Two distinct trimeric conformations of natively membrane-anchored full-length herpes simplex virus 1 glycoprotein B.
Zeev-Ben-Mordehai T. et al, (2016), Proc Natl Acad Sci U S A, 113, 4176 - 4181
Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling.
Zeev-Ben-Mordehai T. et al, (2015), Cell Rep, 13, 2645 - 2652
Structural Basis of Vesicle Formation at the Inner Nuclear Membrane.
Hagen C. et al, (2015), Cell, 163, 1692 - 1701
Extracellular vesicles: a platform for the structure determination of membrane proteins by Cryo-EM.
Zeev-Ben-Mordehai T. et al, (2014), Structure, 22, 1687 - 1692
The full-length cell-cell fusogen EFF-1 is monomeric and upright on the membrane.
Zeev-Ben-Mordehai T. et al, (2014), Nat Commun, 5
A cool hybrid approach to the herpesvirus 'life' cycle.
Zeev-Ben-Mordehai T. et al, (2014), Curr Opin Virol, 5, 42 - 49
The Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein Interaction
Maurer UE. et al, (2013), Structure, 21, 1396 - 1405
Conserved eukaryotic fusogens can fuse viral envelopes to cells.
Avinoam O. et al, (2011), Science, 332, 589 - 592
The quaternary structure of amalgam, a Drosophila neuronal adhesion protein, explains its dual adhesion properties.
Zeev-Ben-Mordehai T. et al, (2009), Biophys J, 97, 2316 - 2326
Amalgam, an axon guidance Drosophila adhesion protein belonging to the immunoglobulin superfamily: over-expression, purification and biophysical characterization.
Zeev-Ben-Mordehai T. et al, (2009), Protein Expr Purif, 63, 147 - 157
Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3.
Paz A. et al, (2008), Biophys J, 95, 1928 - 1944
Eukaryotic expression: developments for structural proteomics
Aricescu AR. et al, (2006), Acta Crystallographica Section D Biological Crystallography, 62, 1114 - 1124
FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded.
Prilusky J. et al, (2005), Bioinformatics, 21, 3435 - 3438
Transient apical polarization of Gliotactin and Coracle is required for parallel alignment of wing hairs in Drosophila.
Venema DR. et al, (2004), Dev Biol, 275, 301 - 314
The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded.
Zeev-Ben-Mordehai T. et al, (2003), Proteins, 53, 758 - 767
Acetylcholinesterase in motion: visualizing conformational changes in crystal structures by a morphing procedure.
Zeev-Ben-Mordehai T. et al, (2003), Biopolymers, 68, 395 - 406