Lisa D. Cabrita
London, ENG, United Kingdom
Last Updated: 09/26/2026
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Found 27 publications
Structures of protein folding intermediates on the ribosome.
Journal: Nature structural & molecular biology
Published: October 30, 2025
Thermodynamic profiles for cotranslational trigger factor substrate recognition.
Journal: Science advances
Published: July 10, 2024
The ribosome lowers the entropic penalty of protein folding.
Journal: Nature
Published: August 10, 2023
Author Correction: Modulating co-translational protein folding by rational design and ribosome engineering.
Journal: Nature communications
Published: September 16, 2022
Modulating co-translational protein folding by rational design and ribosome engineering.
Journal: Nature communications
Published: February 12, 2022
The ribosome stabilizes partially folded intermediates of a nascent multi-domain protein.
Journal: Nature chemistry
Published: December 01, 2021
Thermodynamics of co-translational folding and ribosome-nascent chain interactions.
Journal: Current opinion in structural biology
Published: November 10, 2021
Common sequence motifs of nascent chains engage the ribosome surface and trigger factor.
Journal: Proceedings of the National Academy of Sciences of the United States of America
Published: September 13, 2021
Nascent chain dynamics and ribosome interactions within folded ribosome-nascent chain complexes observed by NMR spectroscopy.
Journal: Chemical science
Published: August 05, 2021
Nascent chains can form co-translational folding intermediates that promote post-translational folding outcomes in a disease-causing protein.
Journal: Nature communications
Published: June 11, 2021
Interactions between nascent proteins and the ribosome surface inhibit co-translational folding.
Journal: Nature chemistry
Published: February 26, 2021
Last Updated: 09/26/2026