L
Leonard H. Rome
Researcher at University of California, Los Angeles
Publications - 147
Citations - 9337
Leonard H. Rome is an academic researcher from University of California, Los Angeles. The author has contributed to research in topics: Vault (organelle) & Major vault protein. The author has an hindex of 49, co-authored 145 publications receiving 8213 citations. Previous affiliations of Leonard H. Rome include University of Michigan & University of Southern California.
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Journal ArticleDOI
Reassessment of Exosome Composition
Dennis K. Jeppesen,Aidan M. Fenix,Jeffrey L. Franklin,James N. Higginbotham,Qin Zhang,Lisa J. Zimmerman,Daniel C. Liebler,Jie Ping,Qi Liu,Rachel Evans,William H. Fissell,James G. Patton,Leonard H. Rome,Dylan T. Burnette,Robert J. Coffey,Robert J. Coffey,Robert J. Coffey +16 more
TL;DR: High-resolution density gradient fractionation and direct immunoaffinity capture are employed to precisely characterize the RNA, DNA, and protein constituents of exosomes and other non-vesicle material and show that small extracellular vesicles are not vehicles of active DNA release.
Journal ArticleDOI
The 193-Kd Vault Protein, Vparp, Is a Novel Poly(Adp-Ribose) Polymerase
Valerie A. Kickhoefer,Amara C. Siva,Nancy Kedersha,Elisabeth M. Inman,Cristina T. Ruland,Michel Streuli,Leonard H. Rome +6 more
TL;DR: The 193-kD vault protein is identified by its interaction with the MVP in a yeast two-hybrid screen and confirmed its identity by peptide sequence analysis, and it is shown that one substrate for this vault-associated PARP activity is the MVP.
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Two species of lysosomal organelles in cultured human fibroblasts
TL;DR: Cultured diploid human skin fibroblasts were fractionated by a procedure that maximizes recovery of particles containing acid hydrolases to suggest that the dense and buoyant lysosomal organelles originate primarily from residual bodies and the GERL network, respectively.
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Isolation and characterization of a novel ribonucleoprotein particle: large structures contain a single species of small RNA.
Nancy Kedersha,Leonard H. Rome +1 more
TL;DR: It appears that these novel ribonucleoprotein structures are broadly distributed among different cell types, and are observed in partially purified fractions from human fibroblasts, murine 3T3 cells, glial cells, and rabbit alveolar macrophages.
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Structural requirements for time-dependent inhibition of prostaglandin biosynthesis by anti-inflammatory drugs.
TL;DR: Several anti-inflammatory drugs have been examined for their ability to cause a time-dependent destruction of the fatty acid oxygenase that produces prostaglandins, and the reversible binding of the agents at the active site was not appreciably dependent upon the free carboxyl group, whereas the subsequent irreversible process was.