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Cammie F. Lesser

Researcher at Harvard University

Publications -  59
Citations -  2667

Cammie F. Lesser is an academic researcher from Harvard University. The author has contributed to research in topics: Effector & Type three secretion system. The author has an hindex of 27, co-authored 49 publications receiving 2199 citations. Previous affiliations of Cammie F. Lesser include University of Washington & University of California, San Francisco.

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Mutations in U6 snRNA that alter splice site specificity: implications for the active site

TL;DR: A genetic approach was used to test the hypothesis that a base-pairing interaction between the 5'splice site and the invariant ACAGAG sequence of U6 is a determinant of 5' splice site choice, and mutations in U6 or the intron that were predicted to stabilize the interaction suppressed aberrant cleavage and increased normal cleavage.
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Functional degradation: A mechanism of NLRP1 inflammasome activation by diverse pathogen enzymes

TL;DR: A distinct mechanism of pathogen-sensing mediated by an immune sensor protein called NLRP1B, a member of the nucleotide-binding domain leucine-rich repeat (NLRP) protein superfamily, is described, which finds that N-terminal cleavage of NL RP1B by LF protease results in destabilization of NLRP 1B and its degradation by the proteasome.
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Mutational analysis of pre-mRNA splicing in Saccharomyces cerevisiae using a sensitive new reporter gene, CUP1.

TL;DR: It is established that the efficiency of splicing correlates with the level of copper resistance of these strains and the use of CUP1 as a reporter gene may be generally applicable for monitoring cellular processes in yeast.
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The phi 80 and P22 attachment sites. Primary structure and interaction with Escherichia coli integration host factor.

TL;DR: Structural similarities in the nucleotide sequences of the att sites of phi 80 and P22 and the interaction of these sites with purified Escherichia coli integration host factor (IHF) suggest that IHF plays a very similar role in the site-specific recombination pathways of all three phage.
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Identification and characterization of ZapC: a stabilizer of the FtsZ-ring in Escherichia coli

TL;DR: The identification of an FtsZ stabilizer, ZapC (Z-associated protein C), in a protein localization screen conducted with E. coli suggests a key role for lateral bundling of the midcell Fts Z polymers in maintaining Ftsz ring stability during division.