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Dr. Ricardo Miguel Biondi

rbiondi@ibioba-mpsp-conicet.gov.ar

Biólogo, doctorado en la Universidad de Buenos Aires, post-doctorado en el Instituto Pasteur (Paris, Francia) y Universidad de Dundee (Escocia, UK); jefe de grupo Research Group PhosphoSites desde 2004 en la Universidad de Saarland y Universidad de Frankfurt (Alemania). Ha obtenido distinciones en Alemania tanto en el área de ciencias como también en desarrollos aplicados y competencias de planes de trabajo para empresas de biotecnología spin-off. Desde 2011 es parte del comité de editores de la revista Journal of Biological Chemistry Desde 2016, es investigador principal de CONICET, liderando un grupo de investigación en IBioBA-MPSP.

Publicaciones destacadas


Schulze JO, Saladino G, Busschots K, Neimanis S, Süß E, Odadzic D, Zeuzem S, Hindie V, Herbrand AK, Lisa MN, Alzari PM, Gervasio FL, Biondi RM.
Bidirectional Allosteric Communication between the ATP-Binding Site and the Regulatory PIF Pocket in PDK1 Protein Kinase
Cell Chemical Biology 23, 1193–1205 (2016)


Kroon E, Schulze JO, Süß E, Camacho CJ, Biondi RM, Dömling A.
Discovery of a Potent Allosteric Kinase Modulator by Combining Computational and Synthetic Methods
Angew Chem Int Ed Engl. 16; 54:13933-6. (2015)


Zhang H, Neimanis S, Lopez-Garcia LA, Arencibia JM, Amon S, Stroba A, Zeuzem S, Proschak E, Stark H, Bauer AF, Busschots K, Jørgensen TJ, Engel M, Schulze JO, Biondi RM.
Molecular Mechanism of Regulation of the Atypical Protein Kinase C by N-terminal Domains and an Allosteric Small Compound
Chem. Biol. 21:754-65 (2014)


Busschots K, Lopez-Garcia LA, Lammi C, Stroba A, Zeuzem S, Piiper A, Alzari PM, Neimanis S, Arencibia JM, Engel M, Schulze JO, Biondi RM
Substrate-Selective Inhibition of Protein Kinase PDK1 by Small Compounds that Bind to the PIF-Pocket Allosteric Docking Site
Chem. Biol. 19:1152-63 (2012)


Lopez-Garcia LA, Schulze JO, Fröhner W, Zhang H, Süß E, Weber N, Navratil J, Amon S, Hindie V, Zeuzem S, Jørgensen TJD, Alzari PM, Neimanis S, Engel M, Biondi RM.
Allosteric regulation of protein kinase PKCz by the N-terminal C1 domain and small compounds to the PIF-pocket
Chem. Biol. 18:1463-73 (2011)


Hindie, Stroba, Zhang, Lopez-Garcia, Idrissova, Zeuzem, Hirschberg, Schaeffer, Jorgensen, Engel, Alzari, Biondi RM.
High resolution complex structure and allosteric effects of low molecular weight activators on the protein kinase PDK1
Nat. Chem. Biol. 5, 758-64. (2009)


Engel M, Hindie V, Lopez-Garcia LA, Stroba A, Schaeffer F, Adrian I, Imig J, Idrissova L, Nastainczyk W, Zeuzem S, Alzari PM, Hartmann RW, Piiper A, Biondi RM.
Allosteric activation of protein kinase PDK1 with low molecular weight compounds
EMBO J. 25:5469-80. (2006)


Biondi RM, Komander D, Thomas CC, Lizcano JM, Deak M, Alessi DR, van Aalten DMF.
High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site
EMBO J. 21, 4219-4228. (2002)


Frodin M, Antal TL, Dummler BA, Jensen CJ, Deak M, Gammeltoft S, Biondi RM.
AGC kinases and PDK1 contain a phospho-Ser/Thr binding pocket that mediates activation by hydrophobic motif phosphorylation
EMBO J. 21, 5396-5407. (2002)


Frame SM, Cohen P, Biondi RM.
A common phosphate binding site explains the substrate specificity of GSK3 and its inactivation by phosphorylation
Mol. Cell. 7, 1321-1327. (2001)


Biondi RM, Kieloch, A, Currie R, Deak M, Alessi DR.
The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK but not PKB
EMBO J. 20, 4380-4390. (2001)


Biondi RM, Cheung PCF, Casamayor A, Deak M, Currie RA, Alessi DR.
Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA
EMBO J. 19, 979-988. (2000)


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