Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Lorenzo Zampighi"'
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e23753 (2011)
Lens transparency depends on the accumulation of massive quantities (600-800 mg/ml) of twelve primary crystallines and two truncated crystallines in highly elongated "fiber" cells. Despite numerous studies, major unanswered questions are how this het
Externí odkaz:
https://doaj.org/article/586ccb2d10ee42369dc297f36e45653d
Autor:
Lorenzo Zampighi, Guido A. Zampighi, Eleonora Salvi, Francesca Cantele, N. Fain, Salvatore Lanzavecchia, Gaia Pigino
Publikováno v:
Journal of Structural Biology. 161:287-297
We are presenting a program for interactive segmentation of tomographic maps, based on objective criteria so as to yield reproducible results. The strategy starts with the automatic segmentation of the entire volume with the watershed algorithm in 3D
Publikováno v:
Journal of Structural Biology. 146:368-380
An important step in determining the three-dimensional structure of single macromolecules is to bring common features in the images into register through alignment and classification. Here, we took advantage of the striking computational properties o
Autor:
Lorenzo Zampighi, Guido A. Zampighi, Michael L. Woodruff, Cataldo Schietroma, Ernest M. Wright, Nicholas C. Brecha
Publikováno v:
PLoS ONE
PloS one, vol 6, iss 3
PLoS ONE, Vol 6, Iss 3, p e16944 (2011)
PloS one, vol 6, iss 3
PLoS ONE, Vol 6, Iss 3, p e16944 (2011)
To characterize the sites of synaptic vesicle fusion in photoreceptors, we evaluated the three-dimensional structure of rod spherules from mice exposed to steady bright light or dark-adapted for periods ranging from 3 to 180 minutes using conical ele
Publikováno v:
Biophysical Journal. 100(3)
Despite advances in molecular biology and genetics, the location of thousand of proteins in cells remains undetermined. The principal problems are their small dimensions and their capacity to form large assemblies by associating either with themselve
Studies using conventional electron microscopy describe the cytoplasm of lens fiber cells as having essentially an amorphous structure. We hypothesized that significant structural detail might have been lost as a result of projecting the entire thick
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ff3f0b9f99457625f2255014895d082
https://europepmc.org/articles/PMC2825116/
https://europepmc.org/articles/PMC2825116/
Conical Electron Tomography of a Chemical Synapse: Polyhedral Cages Dock Vesicles to the Active Zone
Autor:
Lorenzo Zampighi, Guido A. Zampighi, Ernest M. Wright, Francesca Cantele, Salvatore Lanzavecchia, N. Fain
In this study, we tested the hypothesis that the structure of the active zone of chemical synapses has remained uncertain because of limitations of conventional electron microscopy. To resolve these limitations, we reconstructed chemical synapses of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27390cd7b3647177c09798ebd92d0575
http://hdl.handle.net/2434/60823
http://hdl.handle.net/2434/60823
Autor:
Guido A. Zampighi, Lorenzo Zampighi, Francesca Cantele, Michael Radermacher, Salvatore Lanzavecchia
Publikováno v:
Journal of structural biology. 158(1)
A critical problem in electron tomography is the deformation of the specimen due to radiation, or "shrinkage," which interferes with image alignment and thereby limits resolution. Here, we describe a general strategy for refining preliminary reconstr
Autor:
Lorenzo Zampighi, N. Fain, Guido A. Zampighi, Francesca Cantele, Salvatore Lanzavecchia, Ernest M. Wright
Publikováno v:
Journal of structural biology. 151(3)
We have used conical electron tomography in order to reconstruct neuronal organelles in thin sections of plastic embedded rat somato-sensory cortical tissue. The conical tilt series were collected at a 55 degrees tilt and at 5 degrees rotations, alig
Autor:
Francesca Cantele, Lorenzo Zampighi, Pier Luigi Bellon, Ernest M. Wright, Salvatore Lanzavecchia, Guido A. Zampighi, Michael Kreman
Publikováno v:
Journal of structural biology. 149(1)
We have used conical tomography to study the structure of integral proteins in their phospholipid bilayer environments. Complete conical series were collected from replicas of the water channel aquaporin-0 (AQP0), a 6.6 nm side tetramer with a molecu