James A. DeCaprio
Harvard University
236 Papers
3.1K Citations
James A. DeCaprio is an academic researcher from Harvard University. The author has contributed to research in topics: Merkel cell carcinoma & Retinoblastoma protein. The author has an hindex of 75, co-authored 217 publications. Previous affiliations of James A. DeCaprio include Institute of Cancer Research & Dana Corporation.
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Papers
SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene
James A. DeCaprio,John W. Ludlow,James Figge,Jin-Yuh Shew,Chun-Ming Huang,Wen-Hwa Lee,Erika Marsilio,Eva Paucha,David M. Livingston +8 more
TL;DR: Results are consistent with a model for transformation by SV40 which, at least in part, involves T/p110-114 complex formation and the perturbation of Rb protein and/or T function.
1.5K
The product of the retinoblastoma susceptibility gene has properties of a cell cycle regulatory element.
James A. DeCaprio,John W. Ludlow,Dennis C. Lynch,Yusuke Furukawa,James D. Griffin,Helen Piwnica-Worms,Chun-Ming Huang,David M. Livingston +7 more
TL;DR: The cell cycle-dependent phosphorylation of Rb is demonstrated and a model to explain how Rb may suppress cell growth by acting as a cell cycle regulatory element is proposed.
956
Telomerase maintains telomere structure in normal human cells.
Kenkichi Masutomi,Evan Y. Yu,Shilagardy Khurts,Ittai Ben-Porath,Jennifer L. Currier,Geoffrey B. Metz,Mary W. Brooks,Shuichi Kaneko,Seishi Murakami,James A. DeCaprio,Robert A. Weinberg,Sheila A. Stewart,William C. Hahn +12 more
TL;DR: The view that telomerase and telomere structure are dynamically regulated in normal human cells and that telomeres length alone is unlikely to trigger entry into replicative senescence is supported.
741
Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C
TL;DR: Results suggest that the tumor suppression function of pVHL may be linked to its ability to bind to Elongin B and C.
696
14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport.
Anne Brunet,Fumihiko Kanai,Fumihiko Kanai,Justine R. Stehn,Jian Xu,Dilara Sarbassova,Dilara Sarbassova,John V. Frangioni,Sorab N. Dalal,James A. DeCaprio,Michael E. Greenberg,Michael B. Yaffe,Michael B. Yaffe +12 more
TL;DR: It is shown that the leucine-rich region within the COOH-terminal α-helix of 14-3-3, which had been proposed to function as a nuclear export signal (NES), instead functions globally in ligand binding and does not directly mediate nuclear transport.