the Snf1/Mig1 network using population and single cell-based a pproaches
- 2024
-
In: MICROBIAL CELL. - 2311-2638. ; 11:1, s. 143-154
-
Journal article (peer-reviewed)abstract
- The AMPK/SNF1 pathway governs energy balance in eukaryotic cells, notably influencing glucose de-repression. In S. cerevisiae , Snf1 is phosphorylated and hence activated upon glucose depletion. This activation is required but is not sufficient for mediating glucose de-repression, indicating further glucosedependent regulation mechanisms. Employing fluorescence recovery after photobleaching (FRAP) in conjunction with non -linear mixed effects modelling, we explore the spatial dynamics of Snf1 as well as the relationship between Snf1 phosphorylation and its target Mig1 controlled by hexose sugars. Our results suggest that inactivation of Snf1 modulates Mig1 localization and that the kinetic of Snf1 localization to the nucleus is modulated by the presence of non -fermentable carbon sources. Our data offer insight into the true complexity of regulation of this central signaling pathway in orchestrating cellular responses to fluctuating environmental cues. These insights not only expand our understanding of glucose homeostasis but also pave the way for further studies evaluating the importance of Snf1 localization in relation to its phosphorylation state and regulation of downstream targets.
|
|
| 8. |
- Braam, Svenja, 1989, et al.
(author)
-
Exploring carbon source related localization and phosphorylation in the Snf1/Mig1 network using population and single cell-based approaches
- 2024
-
In: Microbial Cell. - 2311-2638. ; 11:1, s. 143-154
-
Journal article (peer-reviewed)abstract
- The AMPK/SNF1 pathway governs energy balance in eukaryotic cells, notably influencing glucose de-repression. In S. cerevisiae, Snf1 is phosphorylated and hence activated upon glucose depletion. This activation is required but is not sufficient for mediating glucose de-repression, indicating further glucose-dependent regulation mechanisms. Employing fluorescence recovery after photobleaching (FRAP) in conjunction with non-linear mixed effects modelling, we explore the spatial dynamics of Snf1 as well as the relationship between Snf1 phosphorylation and its target Mig1 controlled by hexose sugars. Our results suggest that inactivation of Snf1 modulates Mig1 localization and that the kinetic of Snf1 localization to the nucleus is modulated by the presence of non-fermentable carbon sources. Our data offer insight into the true complexity of regulation of this central signaling pathway in orchestrating cellular responses to fluctuating environmental cues. These insights not only expand our understanding of glucose homeostasis but also pave the way for further studies evaluating the importance of Snf1 localization in relation to its phosphorylation state and regulation of downstream targets.
|
|
| 9. |
- Carlsson, Jonas, et al.
(author)
-
A folding study on IAPP (Islet Amyloid Polypeptide) using molecular dynamics simulations
-
Other publication (other academic/artistic)abstract
- Amyloidosis is the largest group among the protein misfolding diseases, and includes well known diseases such as Alzheimer’s disease and type 2 diabetes. In the latter, islet amyloid is present in the pancreas in almost all individuals. Today, more than 25 different proteins have been isolated from amyloid deposits in human. Even though these proteins differ in size, charge and sequence they all have the capacity to assemble in to fibrillar structures with inseparable morphological appearance. Therefore, it can be assumed that the fibril process is based upon principles that are general for all proteins and knowledge derived from one protein can be used for other amyloid proteins. In this paper, we study the process of amyloid formation in parts of islet amyloid polypeptide (residues 18-29 and 11-37) by analyzing mutations using three different in silico methods. Finally, we use the methods to predict the amyloidogenic properties of the native IAPP and 16 variants thereof and compare the result with in vitro measurements. Using a consensus prediction of the three methods we managed to correctly classify all but two peptides. We have also given further evidence to the importance of S28P for inhibiting amyloid fibre formation, found evidence for antiparallel stacking, and identified important regions for beta sheet stability.
|
|
| 10. |
|
|
