about
In situ structural analysis of the human nuclear pore complexStructure and properties of the esterase from non-LTR retrotransposons suggest a role for lipids in retrotranspositionTwo distinct trimeric conformations of natively membrane-anchored full-length herpes simplex virus 1 glycoprotein B.The diverse roles of the Nup93/Nic96 complex proteins - structural scaffolds of the nuclear pore complex with additional cellular functions.Nup153 Recruits the Nup107-160 Complex to the Inner Nuclear Membrane for Interphasic Nuclear Pore Complex Assembly.A single herpesvirus protein can mediate vesicle formation in the nuclear envelopeDimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assemblyThe lysine demethylase LSD1 is required for nuclear envelope formation at the end of mitosis.Herpesvirus membrane fusion - a team effortProtein interactions and consensus clustering analysis uncover insights into herpesvirus virion structure and function relationships
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
ricercatore
@it
հետազոտող
@hy
name
Benjamin Vollmer
@ast
Benjamin Vollmer
@en
Benjamin Vollmer
@es
Benjamin Vollmer
@nl
Benjamin Vollmer
@sl
type
label
Benjamin Vollmer
@ast
Benjamin Vollmer
@en
Benjamin Vollmer
@es
Benjamin Vollmer
@nl
Benjamin Vollmer
@sl
prefLabel
Benjamin Vollmer
@ast
Benjamin Vollmer
@en
Benjamin Vollmer
@es
Benjamin Vollmer
@nl
Benjamin Vollmer
@sl
P214
P106
P21
P214
P2798
P31
P496
0000-0002-7526-0582
P735
P7859
viaf-314867987