Leandro F Estrozi | Centre National de la Recherche Scientifique / French National Centre for Scientific Research (original) (raw)
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Papers by Leandro F Estrozi
Journal of Structural Biology, 2008
Journal of Structural Biology, 2010
Electronics Letters, 1999
ABSTRACT The authors show how exact dilations can be used to obtain multiresolution skeletons and... more ABSTRACT The authors show how exact dilations can be used to obtain multiresolution skeletons and how a new multiresolution approach to shape representation can be achieved in terms of such skeletons. In addition to allowing the accurate reconstruction of multiresolution versions of the original binary shapes, the proposed approach is characterised by great simplicity and the important property that the shape borders are not shifted as the smoothing increases
Journal of Virology, 2008
Digital Signal Processing, 2003
PloS one, 2015
The vesivirus feline calicivirus (FCV) is a positive strand RNA virus encapsidated by an icosahed... more The vesivirus feline calicivirus (FCV) is a positive strand RNA virus encapsidated by an icosahedral T=3 shell formed by the viral VP1 protein. Upon its expression in the insect cell - baculovirus system in the context of vaccine development, two types of virus-like particles (VLPs) were formed, a majority built of 60 subunits (T=1) and a minority probably built of 180 subunits (T=3). The structure of the small particles was determined by x-ray crystallography at 0.8 nm resolution helped by cryo-electron microscopy in order to understand their formation. Cubic crystals belonged to space group P213. Their self-rotation function showed the presence of an octahedral pseudo-symmetry similar to the one described previously by Agerbandje and co-workers for human parvovirus VLPs. The crystal structure could be solved starting from the published VP1 structure in the context of the T=3 viral capsid. In contrast to viral capsids, where the capsomers are interlocked by the exchange of the N-te...
Structure, 2014
Secretins, the outer membrane components of several secretion systems in Gram-negative bacteria, ... more Secretins, the outer membrane components of several secretion systems in Gram-negative bacteria, assemble into channels that allow exoproteins to traverse the membrane. The membrane-inserted, multimeric regions of PscC, the Pseudomonas aeruginosa type III secretion system secretin, and PulD, the Klebsiella oxytoca type II secretion system secretin, were purified after cell-free synthesis and their structures analyzed by single particle cryoelectron microscopy. Both homomultimeric, barrel-like structures display a "cup and saucer" architecture. The "saucer" region of both secretins is composed of two distinct rings, with that of PulD being less segmented than that of PscC. Both secretins have a central chamber that is occluded by a plug linked to the chamber walls through hairpin-like structures. Comparisons with published structures from other bacterial systems reveal that secretins have regions of local structural flexibility, probably reflecting their evolved functions in protein secretion and needle assembly.
Lecture Notes in Computer Science, 2000
Nature Structural & Molecular Biology, 2011
Journal of Virology, 2008
Journal of Structural Biology, 2007
Biophysical Journal, 2013
Journal of Structural Biology, 2008
Journal of Structural Biology, 2010
Electronics Letters, 1999
ABSTRACT The authors show how exact dilations can be used to obtain multiresolution skeletons and... more ABSTRACT The authors show how exact dilations can be used to obtain multiresolution skeletons and how a new multiresolution approach to shape representation can be achieved in terms of such skeletons. In addition to allowing the accurate reconstruction of multiresolution versions of the original binary shapes, the proposed approach is characterised by great simplicity and the important property that the shape borders are not shifted as the smoothing increases
Journal of Virology, 2008
Digital Signal Processing, 2003
PloS one, 2015
The vesivirus feline calicivirus (FCV) is a positive strand RNA virus encapsidated by an icosahed... more The vesivirus feline calicivirus (FCV) is a positive strand RNA virus encapsidated by an icosahedral T=3 shell formed by the viral VP1 protein. Upon its expression in the insect cell - baculovirus system in the context of vaccine development, two types of virus-like particles (VLPs) were formed, a majority built of 60 subunits (T=1) and a minority probably built of 180 subunits (T=3). The structure of the small particles was determined by x-ray crystallography at 0.8 nm resolution helped by cryo-electron microscopy in order to understand their formation. Cubic crystals belonged to space group P213. Their self-rotation function showed the presence of an octahedral pseudo-symmetry similar to the one described previously by Agerbandje and co-workers for human parvovirus VLPs. The crystal structure could be solved starting from the published VP1 structure in the context of the T=3 viral capsid. In contrast to viral capsids, where the capsomers are interlocked by the exchange of the N-te...
Structure, 2014
Secretins, the outer membrane components of several secretion systems in Gram-negative bacteria, ... more Secretins, the outer membrane components of several secretion systems in Gram-negative bacteria, assemble into channels that allow exoproteins to traverse the membrane. The membrane-inserted, multimeric regions of PscC, the Pseudomonas aeruginosa type III secretion system secretin, and PulD, the Klebsiella oxytoca type II secretion system secretin, were purified after cell-free synthesis and their structures analyzed by single particle cryoelectron microscopy. Both homomultimeric, barrel-like structures display a "cup and saucer" architecture. The "saucer" region of both secretins is composed of two distinct rings, with that of PulD being less segmented than that of PscC. Both secretins have a central chamber that is occluded by a plug linked to the chamber walls through hairpin-like structures. Comparisons with published structures from other bacterial systems reveal that secretins have regions of local structural flexibility, probably reflecting their evolved functions in protein secretion and needle assembly.
Lecture Notes in Computer Science, 2000
Nature Structural & Molecular Biology, 2011
Journal of Virology, 2008
Journal of Structural Biology, 2007
Biophysical Journal, 2013