D
David T. Shima
Researcher at Lincoln's Inn
Publications - 25
Citations - 1436
David T. Shima is an academic researcher from Lincoln's Inn. The author has contributed to research in topics: Aptamer & Golgi apparatus. The author has an hindex of 13, co-authored 25 publications receiving 1383 citations. Previous affiliations of David T. Shima include National Institute for Health Research.
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Journal ArticleDOI
Synergistic roles for Pim-1 and c-Myc in STAT3-mediated cell cycle progression and antiapoptosis.
Takahiro Shirogane,Toshiyuki Fukada,Joyce M.M. Müller,David T. Shima,Masahiko Hibi,Toshio Hirano +5 more
TL;DR: The results indicate that Pim-family proteins play crucial roles in gp130-mediated cell proliferation and explain the synergy between Pim and c-Myc proteins in celliferation and lymphomagenesis.
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Partitioning of the Golgi Apparatus during Mitosis in Living HeLa Cells
TL;DR: The results provide direct evidence for mitotic clusters as the unit of partitioning and suggest that precise regulation of the number, position, and compartmentation of mitotic membranes is a critical feature for the ordered inheritance of the Golgi apparatus.
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VEGF-A Is Necessary and Sufficient for Retinal Neuroprotection in Models of Experimental Glaucoma
Richard Foxton,Arthur Finkelstein,Sauparnika Vijay,Annegret Dahlmann-Noor,Peng T. Khaw,James Edwards Morgan,David T. Shima,Yin-Shan Ng +7 more
TL;DR: It is demonstrated that VEGF-A acts directly on retinal ganglion cells (RGCs) to promote survival and that V EGF receptor-2 signaling via the phosphoinositide-3-kinase/Akt pathway was required for the survival response in isolated RGCs.
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Targeted deletion of p97 (VCP/CDC48) in mouse results in early embryonic lethality.
TL;DR: Gene disruption in Saccromyces cerevisiae, Drosophila melanogaster and Trypanosoma brucei demonstrated that p97 is essential in unicellular and multicellular organisms, and disrupted the p97 locus by gene targeting showed that p 97 is an essential gene for early mouse development.
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Molecular Mapping and Functional Characterization of the VEGF164 Heparin-binding Domain
Dominik Krilleke,Andrea DeErkenez,William Schubert,Indrajit Giri,Gregory S. Robinson,Yin-Shan Ng,David T. Shima +6 more
TL;DR: This work used site-directed mutagenesis to identify amino acid residues that are critical for heparin binding activity of the VEGF164 HBD and found Arg-13, Arg-14, and Arg-49 to be critical forheparinbinding and interaction with extracellular matrix in tissue samples.