L
Laura J. Terry
Researcher at Vanderbilt University Medical Center
Publications - 8
Citations - 1056
Laura J. Terry is an academic researcher from Vanderbilt University Medical Center. The author has contributed to research in topics: Nuclear pore & Nucleoporin. The author has an hindex of 8, co-authored 8 publications receiving 985 citations. Previous affiliations of Laura J. Terry include Princeton University & Vanderbilt University.
Papers
More filters
Journal ArticleDOI
Crossing the Nuclear Envelope: Hierarchical Regulation of Nucleocytoplasmic Transport
TL;DR: Transport of macromolecules between the nucleus and cytoplasm is a critical cellular process for eukaryotes, and the machinery that mediates nucleocytoplasmaic exchange is subject to multiple levels of control.
Journal ArticleDOI
Flexible Gates: Dynamic Topologies and Functions for FG Nucleoporins in Nucleocytoplasmic Transport
Laura J. Terry,Susan R. Wente +1 more
TL;DR: A novel family of NPC proteins, the FG-nucleoporins (FG-Nups), coordinates and potentially regulates NPC translocation and are essential components of the nuclear permeability barrier.
Journal ArticleDOI
Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex
Laura J. Terry,Susan R. Wente +1 more
TL;DR: This study uses a large-scale deletion strategy in Saccharomyces cerevisiae to generate a new set of more minimal pore mutants that lack specific FG domains, and finds a requirement for two NPC substructures—one on the nuclear NPC face and one in the NPC central core.
Journal ArticleDOI
Human kinome profiling identifies a requirement for AMP-activated protein kinase during human cytomegalovirus infection
TL;DR: It is proposed that HCMV requires AMPK or related activity for viral replication and reprogramming of cellular metabolism, and a comprehensive RNAi screen predicts that 106 cellular kinases influence growth of the virus.
Journal ArticleDOI
Human cytomegalovirus pUL97 kinase induces global changes in the infected cell phosphoproteome
TL;DR: Analysis of the phosphoproteome of SILAC‐labeled human fibroblasts during infection with either wild‐type HCMV or a pUL97 kinase‐dead mutant virus suggests that modulation of nuclear pore function may be important during H CMV replication.