Ludo Renault
Head of Facility NeCEN
- Naam
- Dr. L.L.R. Renault
- Telefoon
- +31 71 527 1420
- l.renault@biology.leidenuniv.nl
- ORCID iD
- 0000-0001-6464-8808
Ludo Renault is hoofd van het Netherlands Centre of Electron Nanoscopy (NeCEN) dat deel uitmaakt van het Instituut voor Biologie (IBL) van de Faculteit der Wiskunde en Natuurwetenschappen.
Meer informatie over Ludo Renault
Nieuws
-
Gevaarlijke microben in lager veiligheidslevel lab? Met een nieuwe techniek zou het kunnen -
Hoe NeCEN de farmaceut Janssen hielp om een coronavaccin te ontwikkelen -
Tien miljoen euro om nieuwe technologieën beschikbaar te maken voor iedereen -
Life Sciences Café op bezoek bij NeCEN -
NeCEN genoemd als topfaciliteit voor elektronenmicroscopie -
Samen leren over elektronenmicroscopie -
Subsidie van 17 miljoen voor ontwikkeling elektronenmicroscopie in Nederland
Teamleden
Voor meer informatie, zie Engelstalige pagina.
Head of Facility NeCEN
- Wiskunde en Natuurwetenschappen
- NECEN
- Depelteau J.S., Renault L.L.R., Althof N., Cassidy C.K., Mendonca L.M., Jensen G.J., Resch G.P. & Briegel A. (2022), UVC inactivation of pathogenic samples suitable for cryo-EM analysis, Communications Biology 5: 29.
- Juraszek J., Rutten L., Blokland S., Bouchier P., Voorzaat R., Ritschel T., Bakkers M.J.G., Renault L.L.R. & Langedijk J.P.M. (2021), Stabilizing the closed SARS-CoV-2 spike trimer, Nature Communications 12: 244.
- Sun Z., Diebolder C.A., Renault L.L.R. & Groot H.J.M. de (2019), A semisynthetic peptide-metalloporphyrin responsive matrix for artificial photosynthesis, ChemPhotoChem 3(8): 630-635.
- Wilson M.D., Renault L.L.R., Maskell D.P., Ghoneim M., Pye V.E., Nans A., Ruela D.S., Cherepanov P. & Costa A. (2019), Retroviral integration into nucleosomes through DNA looping and sliding along the histone octamer, Nature Communications 10: 4189.
- Jaciuk M., Swuec P., Gaur V., Kasprzak J.M., Renault L., Dobrychlop M., Nirwal S., Bujnicki J.M., Costa A. & Nowotny M. (2019), A combined structural and biochemical approach reveals translocation and stalling of UvrB on the DNA lesion as a mechanism of damage verification in bacterial nucleotide excision repair, DNA Repair 85: 102746.
- Cerofolini L., Fragai M., Ravera E., Diebolder C.A., Renault L.L.R. & Calderone V. (2019), Integrative Approaches in Structural Biology: A More Complete Picture from the Combination of Individual Techniques, Biomolecules 9(8): 370.
- Alewijnse B., Ashton A.W., Chambers M.G., Chen S., Cheng A., Ebrahim M., Eng E.T., Hagen W.J.H., Koster A.J., López C.S., Lukoyanova N., Ortega J., Renault L.L.R., Reyntjens S., Rice W.J., Scapin G., Schrijver R., Siebert A., Stagg S.M., Grum-Tokars V., Wright E.R., Wu S., Yu Z., Zhou Z.H., Carragher B. & Potter C.S. (2017), Best practices for managing large CryoEM facilities, Journal of Structural Biology 199(3): 225-236.
- Frigola J., He J., Kinkelin K., Pye V.E., Renault L.L.R., Douglas M.E., Remus D., Cherepanov P., Costa A. & Diffley J.F.X. (2017), Cdt1 stabilizes an open MCM ring for helicase loading, Nature Communications 8: 15720.
- Zhou J.C., Janska A., Goswami P., Renault L.L.R., Abid Ali F., Kotecha A., Diffley J.F.X. & Costa A. (2017), CMG-Pol epsilon dynamics suggests a mechanism for the establishment of leading-strand synthesis in the eukaryotic replisome, Proceedings of the National Academy of Sciences 114(16): 4141-4146.
- Swuec P., Renault L.L.R., Borg A., Shah F., Murphy V.J., Twest S. van, Snijders A.P., Deans A.J. & Costa A. (2017), The FA Core Complex Contains a Homo-dimeric Catalytic Module for the Symmetric Mono-ubiquitination of FANCI-FANCD2, Cell Reports 18(3): 611-623.
- Abid Ali F., Renault L.L.R., Gannon J., Gahlon H.L., Kotecha A., Zhou J.C., Rueda D. & Costa A. (2016), Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate, Nature Communications 7: 10708.
- Vázquez-Fernandez E., Vos M.R., Afanasyev P., Cebey L., Sevillano A.M., Vidal E., Rosa I., Renault L.L.R., Ramos A., Peters P.J., Fernández J.J., Heel M. van, Young H.S., Requena J.R. & Wille H. (2016), The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy, PLoS Pathogens 12(9): 1005835.
- Bourne Y., Renault L.L.R. & Marchot P. (2015), Crystal structure of snake venom acetylcholinesterase in complex with inhibitory antibody fragment Fab410 bound at the peripheral site: evidence for open and closed states of a back door channel, Journal of Biological Chemistry 290(3): 1522-1535.
- Maskell D.P., Renault L.L.R., Serrao E., Lesbats P., Matadeen R., Hare S., Lindemann D., Engelman A.N., Costa A. & Cherepanov P. (2015), Structural basis for retroviral integration into nucleosomes, Nature 523(7560): 366-369.
- Pike A.C., Gomathinayagam S., Swuec P., Berti M., Zhang Y., Schnecke C., Marino F., Delft F. von der, Renault L.L.R., Costa A., Gileadi O. & Vindigni A. (2015), Human RECQ1 helicase-driven DNA unwinding, annealing, and branch migration: insights from DNA complex structures, Proceedings of the National Academy of Sciences 112(14): 4286-4291.
- Costa A., Renault L.L.R., Swuec P., Petojevic T., Pesavento J.J., Ilves I., MacLellan-Gibson K., Fleck R.A., Botchan M.R. & Berger J.M. (2014), DNA binding polarity, dimerization, and ATPase ring remodeling in the CMG helicase of the eukaryotic replisome, eLife 3: e03273.
- Simon A.C., Zhou J.C., Perera R.L., Deursen F. van, Evrin C., Ivanova M.E., Kilkenny M.L., Renault L.L.R., Kjaer S., Matak-Vinković D., Labib K., Costa A. & Pellegrini L. (2014), A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome, Nature 513(7504): 293-297.
- Bourne Y., Renault L.L.R., Essono S., Mondielli G., Lamourette P., Boquet D., Grassi J. & Marchot P. (2013), Molecular characterization of monoclonal antibodies that inhibit acetylcholinesterase by targeting the peripheral site and backdoor region, PLoS ONE 8(10): e77226.
- Glaves J.P., Gorski P.A., Alier K., Ma L., Renault L.L.R., Primeau J.O., Jhamandas J.H. & Young H.S. (2013), Distinct morphological and electrophysiological properties of an elk prion peptide, Peptides 40: 49-56.
- Cortez L.M., Kumar J., Renault L.L.R., Young H.S. & Sim V.L. (2013), Mouse prion protein polymorphism Phe-108/Val-189 affects the kinetics of fibril formation and the response to seeding: evidence for a two-step nucleation polymerization mechanism, Journal of Biological Chemistry 288(7): 4772-4781.
- Liu J., Renault L.L.R., Veaute X., Fabre F., Stahlberg H. & Heyer W.D. (2011), Rad51 paralogues Rad55-Rad57 balance the antirecombinase Srs2 in Rad51 filament formation, Nature 479(7372): 245-248.
- Klammt C., Perrin M.H., Maslennikov I., Renault L.L.R., Krupa M., Kwiatkowski W., Stahlberg H., Vale W. & Choe S. (2011), Polymer-based cell-free expression of ligand-binding family B G-protein coupled receptors without detergents, Protein Science 20(6): 1030-1041.
- Zeng X., Gipson B., Zheng Z.Y., Renault L.L.R. & Stahlberg H. (2007), Automatic lattice determination for two-dimensional crystal images, Journal of Structural Biology 160(3): 353-361.
- Renault L.L.R., Chou H.T., Chiu P.L., Hill R.M., Zeng X., Gipson B., Zhang Z.Y., Cheng A., Unger V. & Stahlberg H. (2006), Milestones in electron crystallography, Journal of Computer-Aided Molecular Design 20(7-8): 519-527.
- Renault L.L.R., Negre V., Hotelier T., Cousin X., Marchot P. & Chatonnet A. (2005), New friendly tools for users of ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins, Chemico-Biological Interactions 157-158: 339-343.
- Bourne Y., Hasper A.A., Chahinian H., Renault L.L.R., Juin M., Graaff L.H. de & Marchot P. (2005), A. niger protein EstA, perhaps a new electrotactin, defines a new class of fungal esterases within the alpha/beta hydrolase fold superfamily, Chemico-Biological Interactions 157-158: 395-396.
- Renault L.L.R., Essono S., Juin M., Boquet D., Grassi J., Bourne Y. & Marchot P. (2005), Structural insights into AChE inhibition by monoclonal antibodies, Chemico-Biological Interactions 157-158: 397-400.
- Hotelier T., Renault L.L.R., Cousin X., Negre V., Marchot P. & Chatonnet A. (2004), ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins, Nucleic Acids Research 32(Database Issue): D145-D147.