Full name : Botti Simone
First name : Simone
Mail : Weizmann Institute of Science, Dept. Neurobiology, 76100 Rehovot
Zip Code :
City :
Country : Israel
Email : csbotti@wicc.weizmann.ac.il
Phone : 972 89343759
Fax : 972 89344159
Website :
Directory :
Comment
Title : Overexpression of the extracellular and cytoplasmic domains of the Drosophila adhesion protein, gliotactin. - |
Author(s) : Rydberg EH , Macion R , Zeev-Ben-Mordehai T , Solomon A , Rees DM , Toker L , Botti SA , Auld VJ , Silman I , Sussman JL |
Ref : Cholinergic Mechanisms, CRC Press :687 , 2004 |
PubMedID: |
Title : Poster (31) Natively unstructured proteins: a case study of cholinesterase-like adhesion molecules (clams) - |
Author(s) : Sussman JL , Zeev-Ben-Mordehai T , Rydberg EH , Solomon A , Toker L , Botti SA , Auld VJ , Silman I |
Ref : In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects , (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina :337 , 2004 |
PubMedID: |
Title : The complex of a bivalent derivative of galanthamine with torpedo acetylcholinesterase displays drastic deformation of the active-site gorge: implications for structure-based drug design - Greenblatt_2004_J.Am.Chem.Soc_126_15405 |
Author(s) : Greenblatt HM , Guillou C , Guenard D , Argaman A , Botti SA , Badet B , Thal C , Silman I , Sussman JL |
Ref : Journal of the American Chemical Society , 126 :15405 , 2004 |
Abstract : |
PubMedSearch : Greenblatt_2004_J.Am.Chem.Soc_126_15405 |
PubMedID: 15563167 |
Gene_locus related to this paper: torca-ACHE |
Title : The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded - Zeev-Ben-Mordehai_2003_Proteins_53_758 |
Author(s) : Zeev-Ben-Mordehai T , Rydberg EH , Solomon A , Toker L , Auld VJ , Silman I , Botti SA , Sussman JL |
Ref : Proteins , 53 :758 , 2003 |
Abstract : |
PubMedSearch : Zeev-Ben-Mordehai_2003_Proteins_53_758 |
PubMedID: 14579366 |
Title : A modular treatment of molecular traffic through the active site of cholinesterase - Botti_1999_Biophys.J_77_2430 |
Author(s) : Botti SA , Felder CE , Lifson S , Sussman JL , Silman I |
Ref : Biophysical Journal , 77 :2430 , 1999 |
Abstract : |
PubMedSearch : Botti_1999_Biophys.J_77_2430 |
PubMedID: 10545346 |
Title : The Conjunction of a Conserved Electrostatic Motif and a Common Cholinesterase Fold Defines a Class of Adhesion Proteins - |
Author(s) : Botti SA , Felder CE , Sussman JL , Silman I |
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :448 , 1998 |
PubMedID: |
Title : Electrotactins: a class of adhesion proteins with conserved electrostatic and structural motifs - Botti_1998_Protein.Eng_11_415 |
Author(s) : Botti SA , Felder CE , Sussman JL , Silman I |
Ref : Protein Engineering , 11 :415 , 1998 |
Abstract : |
PubMedSearch : Botti_1998_Protein.Eng_11_415 |
PubMedID: 9725619 |
Title : Electrostatic homology modelling of a set of ChE-like neural adhesion proteins identifies a shared annular motif with ChEs. Structural implications for a cell-recognition role of ChEs - |
Author(s) : Botti SA , Felder CE , Sussman JL , Silman I |
Ref : Journal de Physiologie (Paris) , 92 :414 , 1998 |
PubMedID: |
Title : An Integrated Model for the Molecular Traffic through the Active Site of Cholinesterases - |
Author(s) : Botti SA , Felder CE , Lifson S , Sussman JL , Silman I |
Ref : In: Structure and Function of Cholinesterases and Related Proteins - Proceedings of Sixth International Meeting on Cholinesterases , (Doctor, B.P., Taylor, P., Quinn, D.M., Rotundo, R.L., Gentry, M.K. Eds) Plenum Publishing Corp. :227 , 1998 |
PubMedID: |
Title : External and internal electrostatic potentials of cholinesterase models - Felder_1997_J.Mol.Graph.Model_15_318 |
Author(s) : Felder CE , Botti SA , Lifson S , Silman I , Sussman JL |
Ref : J Mol Graph Model , 15 :318 , 1997 |
Abstract : |
PubMedSearch : Felder_1997_J.Mol.Graph.Model_15_318 |
PubMedID: 9640563 |