Has the code for protein translocation been broken?
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Summary
It is the view that the "code" for protein translocation has not yet been deciphered and that further experiments are required for teasing apart the various energetic factors contributing toprotein translocation.
- Type
- article
- Published
- 2006-04-01
- Cited by
- 23
- References
- 27
- OpenAlex
- https://openalex.org/W16530414
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:1196780
Keywords
Political science
References
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Cited by
- MINS2: Revisiting the molecular code for transmembrane-helix recognition by the Sec61 translocon
- Sequence-based predictions of membrane-protein topology, homology and insertion
- Prédiction de la localisation des protéines membranaires : méthodes méta-heuristiques pour la détermination du potentiel d'insertion des acides aminés
- Bacterial Physiology and Metabolism: Contents
- Structural determinants of lateral gate opening in the protein translocon.
- Penetration depth of surfactant peptide KL4 into membranes is determined by fatty acid saturation.
- Hydrophobicity scales: a thermodynamic looking glass into lipid-protein interactions.
- On the energetics of translocon-assisted insertion of charged transmembrane helices into membranes
- Bilayer deformation by the Kv channel voltage sensor domain revealed by self-assembly simulations
- Membrane bending is critical for the stability of voltage sensor segments in the membrane
- Arginine in Membranes: The Connection Between Molecular Dynamics Simulations and Translocon-Mediated Insertion Experiments
- Lonely Arginine Seeks Friendly Environment
- Prediction of the translocon-mediated membrane insertion free energies of protein sequences
- On the thermodynamic stability of a charged arginine side chain in a transmembrane helix
- MEMBRANE BENDING IS CRITICAL FOR ASSESSING THE THERMODYNAMIC STABILITY OF PROTEINS IN THE MEMBRANE
- Mutational scanning reveals the determinants of protein insertion and association energetics in the plasma membrane
- Decrypting protein insertion through the translocon with free-energy calculations.
- Interplay between hydrophobicity and the positive-inside rule in determining membrane-protein topology
- potentiel d'insertion des acides amin es
- A lipophilicity-based energy function for membrane-protein modelling and design
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