Cyclin-specific docking mechanisms reveal the complexity of M-CDK function in the cell cycle. Örd et al.

NIAID Data Ecosystem2026-04-18 收录

细胞周期调控

蛋白质相互作用

数据链接：

https://data.mendeley.com/datasets/r7hv4zj6zw 数据链接链接失效反馈

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Unprocessed autoradiographs and western blot images of Örd et al.

创建时间：

2019-05-14

DataSheet4_PRR11 promotes cell proliferation by regulating PTTG1 through interacting with E2F1 transcription factor in pan-cancer.zip

癌症分子机制

细胞周期调控

The upregulated proline rich 11 (PRR11) plays a critical role in cancer progression. The relevant biological functions of PRR11 in pan-cancer development are not well understood. In the current study,

NIAID Data Ecosystem30

Composition of MIX (new) set.

蛋白质热点残基预测

蛋白质相互作用

Protein hotspot residues are key sites that mediate protein-protein interactions. Accurate identification of these residues is essential for understanding the mechanism from protein to function and fo

NIAID Data Ecosystem20

Data Sheet 3_Using AlphaFold-Multimer to study novel protein-protein interactions of predation essential hypothetical proteins in Bdellovibrio.zip

蛋白质相互作用

细菌捕食机制

Bdellovibrio bacteriovorus is the most studied member of a group of small motile Gram-negative bacteria called Bdellovibrio and Like Organisms (BALOs). B. bacteriovorus can prey on Gram-negative bacte

NIAID Data Ecosystem00

Calpains 8 and 9 form a complex.

蛋白质相互作用

calpains复合物

(A) RT-PCR analysis of calpains 8 and 9 mRNA in the WT, Capn8+/−, Capn8−/−, Capn9+/−, and Capn9−/− gastric mucosa using primer pairs: calpain 8-5′/-3′ for calpain 8, calpain 9-5′/-3′ for calpain 9, an

NIAID Data Ecosystem20

Table 5_Successful prediction of LC8 binding to intrinsically disordered proteins sheds light on AlphaFold’s black box.xlsx

蛋白质相互作用

结构生物信息学

IntroductionLC8 is a hub protein involved in many processes from tumor suppression and cell cycle regulation to neurotransmission and viral infection. Despite recent progress, prediction of binding si

NIAID Data Ecosystem00

Cyclin-specific docking mechanisms reveal the complexity of M-CDK function in the cell cycle. Örd et al.

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