The SCHOOL of nature: II. Protein order, disorder and oligomericity in transmembrane signaling.
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Summary
This work structures the current multidisciplinary knowledge and views of the mechanisms governing the coupling of recognition to signal transduction and cell response and suggests the similarity between therapeutic targets, thus opening new horizons for both fundamental and clinically relevant studies.
- Type
- dissertation
- Published
- 2010-04-01
- Cited by
- 13
- References
- 147
- Access
- Open access
- OpenAlex
- https://openalex.org/W21487511
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:31646588
Keywords
Chemistry
References
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- Novel mechanistic concept of platelet inhibition
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Cited by
- Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes.
- Unusual biophysics of immune signaling-related intrinsically disordered proteins.
- Cells diversify transmembrane signaling through the controlled chaos of protein disorder.
- "Monovalent" ligands that trigger TLR-4 and TCR are not necessarily truly monovalent.
- Differential occurrence of protein intrinsic disorder in the cytoplasmic signaling domains of cell receptors.
- The SCHOOL of nature: IV. Learning from viruses.
- Uncoupled binding and folding of immune signaling-related intrinsically disordered proteins.
- Homodimerization propensity of the intrinsically disordered N-terminal domain of Ultraspiracle from Aedes aegypti.
- Membrane-mediated regulation of the intrinsically disordered CD3ϵ cytoplasmic tail of the TCR.
- Structural biology of intrinsically disordered proteins: Revisiting unsolved mysteries.
- The SCHOOL of nature: III. From mechanistic understanding to novel therapies.
- Targeting Intramembrane Protein–Protein Interactions: Novel Therapeutic Strategy of Millions Years Old
- SCHOOL of nature: ligand-independent immunomodulatory peptides
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