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Martin D Jennings

Showing results (1-10 of 19) with videos related to

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Small Gtpases|June 21, 2011
eIF5 is a dual function GAP and GDI for eukaryotic translational controlMartin D Jennings, Graham D Pavitt
Methods in Molecular Biology (Clifton, N.J.)|February 16, 2022
Quantifying the Binding of Fluorescently Labeled Guanine Nucleotides and Initiator tRNA to Eukaryotic Translation Initiation Factor 2Martin D Jennings, Graham D Pavitt
Nature|May 21, 2010
eIF5 has GDI activity necessary for translational control by eIF2 phosphorylationMartin D Jennings, Graham D Pavitt
Cell Cycle (Georgetown, Tex.)|December 9, 2014
A new function and complexity for protein translation initiation factor eIF2BMartin D Jennings, Graham D Pavitt
Biochemical Society Transactions|July 18, 2008
Clues to the mechanism of action of eIF2B, the guanine-nucleotide-exchange factor for translation initiationSarah S Mohammad-Qureshi, Martin D Jennings, Graham D Pavitt
Elife|March 19, 2017
Fail-safe control of translation initiation by dissociation of eIF2α phosphorylated ternary complexesMartin D Jennings, Christopher J Kershaw, Tomas Adomavicius, et al.
The Journal of Biological Chemistry|July 28, 2007
Specificity and autoregulation of Notch binding by tandem WW domains in suppressor of DeltexMartin D Jennings, Richard T Blankley, Martin Baron, et al.
Genes & Development|December 20, 2013
eIF2B promotes eIF5 dissociation from eIF2*GDP to facilitate guanine nucleotide exchange for translation initiationMartin D Jennings, Yu Zhou, Sarah S Mohammad-Qureshi, et al.
Iscience|December 8, 2021
GTP binding to translation factor eIF2B stimulates its guanine nucleotide exchange activityChristopher J Kershaw, Martin D Jennings, Francesco Cortopassi, et al.
Nature Communications|May 24, 2014
eIF2B is a decameric guanine nucleotide exchange factor with a γ2ε2 tetrameric coreYuliya Gordiyenko, Carla Schmidt, Martin D Jennings, et al.
Pageof 2

Showing results (1-10 of 19) with videos related to

Sort By:
Pageof 2
Small Gtpases|June 21, 2011
eIF5 is a dual function GAP and GDI for eukaryotic translational controlMartin D Jennings, Graham D Pavitt
Methods in Molecular Biology (Clifton, N.J.)|February 16, 2022
Quantifying the Binding of Fluorescently Labeled Guanine Nucleotides and Initiator tRNA to Eukaryotic Translation Initiation Factor 2Martin D Jennings, Graham D Pavitt
Nature|May 21, 2010
eIF5 has GDI activity necessary for translational control by eIF2 phosphorylationMartin D Jennings, Graham D Pavitt
Cell Cycle (Georgetown, Tex.)|December 9, 2014
A new function and complexity for protein translation initiation factor eIF2BMartin D Jennings, Graham D Pavitt
Biochemical Society Transactions|July 18, 2008
Clues to the mechanism of action of eIF2B, the guanine-nucleotide-exchange factor for translation initiationSarah S Mohammad-Qureshi, Martin D Jennings, Graham D Pavitt
Elife|March 19, 2017
Fail-safe control of translation initiation by dissociation of eIF2α phosphorylated ternary complexesMartin D Jennings, Christopher J Kershaw, Tomas Adomavicius, et al.
The Journal of Biological Chemistry|July 28, 2007
Specificity and autoregulation of Notch binding by tandem WW domains in suppressor of DeltexMartin D Jennings, Richard T Blankley, Martin Baron, et al.
Genes & Development|December 20, 2013
eIF2B promotes eIF5 dissociation from eIF2*GDP to facilitate guanine nucleotide exchange for translation initiationMartin D Jennings, Yu Zhou, Sarah S Mohammad-Qureshi, et al.
Iscience|December 8, 2021
GTP binding to translation factor eIF2B stimulates its guanine nucleotide exchange activityChristopher J Kershaw, Martin D Jennings, Francesco Cortopassi, et al.
Nature Communications|May 24, 2014
eIF2B is a decameric guanine nucleotide exchange factor with a γ2ε2 tetrameric coreYuliya Gordiyenko, Carla Schmidt, Martin D Jennings, et al.
Pageof 2