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Making better enzymes and protein drugs
29 February 2016
Scientists from the SWITCH laboratory (VIB/KU Leuven) show anti-correlation between number of aggregation prone regions in protein sequence and its solubility.
Novel insights in the attachment of the bacterial carcinogen Helicobacter pylori
14 January 2016
This BabA protein proves to be a molecular chameleon that adapts it binding properties and preference for different ABO-blood group sugars according to their prevalence in different human populations.
Two papers in Nature revealing the receptor activation mechanism for opioid and morphinan analgesics
5 August 2015
Jan Steyaert: 'This knowledge may pave the way to new morphine-like pain killers with fewer side effects.'
Structure and mechanism of ryanodine receptor revealed - step forward in understanding muscle diseases
1 December 2014
Every single moment our life depends on the reliable functioning of muscles. Even slight malfunction of muscles results in diseases.
Structural dynamics in cellular communication
6 August 2014
VIB invites you to ‘Structural dynamics in cellular communication’, a high-level science conference taking place in the heart of Europe (Brussels, Belgium) from 9-10 February, 2015.
Movements of proteins can be predicted from their amino acid sequence
25 November 2013
Researchers of the VIB department of Structural Biology and the ‘Interuniversity Institute of Bioinformatics in Brussels (IB2)’, have developed a method to predict how much the backbone chain of a protein moves based on only its amino acid sequence.
New technology for a more efficient treatment of Pompe disease and other metabolic disorders
19 November 2012
VIB researchers from UGent and Vrije Universiteit Brussel , together with a team of the firm Oxyrane have developed a new technology that can lead to a more efficient and possibly also cheaper therapy for diseases such as Pompe disease.
VIB researchers involved in Brian Kobilka’s Nobel-prizewinning research
10 October 2012
Jan Steyaert and his colleagues were involved in the groundbreaking work in which Brian Kobilka’s research team discovered the structure of these receptors.
Bacterial armor for the first time visualized in minute detail
11 June 2012
Many bacteria protect themselves against threats from the outside world by developing a protective protein layer that acts as armor. Scientists at VIB and Vrije Universiteit Brussel succeeded in imaging the structure of this armor for the first time.
Common drugs initiate a molecular pas de quatre at the surface of the cell membrane
25 July 2011
In a Nature article, an international consortium reveals the complete 3D structure of an activated GPCR (beta-2AR) in a complex with its G protein. The Jan Steyaert Lab (VIB-VUB) produced the Xaperone™ that holds these proteins together.
Cancer turns out to be a p53 protein aggregation disease
28 March 2011
Protein aggregation, generally associated with Alzheimer’s and mad cow disease, turns out to play a significant role in cancer. Certain mutations of p53 cause the protein to aggregate, disrupting its protective function.
Adrenaline receptor ‘frozen in action’ by VIB researchers - Discovery means breakthrough for the development of new drugs based on GPCR’s
12 January 2011
Using tiny antibodies, dubbed Xaperones (TM), scientists from VIB and Vrije Universiteit Brussels collaborated in elucidating the structure of the adrenaline receptor - a scientific first with possibly profound implications for drug development.
Publication in top journal thanks to brand-new NMR Center
9 July 2010
Flemish scientists put NMR to use to find out how the activity of certain proteins involved in the stress physiology of bacteria is regulated. It led to a breakthrough publication in Cell.
Bacteria pack their own demise
30 July 2009
Numerous pathogens contain an ‘internal time bomb’, a deadly mechanism that can be used against them.
Are lipids in the brain an important factor for Alzheimer's disease, Flemish scientists crack the code
10 December 2007
VIB researchers have now discovered that certain lipids, present also in our brains, promote the formation of this protofibril.
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