Search Results - "Cocozaki, Alexis I"

Structure of the Cmr2 Subunit of the CRISPR-Cas RNA Silencing Complex by Cocozaki, Alexis I., Ramia, Nancy F., Shao, Yaming, Hale, Caryn R., Terns, Rebecca M., Terns, Michael P., Li, Hong

“…Cmr2 is the largest and an essential subunit of a CRISPR RNA-Cas protein complex (the Cmr complex) that cleaves foreign RNA to protect prokaryotes from…”
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Structure of the Cmr2-Cmr3 Subcomplex of the Cmr RNA Silencing Complex by Shao, Yaming, Cocozaki, Alexis I., Ramia, Nancy F., Terns, Rebecca M., Terns, Michael P., Li, Hong

“…The Cmr complex is an RNA-guided effector complex that cleaves invader RNA in the prokaryotic immune response mediated by the CRISPR (Clustered Regularly…”
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Bacteriophage P22 Antitermination boxB Sequence Requirements Are Complex and Overlap with Those of λ by COCOZAKI, Alexis I, GHATTAS, Ingrid R, SMITH, Colin A

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The RNA-Binding Domain of Bacteriophage P22 N Protein Is Highly Mutable, and a Single Mutation Relaxes Specificity toward λ by COCOZAKI, Alexis I, GHATTAS, Ingrid R, SMITH, Colin A

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Resistance mutations generate divergent antibiotic susceptibility profiles against translation inhibitors by Cocozaki, Alexis I., Altman, Roger B., Huang, Jian, Buurman, Ed T., Kazmirski, Steven L., Doig, Peter, Prince, D. Bryan, Blanchard, Scott C., Cate, Jamie H. D., Ferguson, Andrew D.

“…Mutations conferring resistance to translation inhibitors often alter the structure of rRNA. Reduced susceptibility to distinct structural antibiotic classes…”
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Staphylococcus epidermidis Csm1 is a 3'-5' exonuclease by Ramia, Nancy F, Tang, Li, Cocozaki, Alexis I, Li, Hong

“…Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR) offer an adaptive immune system that protects bacteria and archaea from nucleic acid…”
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Structural Insights Lead to a Negamycin Analogue with Improved Antimicrobial Activity against Gram-Negative Pathogens by McKinney, David C, Basarab, Gregory S, Cocozaki, Alexis I, Foulk, Melinda A, Miller, Matthew D, Ruvinsky, Anatoly M, Scott, Clay W, Thakur, Kumar, Zhao, Liang, Buurman, Ed T, Narayan, Sridhar

“…Negamycin is a natural product with antibacterial activity against a broad range of Gram-negative pathogens. Recent revelation of its ribosomal binding site…”
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The RNA-Binding Domain of Bacteriophage P22 N Protein Is Highly Mutable, and a Single Mutation Relaxes Specificity toward [lamda] by Cocozaki, Alexis I, Ghattas, Ingrid R, Smith, Colin A

“…Antitermination in bacteriophage P22, a lambdoid phage, uses the arginine-rich domain of the N protein to recognize boxB RNAs in the nut site of two regulated…”
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Bacteriophage P22 Antitermination boxB Sequence Requirements Are Complex and Overlap with Those of l by Cocozaki, Alexis I, Ghattas, Ingrid R, Smith, Colin A

“…Transcription antitermination in phages l and P22 uses N proteins that bind to similar boxB RNA hairpins in regulated transcripts. In contrast to the l N-boxB…”
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Bacteriophage P22 Antitermination boxB Sequence Requirements Are Complex and Overlap with Those of [lamda] by Cocozaki, Alexis I, Ghattas, Ingrid R, Smith, Colin A

“…Transcription antitermination in phages ... and P22 uses N proteins that bind to similar boxB RNA hairpins in regulated transcripts. In contrast to the …”
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