Koc University Digital Collections
metadata only
CC BY 3.0
Cyclophilin40 isomerase activity is regulated by a temperature-dependent allosteric interaction with Hsp90
Cyclophilin 40 (Cyp40) comprises an N-terminal cyclophilin domain with peptidyl-prolyl isomerase (PPIase) activity and a C-terminal tetratricopeptide repeat (TPR) domain that binds to the C-terminal -EEVD sequence common to both heat shock protein 70 (Hsp70) and Hsp90. We show in the present study t
Conceptio Open Archive
Analyze & explore related research in Conceptio
Connect this record directly into your research workflow or AI agent. Explore citations across open repositories, query full text, and export structured proof bundles.
This document is indexed with metadata only: full text is not available in the archive for this record. Open the official source ↗
Related documents
- RNA target profiles direct the discovery of virulence functions for the cold-shock proteins CspC and CspE#1175189
- Can the PHS model (ISO7933) predict reasonable thermophysiological responses while wearing protective clothing in hot environments?#677991
- Research progress on neutrophil extracellular traps in sepsis‑induced coagulopathy (Review).#182422
- IL-40 and IL-41 Levels in Sepsis, Septic Shock, and Healthy Individuals#841355
- Ageing alters cysteine oxidation-regulated redox signalling in skeletal muscle: Integrative omics and AI-based structural predictions.#396090
Record · ID 934614
Retrieved via Conceptio: every document is proof-bundled with source, license, and retrieval metadata.
Retrieved via Conceptio: every document is proof-bundled with source, license, and retrieval metadata.
Bring this data into your agent: Connect via MCP or API · 20 free credits to start · no card required
Read the Docs → · View CLI source on GitHub · Conceptio Open Knowledge Archive
Read the Docs → · View CLI source on GitHub · Conceptio Open Knowledge Archive