Marc E. Colosimo
Mitre Corporation
13 Papers
110 Citations
Marc E. Colosimo is an academic researcher from Mitre Corporation. The author has contributed to research in topics: Computer science & Tree (data structure). The author has an hindex of 12, co-authored 13 publications. Previous affiliations of Marc E. Colosimo include Brandeis University.
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Papers
BioCreAtIvE Task 1A: gene mention finding evaluation
TL;DR: The 80% plus F-measure results are good, but still somewhat lag the best scores achieved in some other domains such as newswire, due in part to the complexity and length of gene names, compared to person or organization names in newswire.
Overview of BioCreAtIvE task 1B: normalized gene lists.
TL;DR: This assessment demonstrates that multiple groups were able to perform a real biological task across a range of organisms, and holds out promise that the technology can provide partial automation of the curation process in the near future.
Gene name identification and normalization using a model organism database
TL;DR: These experiments indicate that the lexical resources provided by FlyBase are complete enough to achieve high recall on the gene list task, and that normalization requires accurate disambiguation; different strategies for tagging and normalization trade off recall for precision.
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Gene Name Extraction Using FlyBase Resources
Alexander A. Morgan,Lynette Hirschman,Alexander S. Yeh,Marc E. Colosimo +3 more
- 11 Jul 2003
TL;DR: A simple method for the automatic creation of large quantities of imperfect training data for a biological entity (gene or protein) extraction system and has the advantage of being rapidly transferable to new domains that have similar existing resources.
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The UNC-3 Olf/EBF protein represses alternate neuronal programs to specify chemosensory neuron identity.
TL;DR: The results indicate that UNC-3 is a critical component of the transcription factor code that integrates cell-intrinsic developmental programs with external signals to specify sensory neuronal identity and suggest models for O/E protein functions in other systems.
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