专题:Heat shock proteins research

This cluster of papers explores the role of molecular chaperones, such as Hsp70 and Hsp90, in protein folding, proteostasis, cancer therapy, cell stress responses, and innate immunity. It delves into the mechanisms of chaperone machinery, protein quality control, and their implications in disease intervention.
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近5年高被引文献
Endoplasmic reticulum stress: molecular mechanism and therapeutic targets

article Full Text OpenAlex 1015 FWCI121.5915

Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities

article Full Text OpenAlex 788 FWCI41.2043

The molecular basis for cellular function of intrinsically disordered protein regions

review Full Text OpenAlex 706 FWCI17.4638

Heat Shock Response

book Full Text OpenAlex 565 FWCI0.3788

Reshaping endoplasmic reticulum quality control through the unfolded protein response

article Full Text OpenAlex 442 FWCI36.4206

Ubiquitination-Proteasome System (UPS) and Autophagy Two Main Protein Degradation Machineries in Response to Cell Stress

article Full Text OpenAlex 369 FWCI18.0818

Mechanisms and pathology of protein misfolding and aggregation

review Full Text OpenAlex 253 FWCI6.2952

Intrinsically Disordered Proteins: An Overview

article Full Text OpenAlex 250 FWCI10.9042

Ageing exacerbates ribosome pausing to disrupt cotranslational proteostasis

article Full Text OpenAlex 237 FWCI12.0893

Role of p53 in breast cancer progression: An insight into p53 targeted therapy

article Full Text OpenAlex 230 FWCI23.4559