热休克蛋白90（HSP90）分子伴侣系统的共伴侣蛋白细胞分裂周期37（CDC37）蛋白在HSP90分子伴侣系统中负责招募待折叠成熟的激酶，随后与HSP90蛋白互作，进而将招募的客户激酶递送给HSP90蛋白。CDC37同时结合HSP90和激酶，在肿瘤细胞中过表达，成为潜在的药物靶标。

An exploration of the unanswered questions in how the molecular chaperone Hsp90 supports protein homeostasis, and how single-molecule techniques could drive future breakthroughs in answering them.

deletion of an N-terminal JNK structural motif induced Hsp90 and Cdc37 binding, whereas deletion of a C-terminal motif induced only Hsp90 binding 23. In contrast, mutations in the kinase ...

New tools may help us understand how Aha1 complexes interact and complement other hetero-oligomeric complexes with Hsp90 co-chaperones including FKBP51 and CDC37 in driving cancers and/or ...

For example, chaperones such as heat-shock protein-90 (HSP90) refold mutated or otherwise perturbed proteins, thereby enabling normal activity while the system accumulates mutations but suppresses ...

Department of Oral Anatomy and Physiology, Jilin Provincial Key Laboratory of Oral Biomedical Engineering, Hospital of Stomatology, Jilin University, Changchun, China Oral squamous cell carcinoma ...

The Center for Basic Research and Innovation of Medicine and Pharmacy (MOE), School of Pharmacy, Second Military Medical University (Naval Medical University), 325 Guohe Road, Shanghai 200433, China ...

2024年12月11日，中国科学技术大学生命科学与医学部黄成栋教授团队在 Nature Communications 期刊发表了题为“The Dynamic Triage Interplay of Hsp90 with its Chaperone Cycle and Client Binding”的研究论文。该研究利用液体核磁共振（NMR）技术，首次在原子分辨率上解析了Hsp90在ATP循环 ...