MIMS/UCMR Mini-Symposium, 29 May 2018
 Welcome to the 3rd MIMS/UCMR-Mini-Symposium of the year!
Welcome to the 3rd MIMS/UCMR-Mini-Symposium of the year!
29 May 2018, 9:00 - 11:50
Bergasalen, Umeå University Hospital (NUS), South Entrance
In the first session presentations by the Oliver Billker, appointed new Director of MIMS from 1st October, Barbara Sixt, new MIMS Group Leader,  Gemma Atkinson and Linda Sandblad, recipients of UCMR Gender Policy Support. In the second session five Postdoctoral Fellows from the MIMS/UCMR Postdoctoral Programme will present: Christian Pett, Hiraku Takada, Ravendra Nagampalli, Dharmedra Kumar Soni, Rajender Kumar.
Hosts: Bernt Eric Uhlin, Maria Fällman, Elisabeth Sauer-Eriksson, Åke Forsberg
Please register here latest on 27 May:
https://kbc-forms.upsc.se/forms/75-ucmr-mims-minisymposium.html
Contact for questions: Eva-Maria Diehl, This email address is being protected from spambots. You need JavaScript enabled to view it.
NOTE the programme is updated (Christian Pett's presentation has been cancelled)
 
	 
	
 [2020-05-11] When stressed or starved, bacteria regulate their metabolism by producing signalling molecules called alarmones or ‘magic spots’. In the majority of bacteria, the magic spot compounds are both made and destroyed by a large, complex enzyme called Rel. The question of how Rel switches from making the alarmone to degrading it was finally resolved by an international team from Sweden – Vasili Hauryliuk (MIMS & UCMR) – and Belgium: Jelle Hendrix (Hasselt University) and Abel Garcia-Pino (Université Libre de Bruxelles). The results of this study were published in the high impact journal Nature Chemical Biology ("A nucleotide-switch mechanism mediates opposing catalytic activities of Rel enzymes", 11 May 2020).
[2020-05-11] When stressed or starved, bacteria regulate their metabolism by producing signalling molecules called alarmones or ‘magic spots’. In the majority of bacteria, the magic spot compounds are both made and destroyed by a large, complex enzyme called Rel. The question of how Rel switches from making the alarmone to degrading it was finally resolved by an international team from Sweden – Vasili Hauryliuk (MIMS & UCMR) – and Belgium: Jelle Hendrix (Hasselt University) and Abel Garcia-Pino (Université Libre de Bruxelles). The results of this study were published in the high impact journal Nature Chemical Biology ("A nucleotide-switch mechanism mediates opposing catalytic activities of Rel enzymes", 11 May 2020).


 More information and registration
More information and registration