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Akinori Sarai

Researcher at Kyushu Institute of Technology

Publications -  225
Citations -  10469

Akinori Sarai is an academic researcher from Kyushu Institute of Technology. The author has contributed to research in topics: DNA & Base pair. The author has an hindex of 49, co-authored 225 publications receiving 9663 citations. Previous affiliations of Akinori Sarai include National Institutes of Health & Japan Atomic Energy Research Institute.

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PrognoScan: a new database for meta-analysis of the prognostic value of genes

TL;DR: PrognoScan employs the minimum P-value approach for grouping patients for survival analysis that finds the optimal cutpoint in continuous gene expression measurement without prior biological knowledge or assumption and, as a result, enables systematic meta-analysis of multiple datasets.
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Identification of genes upregulated in ALK-positive and EGFR/KRAS/ALK-negative lung adenocarcinomas.

TL;DR: An extensive genome-wide expression profiling of 226 primary human stage I-II lung adenocarcinomas helps identify patients who may gain the most benefit from adjuvant chemotherapy after surgical resection and further stratify more or less aggressive subgroups of triple-negative lung ADC.
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Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices.

TL;DR: The solution structure of a specific DNA complex of the minimum DNA-binding domain (R2R3) is determined by heteronuclear multidimensional NMR by determining that both R2 and R3 contain three helices, and the third helix in each is found to be a recognition helix.
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ProTherm and ProNIT: thermodynamic databases for proteins and protein–nucleic acid interactions

TL;DR: ProTherm and ProNIT are two thermodynamic databases that contain experimentally determined thermodynamic parameters of protein stability and protein–nucleic acid interactions, respectively.
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Unique Mode of GCC Box Recognition by the DNA-binding Domain of Ethylene-responsive Element-binding Factor (ERF Domain) in Plant

TL;DR: Systematic DNA mutation analyses demonstrate that the specific amino acid contacts are confined within the 6-base pair GCCGCC region of the GCC box, and the first G, the fourth G and the sixth C exhibit highest binding specificity common in all three ERF domain-containing fragments studied.