Year |
Citation |
Score |
2017 |
Vallaster C, Gharadaghi F, Cocozaki A, Jacques K, Price B, Guichard S. Abstract B14: A novel role for BRD9 in regulating cellular growth and DNA damage response pathways Molecular Cancer Research. 15. DOI: 10.1158/1557-3125.Dnarepair16-B14 |
0.356 |
|
2014 |
Ramia NF, Spilman M, Tang L, Shao Y, Elmore J, Hale C, Cocozaki A, Bhattacharya N, Terns RM, Terns MP, Li H, Stagg SM. Essential structural and functional roles of the Cmr4 subunit in RNA cleavage by the Cmr CRISPR-Cas complex. Cell Reports. 9: 1610-7. PMID 25482566 DOI: 10.1016/J.Celrep.2014.11.007 |
0.754 |
|
2014 |
Hale CR, Cocozaki A, Li H, Terns RM, Terns MP. Target RNA capture and cleavage by the Cmr type III-B CRISPR-Cas effector complex. Genes & Development. 28: 2432-43. PMID 25367038 DOI: 10.1101/Gad.250712.114 |
0.739 |
|
2014 |
Ramia NF, Tang L, Cocozaki AI, Li H. Staphylococcus epidermidis Csm1 is a 3'-5' exonuclease. Nucleic Acids Research. 42: 1129-38. PMID 24121684 DOI: 10.1093/Nar/Gkt914 |
0.727 |
|
2013 |
Spilman M, Cocozaki A, Hale C, Shao Y, Ramia N, Terns R, Terns M, Li H, Stagg S. Structure of an RNA silencing complex of the CRISPR-Cas immune system. Molecular Cell. 52: 146-52. PMID 24119404 DOI: 10.1016/J.Molcel.2013.09.008 |
0.759 |
|
2013 |
Shao Y, Cocozaki AI, Ramia NF, Terns RM, Terns MP, Li H. Structure of the Cmr2-Cmr3 subcomplex of the Cmr RNA silencing complex. Structure (London, England : 1993). 21: 376-84. PMID 23395183 DOI: 10.1016/J.Str.2013.01.002 |
0.761 |
|
2013 |
Spilman M, Cocozaki A, Shao Y, Ramia N, Li H, Stagg S. Structure of an RNA Silencing Complex in CRISPR-Mediated Immunity Microscopy and Microanalysis. 19: 124-125. DOI: 10.1017/S1431927613002614 |
0.738 |
|
2012 |
Cocozaki AI, Ramia NF, Shao Y, Hale CR, Terns RM, Terns MP, Li H. Structure of the Cmr2 subunit of the CRISPR-Cas RNA silencing complex. Structure (London, England : 1993). 20: 545-53. PMID 22405013 DOI: 10.1016/J.Str.2012.01.018 |
0.732 |
|
2008 |
Cocozaki AI, Ghattas IR, Smith CA. The RNA-binding domain of bacteriophage P22 N protein is highly mutable, and a single mutation relaxes specificity toward lambda. Journal of Bacteriology. 190: 7699-708. PMID 18820025 DOI: 10.1128/Jb.00997-08 |
0.358 |
|
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