Martin D Jennings

发表

eIF2B promotes eIF5 dissociation from eIF2•GDP to facilitate guanine nucleotide exchange for translation initiation

G. Pavitt, Martin D Jennings, Yu Zhou, 2013, Genes & development.

eIF2B is a decameric guanine nucleotide exchange factor with a γ2ε2 tetrameric core

Carol V. Robinson, Carla Schmidt, C. Robinson, 2014, Nature Communications.

Fail-safe control of translation initiation by dissociation of eIF2α phosphorylated ternary complexes

G. Pavitt, Martin D Jennings, Christopher J. Kershaw, 2017, eLife.

A new function and complexity for protein translation initiation factor eIF2B

G. Pavitt, Martin D Jennings, Martin D. Jennings, 2014, Cell cycle.

eIF5 is a dual function GAP and GDI for eukaryotic translational control.

G. Pavitt, Martin D Jennings, Martin D. Jennings, 2010, Small GTPases.

Quantifying the Binding of Fluorescently Labeled Guanine Nucleotides and Initiator tRNA to Eukaryotic Translation Initiation Factor 2.

G. Pavitt, Martin D Jennings, Martin D. Jennings, 2022, Methods in molecular biology.

Specificity and Autoregulation of Notch Binding by Tandem WW Domains in Suppressor of Deltex*

Martin D Jennings, A. Golovanov, J. Avis, 2007, Journal of Biological Chemistry.

GTP binding to translation factor eIF2B stimulates its guanine nucleotide exchange activity

G. Pavitt, Martin D Jennings, Christopher J. Kershaw, 2021, iScience.

The structural basis of translational control by eIF2 phosphorylation

A. Roseman, G. Pavitt, Martin D Jennings, 2019, Nature communications.

Impaired eIF5A function causes a Mendelian disorder that is partially rescued in model systems by spermidine

Carol J. Saunders, C. Saunders, W. Newman, 2021, Nature communications.