# task 1

> library(RISmed)

> Cell_2017 <- EUtilsSummary('(cell[TA]) AND 2017[DP]')

> summary(Cell_2017)

Query:

"Cell"[Journal] AND 2017[DP] 

Result count:  563

#task 2

> records <- EUtilsGet(Cell_2017)

> pubmed_data <- data.frame('Title'=ArticleTitle(records),'Abstract'=AbstractText(records),'ID'= ArticleId(records))

> pubmed_data$Title[pubmed_data$ID == 29290466]

[1] Structural Insights into Yeast Telomerase Recruitment to Telomeres.

555 Levels: 30 Years of NF-\u03baB: A Blossoming of Relevance to Human Pathobiology. ...

> pubmed_data$Abstract[pubmed_data$ID == 29290466]

[1] Telomerase maintains chromosome ends from humans to yeasts. Recruitment of yeast telomerase to telomeres occurs through its Ku and Est1 subunits<U+00A0>via independent interactions with telomerase<U+00A0>RNA<U+00A0>(TLC1) and telomeric proteins Sir4 and Cdc13,<U+00A0>respectively. However, the structures of the molecules comprising these telomerase-recruiting pathways remain unknown. Here, we report crystal structures of the Ku heterodimer and Est1 complexed with their key binding partners. Two major findings are as follows: (1) Ku specifically binds to telomerase RNA in a distinct, yet related, manner to how it binds DNA; and (2) Est1 employs two separate pockets to bind distinct motifs of Cdc13. The N-terminal Cdc13-binding site of Est1 cooperates with the TLC1-Ku-Sir4 pathway for telomerase recruitment, whereas the C-terminal interface is dispensable for binding Est1 in<U+00A0>vitro yet is nevertheless essential for telomere maintenance in<U+00A0>vivo. Overall, our results integ... <truncated>

521 Levels:  ...

Special Acknowledge to Dr. Wang Tao.