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- Team D. Lévy. Functional and structural analysis of membrane proteins
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- concentration wave of E. coli bacteria in a microchannel
- Amphiphilic Poly(ethylene oxide)-block-poly(butadiene-graft-liquid crystal) Copolymers: Synthesis and Self-Assembly in Water
- Binding, reconstitution and 2D crystallization of membrane or soluble proteins onto functionalised lipid layer observed in situ
- collectively migrating epithelium biophys cover
- Fig 5. Non-conservation of network motifs
- Fig 4. Model of biomolecular networks under duplication-divergence evolution
- Fig 3. Whole genome duplications in evolution
- Fig 2. Novel nanostructures made of DsrA ncRNA of E.coli
- Fig 1. RNA synthetic biology
- Fig 1. RNA synthetic biology
- Fig 1. RNA synthetic biology
- Fig 4. Model of biomolecular networks under duplication-divergence evolution
- Fig 4. Model of biomolecular networks under duplication-divergence evolution
- Fig 5. Expansion of signaling networks by whole genome duplication
- Fig. 1 Motor oscillations
- Fig. 2 Tissue competition
- Fig. 2 Compétition entre tissus
- Fig. 1 Oscillations de moteurs moléculaires
- Expansion of signaling networks by whole genome duplication
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- Brigitte da Silva
- Giulia carzedda
- laurence turpin
- Agnes verin
- anne-christine brunet
- Aurelie
- Fahima
- John Manzi
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- rémy
- benoit
- Brigitte Da Silva
- Brigitte Da Silva
- Giulia Carzedda
- Laurence Turpin
- Agnès Vérin
- Anne-Christine Brunet
- Aurélie Di Cicco
- Fahima Faqir
- Jean-Hugues Codarbox
- Rémy Fert
- Benoît Lemaire
- Giulia Carzedda
- Optical tweezer and edge fluctuation setup
- Functional and structural analysis of BmrC/BmrD abacterial heterodimeric MDR transporter
- Functional and structural analysis of BmrC/BmrD bacterial heterodimeric MDR transporter
- John Manzi
- Structural changes in liquid crystal polymer vesicles induced by temperature variation and magnetic fields
- Biocompatible gold nanorods for cancer research
- Self-assembly of amphiphilic liquid crystal block copolymers containing a cholesteryl mesogen: Effects of block ratio and solven
- Mechanical measurements of biomimetic cortex
- Bleb mechanics
- Confined Actin Gel Mechanics
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- Smectic polymer micellar aggregates with temperature-controlled morphologies
- Smectic polymer micellar aggregates with temperature-controlled morphologies
- Smectic polymer micellar aggregates with temperature-controlled morphologies
- Smectic polymer micellar aggregates with temperature-controlled morphologies
- C. elegans sperm cell crawling on a substrate.
- Actin filled liposome
- Actin Beads and VASP
- C. elegans sperm cells transfected with fluorescent MSP
- Multilayered liposome observed by cryoEM
- electron microscopy images
- 2D crystals of BmrC/BmrD
- 2D crystals of BmrC/BmrD, a bacterial heterodimeric ABC transporter
- Multilayered liposome obserbed by cryoEM
- 2D crystals of Light Harversting Complex, LH2, from Rba. sphaeroides
- Single particle analysis of 300kDa LH1-RC-PufX core complex of Rbs. veldkampii
- Atomic model of LH1-RC-PuhX from Rba. sphaeroides
- Atomic Model of LH1-RC-PufX from Rba. sphaeroides
- Single particle analysis by cryoElectron Microscopy of a small non symemetrical membrane protein
- 2D crystals of Light Harversting Complex, LH2, from Rba. sphaeroides
- 3D reconstruction of LH1-RC-PufX, 280 Kda, at 12 A resolution
- 3D reconstruction of LH1-RC-PufX, 280 kDa, at 12 A resolution
- 2D crystals of Light Harversting Complex, LH2, from Rba. sphaeroides
- schematic model of the coupling between the non equivalent catalytic sites of ABC transporters
- schematic model of the coupling between the non equivalent catalytic sites of ABC transporters
- schematic model of the coupling between the equivalent catalytic sites of ABC transporters
- Tubular to planar membranes upon conformational changes of BmrA, a ABC transporter
- Orientation of the Shiga toxin B subunit toward the membrane
- Pores in lipid membrane
- Functionalyzed tubes made of cerebroside lipids
- Polymersomes
- Light sensitive Polymersomes
- Tubular to planar membrane transition mediated by transmembrane protein
- Biocompatible gold nanorods for cancer research
- visuel publication
- Liposome with actin cortex aspirated in a micropipet
- Actin filled liposomes form a cortex if polymerization is activated at the membrane
- Cell fragments show spontaneous osscilation
- Symmetry breaking of the actin gel around a bead
- C. elegans embryo during ventral closure
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- TEM of gold nanorod
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- Map Institut Curie, Circle Meeting 2012
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- Karen Brémond
- Karen Brémond
- Speed and orientation in a migrating monolayer.
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- MAgnetic Tweezers
- Bassereau-group-2012
- Map_BDD_Amphi_Curie
- TEM images of block copolymer self-assemblies
- simulations modele
- LH1-RC
- LH1-RC Rba. veldkampii
- LH2 from Rba. sphaeroides
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- Incorporation of membrane proteins in planar lipid bilayer
- 2D crystallization by the lipid layer
- Reconstitution of membrane proteins in GUVS
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- Film 1 - C. Sykes
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- Film 1 : Oscillations spontanées
- Film 2 - Martin
- Film 1 - Amblard
- Film 1 - Brochard
- Film 2 - Brochard
- Film 3 - Brochard
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- S2 RNA regulatory module
- A2 activated S2 RNA regulatory module
- Red Blood Cell Flickering
- E. coli collective migration
- 2D crystallization of proteins onto functionalyzed lipid layer
Partagez
FIG1
Capture and analysis of circulating tumour cells.
Upper panel: sketch of the technology we have developed for the capture and study of tumour cells. Arrays of columns containing magnetic particles with antibodies directed against the cells of interest are self-assembled under a magnetic field in a microfluidic channel. The sample (e.g. blood from a patient) is flown in the channel. The cells bearing the relevant surface antigens (red and blue) are captured, whereas negative cells (blue) are not. The captured cells can be stained with different biomarkers, observed and studied with high accuracy after their capture. The lower panel displays a real image of cancer cells from a lymphoma patient, with multiple immunostaining (green, yellow and red antibodies, and blue DNA marker), imaged by confocal microscopy in situ after capture.