4 research departments
750 employees
45 nationalities
49 research teams
11 ERC laureates
250 publications per year
24000 m² lab area

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Fondation universite de Strasbourg
Monday, August 17th 2015 - 11 a.m.
Dr Farrah El-Saafin

Investigating the Molecular and Cellular function of TAF8

Friday, August 28th 2015 - 11 a.m.
Dr Nabil Djouder

Growth factors, Nutrients and Cancer

Médaille de bronze 2015 CNRS : Evi SOUTOGLOU Médaille de cristal 2015 CNRS : Philippe ANDRE


IGBMC call for group leaders positions in Bioinformatics

June 2, 2015



IGBMC is recruiting up to 4 new group leaders in Bioinformatics with support from the Laboratory of Excellence (LabEx INRT) initiative.

  • Application deadline: 3 August 2015.

  • Interviews: 24 & 25 September 2015.

 New groups are expected to start in 2016.


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Cardiac valves development directly depends on two proteins sensitive to blood flows forces

© IGBMC


The embryonic formation of the cardiac valves allows the blood flow to favor little by little a one-way circulation.

The expression level of the gene klf2a and the formation of the cardiac valves depend on flow oscillations intensity that induce an increase in intracellular Ca+ rates via Trpv4 and Trpp2 ionic channels.

 

 

May 12, 2015


The team of Julien Vermot at IGBMC has evidenced how the mechanical forces generated by blood flows activate the embryonic cardiac valves formation. They show that force sensing is mediated by two transient receptor channel, Trpv4 and Trpp2 (or PC2).

Cardiac valves anomalies are among the most frequent human cardiovascular system anomalies and abnormal valve are usually replaced by valve transplantation directly in the patient.

These results lead to a better understanding of the contribution of mechanical forces during cardiac morphogenesis and might contribute to optimize in vitro valves formation.
These results are published on May 7th, 2015 in the Current Biology.

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A dual role for Parp3 during immunoglobulin class switch recombination

© IGBMC

 

While being dispensable for somatic hypermutation (SHM), the DNA repair factor Parp3 plays a dual role during immunoglobulin class switch recombination (CSR). Parp3 promotes the repair of double stranded DNA breaks (DSBs) induced by AID through the non homologous end joining (NHEJ) pathway and protects the immunoglobulin heavy (IgH) chain locus from sustained AID-induced DNA damage by promoting the eviction of the mutagenic enzymatic activity of AID from chromatin.

June 15, 2015

The team of Bernardo Reina-San-Martin at IGBMC revealed new control mechanisms operating during antibody diversification. They have shown that the DNA repair factor Parp3 plays a dual role during immunoglobulin class switch recombination (CSR).

Parp3 promotes the repair of physiological DNA double strand breaks inflicted at the immunoglobulin heavy chain (IgH) locus and it protects the locus against sustained DNA damage.

This work provides novel insight in the mechanisms underlying the efficient generation of protective antibodies and the maintenance of genomic stability.


These results are published in Plos Genetics May 22nd 2015.


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The fine structure of the human ribosome unveiled!

© IGBMC


Example of 3D elements revealed in the atomic structure of the full human ribosome (80S). The high resolution (in the Angstrom range, Å, i.e. 0.1 nanometer) allows discrimination between elements interacting or not.

April 22, 2015

The team of Bruno Klaholz, at IGBMC reveals the atomic 3D structure of the full human ribosome and its fine interactions, notably between RNAs and proteins, the human’s molecular machinery catalyzing protein biosynthesis.

These outstanding findings provide unprecedented insights into the structure and the dynamics of the full human ribosome and pave the way for new major explorations like analyzing antibiotic side-effects or, in the long term, the treatment of diseases related to ribosome’s dysfunction and deregulated protein synthesis, including cancer.


These results are published April 22th, 2015 in Nature.

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