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Functional architecture of the retromer cargo-recognition complex

• Aitor Hierro, Adriana L. Rojas, +6 authors James H. Hurley
• Nature
• 2007

The retromer complex is required for the sorting of acid hydrolases to lysosomes, transcytosis of the polymeric immunoglobulin receptor, Wnt gradient formation, iron transporter recycling and… (More)

Charged multivesicular body protein 2B (CHMP2B) of the endosomal sorting complex required for transport-III (ESCRT-III) polymerizes into helical structures deforming the plasma membrane.

• Gilles Bodon, Romain Chassefeyre, +10 authors Rémy Sadoul
• The Journal of biological chemistry
• 2011

The endosomal sorting complexes required for transport (ESCRT-0-III) allow membrane budding and fission away from the cytosol. This machinery is used during multivesicular endosome biogenesis,… (More)

ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding.

• Grégory Effantin, Aurélien Dordor, +4 authors Winfried Weissenhorn
• Cellular microbiology
• 2013

The endosomal sorting complex required for transport-III (ESCRT-III) proteins are essential for budding of some enveloped viruses, for the formation of intraluminal vesicles at the endosome and for… (More)

Near-atomic cryo-EM structure of the helical measles virus nucleocapsid

• Irina Gutsche, Ambroise Desfosses, +5 authors Guy Schoehn
• Science
• 2015

Measles is a highly contagious human disease. We used cryo–electron microscopy and single particle–based helical image analysis to determine the structure of the helical nucleocapsid formed by the… (More)

Local and global mobility in the ClpA AAA+ chaperone detected by cryo-electron microscopy: functional connotations.

• Grégory Effantin, Takashi Ishikawa, Gian Marco De Donatis, Michael R. Maurizi, Alasdair C. Steven
• Structure
• 2010

The ClpA chaperone combines with the ClpP peptidase to perform targeted proteolysis in the bacterial cytoplasm. ClpA monomer has an N-terminal substrate-binding domain and two AAA+ ATPase domains (D1… (More)

Bacteriophage T5 structure reveals similarities with HK97 and T4 suggesting evolutionary relationships.

• Grégory Effantin, Pascale Boulanger, Emmanuelle Neumann, Lucienne Letellier, James F Conway
• Journal of molecular biology
• 2006

Evolutionary relationships between viruses may be obscure by protein sequence but unmasked by structure. Analysis of bacteriophage T5 by cryo-electron microscopy and protein sequence analysis reveals… (More)

Electron microscopic evidence in support of alpha-solenoid models of proteasomal subunits Rpn1 and Rpn2.

• Grégory Effantin, Rina Rosenzweig, Michael H. Glickman, Alasdair C. Steven
• Journal of molecular biology
• 2009

Rpn1 (109 kDa) and Rpn2 (104 kDa) are components of the 19S regulatory complex of the proteasome. The central portions of both proteins are predicted to have toroidal alpha-solenoid folds composed of… (More)

Intravacuolar Membranes Regulate CD8 T Cell Recognition of Membrane-Bound Toxoplasma gondii Protective Antigen.

• Jodie Lopez, Amina Bittame, +15 authors Nicolas Blanchard
• Cell reports
• 2015

Apicomplexa parasites such as Toxoplasma gondii target effectors to and across the boundary of their parasitophorous vacuole (PV), resulting in host cell subversion and potential presentation by MHC… (More)

Poliovirus 2C protein forms homo-oligomeric structures required for ATPase activity.

• Peter X. Adams, Eaazhisai Kandiah, Grégory Effantin, Alasdair C. Steven, Ellie Ehrenfeld
• The Journal of biological chemistry
• 2009

The poliovirus protein 2C plays an essential role in viral RNA replication, although its precise biochemical activities or structural requirements have not been elucidated. The protein has several… (More)

Binding of the ClpA unfoldase opens the axial gate of ClpP peptidase.

• Grégory Effantin, Michael R. Maurizi, Alasdair C. Steven
• The Journal of biological chemistry
• 2010

ClpP is a serine protease whose active sites are sequestered in a cavity enclosed between two heptameric rings of subunits. The ability of ClpP to process folded protein substrates depends on its… (More)

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