Emmanuelle Braud

Dr. Emmanuelle Braud

Université Paris Descartes, Paris, France
orcid

Research Focus & Metrics

Academic Career Length

18Years (2009-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

View All Publications
9 April 2009 in ChemMedChem
Verified
Journal Article
Closed access
PDF file
SKStéphanie Kolb
Stéphanie Kolb
OMOdile Mondésert
Odile Mondésert
MGMary‐Lorène Goddard
Mary‐Lorène Goddard
DJDenis Jullien
Denis Jullien
Bruno VilloutreixBruno Villoutreix
Bruno Villoutreix
EBEmmanuelle Braud
Emmanuelle Braud

21 February 2018 in Chemistry – A European Journal
Verified
Journal Article
Closed access
PDF file
FNFlora Ngadjeua
Flora Ngadjeua
EBEmmanuelle Braud
Emmanuelle Braud
SSSaidbakhrom Saidjalolov
Saidbakhrom Saidjalolov
LILaura Iannazzo
Laura Iannazzo
DSDirk Schnappinger
Dirk Schnappinger
MAMichel Arthur
Michel Arthur

16 August 2018 in European Journal of Organic Chemistry
Verified
Journal Article
Closed access
PDF file
CAColette Atdjian
Colette Atdjian
LILaura Iannazzo
Laura Iannazzo
EBEmmanuelle Braud
Emmanuelle Braud
MEMélanie Ethève-Quelquejeu
Mélanie Ethève-Quelquejeu

16 July 2020 in Molecules
Verified
Journal Article
Open access
PDF file
CAColette Atdjian
Colette Atdjian
CDCOELHO Dylan
COELHO Dylan
LILaura Iannazzo
Laura Iannazzo
MEMélanie Ethève-Quelquejeu
Mélanie Ethève-Quelquejeu
EBEmmanuelle Braud
Emmanuelle Braud
More than 150 RNA chemical modifications have been identified to date. Among them, methylation of adenosine at the N-6 position (m6A) is crucial for RNA metabolism, stability and other important biological events. In particular, this is the most abundant mark found in mRNA in mammalian cells. The presence of a methyl group at the N-1 position of adenosine (m1A) is mostly found in ncRNA and mRNA and is mainly responsible for stability and translation fidelity. These modifications are installed by m6A and m1A RNA methyltransferases (RNA MTases), respectively. In human, deregulation of m6A RNA MTases activity is associated with many diseases including cancer. To date, the molecular mechanism involved in the methyl transfer, in particular substrate recognition, remains unclear. We report the synthesis of new SAM-adenosine conjugates containing a triazole linker branched at the N-1 or N-6 position of adenosine. Our methodology does not require protecting groups for the functionalization of adenosine at these two positions. The molecules described here were designed as potential bisubstrate analogues for m6A and m1A RNA MTases that could be further employed for structural studies. This is the first report of compounds mimicking the transition state of the methylation reaction catalyzed by m1A RNA MTases.

5 January 2017 in Proteins: Structure, Function, and Bioinformatics
Verified
Journal Article
Closed access
PDF file
MSManal Sarkis
Manal Sarkis
Maria A. MitevaMaria A. Miteva
Maria A. Miteva
MLMaria Chiara Dasso Lang
Maria Chiara Dasso Lang
MJMaryse Jaouen
Maryse Jaouen
MSMarie‐Agnès Sari
Marie‐Agnès Sari
EBEmmanuelle Braud
Emmanuelle Braud

18 December 2020 in Chemistry – A European Journal
Verified
Journal Article
Closed access
PDF file
SSSaidbakhrom Saidjalolov
Saidbakhrom Saidjalolov
ZEZainab Edoo
Zainab Edoo
MFMatthieu Fonvielle
Matthieu Fonvielle
LMLouis Mayer
Louis Mayer
LILaura Iannazzo
Laura Iannazzo
EBEmmanuelle Braud
Emmanuelle Braud