Lisa D Cabrita
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Explore the profile of Lisa D Cabrita including associated specialties, affiliations and a list of published articles.
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56
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1098
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Recent Articles
1.
Streit J, Bukvin I, Chan S, Bashir S, Woodburn L, Wlodarski T, et al.
Nature
. 2024 Aug;
633(8028):232-239.
PMID: 39112704
Most proteins fold during biosynthesis on the ribosome, and co-translational folding energetics, pathways and outcomes of many proteins have been found to differ considerably from those in refolding studies. The...
2.
Wlodarski T, Streit J, Mitropoulou A, Cabrita L, Vendruscolo M, Christodoulou J
Sci Rep
. 2024 Aug;
14(1):18149.
PMID: 39103467
Cryogenic electron microscopy (cryo-EM) has emerged as a powerful method for the determination of structures of complex biological molecules. The accurate characterisation of the dynamics of such systems, however, remains...
3.
Herling T, Cassaignau A, Wentink A, Peter Q, Kumar P, Kartanas T, et al.
Sci Adv
. 2024 Jul;
10(28):eadn4824.
PMID: 38985872
Molecular chaperones are central to the maintenance of proteostasis in living cells. A key member of this protein family is trigger factor (TF), which acts throughout the protein life cycle...
4.
Ahn M, Wlodarski T, Mitropoulou A, Chan S, Sidhu H, Plessa E, et al.
Nat Commun
. 2022 Sep;
13(1):5441.
PMID: 36114226
No abstract available.
5.
Chan S, Wlodarski T, Streit J, Cassaignau A, Woodburn L, Ahn M, et al.
Nat Chem
. 2022 Aug;
14(10):1165-1173.
PMID: 35927328
Co-translational folding is crucial to ensure the production of biologically active proteins. The ribosome can alter the folding pathways of nascent polypeptide chains, yet a structural understanding remains largely inaccessible...
6.
Ahn M, Wlodarski T, Mitropoulou A, Chan S, Sidhu H, Plessa E, et al.
Nat Commun
. 2022 Jul;
13(1):4243.
PMID: 35869078
Co-translational folding is a fundamental process for the efficient biosynthesis of nascent polypeptides that emerge through the ribosome exit tunnel. To understand how this process is modulated by the shape...
7.
Waudby C, Burridge C, Cabrita L, Christodoulou J
Curr Opin Struct Biol
. 2022 Apr;
74:102357.
PMID: 35390638
Proteins can begin the conformational search for their native structure in parallel with biosynthesis on the ribosome, in a process termed co-translational folding. In contrast to the reversible folding of...
8.
Deckert A, Cassaignau A, Wang X, Wlodarski T, Chan S, Waudby C, et al.
Proc Natl Acad Sci U S A
. 2021 Dec;
118(52).
PMID: 34930833
In the cell, the conformations of nascent polypeptide chains during translation are modulated by both the ribosome and its associated molecular chaperone, trigger factor. The specific interactions that underlie these...
9.
Plessa E, Chu L, Chan S, Thomas O, Cassaignau A, Waudby C, et al.
Nat Commun
. 2021 Nov;
12(1):6447.
PMID: 34750347
During biosynthesis, proteins can begin folding co-translationally to acquire their biologically-active structures. Folding, however, is an imperfect process and in many cases misfolding results in disease. Less is understood of...
10.
Burridge C, Waudby C, Wlodarski T, Cassaignau A, Cabrita L, Christodoulou J
Chem Sci
. 2021 Nov;
12(39):13120-13126.
PMID: 34745542
The folding of many proteins can begin during biosynthesis on the ribosome and can be modulated by the ribosome itself. Such perturbations are generally believed to be mediated through interactions...