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Expertises

 
 

Veuillez visiter cette page régulièrement pour vous informer des dernières découvertes dans le domaine des bionanomachines! Des images et vidéos provenant des laboratoires des membres du CTPB seront présentées ici.

 

Domaine de la protéine mutée dans le syndrome Johanson-Blizzard. (Edna Matta-Camacho, Guennadi Kozlov, Flora F Li and Kalle Gehring. Structural basis of substrate recognition and specificity in the N-end rule pathway. 2010. Nature Structural & Molecular Biology 117(10), 1182-1187)

 

Auto-assemblage de l’hexagone d’ADN. (Faisal Aldaye and Hanadi F. Sleiman. Sequential Self-Assembly of a DNA Hexagon as a Template for the Organization of Gold Nanoparticles. Angew. Chem. Int. Ed. 2006. 45, 2204-2209.)

 

Libération sélective de cargo de nanotubes d’ADN. (Peggy Lo, Pierre Karam, Faisal Aldaye, Graham Hamblin, Gonzalo Cosa and Hanadi F. Sleiman. Loading and Selective Release of Cargo in DNA Nanotubes with Longitudinal Variation. 2010. Nature Chemistry 2, 319-328)

 

Assemblage d’une cage de métal-acide nucléique. (Hua Yang, Christopher McLaughlin, Graham Hamblin, Faisal Aldaye, Andrzej Rys, and Hanadi F. Sleiman. Metal Nucleic-Acid Cages. Nature Chemistry 2009. 1, 390-396)



 

Le <<AutoLoader>> du Titan Krios permet le chargement automatique et l’analyse de 12 échantillons congelés de complexes protéiques purifiés.

 

L’équipe de la plateforme de Spectrométrie par Résonance Magnétique Nucléaire.

PUBLICATIONS

1. Abbas YM, Pichlmair A, Górna MW, Superti-Furga G and Nagar B (2013) Structural basis for viral 5´-PPP-RNA recognition by human IFIT proteins. Nature 494, 60-64. McGill Best paper award from Medstar (January – April 2013 period) $500

2. Ishiyama N, Tanaka N, Abe K, Yang YJ, Abbas YM, Umitsu M, Nagar B, Bueler SA, Rubinstein JL, Takeichi M and Ikura M (2013) An autoinhibited structure of α-catenin and its implications for vinculin recruitment to adherens junctions. JBC 288, 15913-15925.

3. Trempe JF, Sauvé V, Grenier K, Seirafi M, Tang MY, Ménade M, Al-Abdul-Wahid S, Krett J, Wong K, Kozlov G, Nagar B, Fon EA and Gehring K (2013) Structure of Parkin reveals mechanisms for ubiquitin ligase activation. Science 340, 1451-1455.

4. Rodina A*, Patel PD*, Kang Y*, Patel Y*, Baaklini I, Wong MJH, Taldone T, Yan P, Yang C, Maharaj R, Gozman A, Patel MR, Patel HJ, Erdjument-Bromage H, Talele TT, Young JC and Chiosis G (2013) Identification of an allosteric pocket on the human Hsp70 reveals a novel mode of inhibition of this therapeutically important protein. Cell Chemistry & Biology.20: 1469–1480 * Co-first author.

5. Berard D, Michaud M, Mahshid S, Ahamed MJ, McFaul CMJ, Leith JS, Bérubé P, Sladek R, Reisner W and Leslie SR (2014) Convex lens-induced nanoscale templating. PNAS 1321089111.

6. Serpell CJ, Edwardson T, Chidchob P, Carneiro K and Sleiman H (2014) Precision polymers and 3D DNA nanostructures: emergent assemblies from new parameter space. JACS 136, 15767 (selected as JACS Spotlight article).

7. Kathiresan M, Martins D and English AM (2014) Respiration triggers heme transfer from cytochrome c peroxidase to catalase in yeast mitochondria. PNAS 111, (49) 17468-17473.

8. Hariri AA, Hamblin GD, Gidi Y, Sleiman HF and Cosa G (2015) Stepwise growth of surface-grafted DNA nanotubes visualized at the single-molecule level. Nature Chemistry. 7, 295–300. (Journal Cover).

9. Sauvé V, Lilov A, Seirafi M, Vranas M, Rasool S, Kozlov G, Sprules T, Wang J, Trempe JF, Gehring K. (2015) A Ubl/ubiquitin switch in the activation of Parkin. EMBO J. 34 (20) 2492-505.

10. Glembockyte V, Lincoln R and Cosa G. (2015) Photoprotection mediated by Ni2+ for extended single-molecule imaging: old tricks for new techniques. JACS 137 (3) 1116–1122.

11. Hamblin GD, Rahbani JF and Sleiman HF (2015) Temporal control of DNA sequence patterns: designer DNA templates for scaffolds and nanostructures. Nature Communications. doi:10.1038/ncomms8065.

12. Seirafi M, Kozlov G and Gehring K (2015) Parkin structure and function. FEBS Journal V 282, (11) 2076–2088.

13. Wong K, Kozlov G, Zhang Y and Gehring K (2015) Structure of the Legionella effector, lpg1496, suggests a role in nucleotide metabolism. JBC 9; 29 (41):24727-37.