首页/数据集/Development of D2HG biosensors inspired by the molecular mechanism of the D2HG-DhdR complex structure.

Development of D2HG biosensors inspired by the molecular mechanism of the D2HG-DhdR complex structure.

NIAID Data Ecosystem2026-05-10 收录

生物传感器开发

代谢物-蛋白相互作用

数据链接：

https://data.mendeley.com/datasets/3yh5f86cmv 数据链接链接失效反馈

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资源简介：

Excel datasheets for graphs and Uncropped immunoblotting (Data S1 and S2).

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创建时间：

2025-10-21

蛋白质结构解析

代谢物-蛋白相互作用

Solution Structure Of The SH3 Domain Of Human SH3GL3 Descriptor: SH3-containing GRB2-like protein 3 Authors: Gao, Y.G, Yan, X.Z, Hu, H.Y. Deposit date: 2005-11-02 Release date: 2006-11-14 Last modifie

Protein Data Bank Japan2024-05-29 更新130

Ranges for thermodynamic parameters for LC8-client binding.

代谢物-蛋白相互作用

力学参数分析

Values delineate 95% Bayesian credibility regions from sampled posterior distributions in kcal/mol, which are akin to 95% confidence intervals. Previously published binding parameters from an identica

Figshare2023-04-21 更新60

Identification of the retinoschisin-binding site on the retinal Na/K-ATPase

代谢物-蛋白相互作用

视网膜疾病分子机制

X-linked juvenile retinoschisis (XLRS) is a hereditary retinal dystrophy, caused by mutations in the RS1 gene which encodes the secreted protein retinoschisin. In recent years, several molecules have

NIAID Data Ecosystem50

Structural basis for the asymmetric binding of coactivator SRC1 to FXR-RXRα and allosteric communication within the complex

核受体信号转导

代谢物-蛋白相互作用

Structural basis for the asymmetric binding of coactivator SRC1 to FXR-RXRα and allosteric communication within the complex

integrated proteome resources70

Interaction of the Transcription Factor TFIID with Simian Virus 40 (SV40) Large T Antigen Interferes with Replication of SV40 DNA In Vitro

病毒复制调控

代谢物-蛋白相互作用

Simian virus 40 (SV40) large tumor (T) antigen is the major regulatory protein that directs the course of viral infection, primarily by interacting with host cell proteins and modulating their functio

PubMed Central60

Development of D2HG biosensors inspired by the molecular mechanism of the D2HG-DhdR complex structure.

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