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
11.
Cassaignau A, Wlodarski T, Chan S, Woodburn L, Bukvin I, Streit J, et al.
Nat Chem
. 2021 Oct;
13(12):1214-1220.
PMID: 34650236
Most proteins begin to fold during biosynthesis on the ribosome. It has been suggested that interactions between the emerging polypeptide and the ribosome surface might allow the ribosome itself to...
12.
Capitini C, Fani G, Vega M, Penco A, Canale C, Cabrita L, et al.
Amyloid
. 2020 Oct;
28(1):56-65.
PMID: 33026249
Accumulation of ubiquitin-positive, tau- and α-synuclein-negative intracellular inclusions of TDP-43 in the central nervous system represents the major hallmark correlated to amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with...
13.
Cassaignau A, Cabrita L, Christodoulou J
Annu Rev Biochem
. 2020 Jun;
89:389-415.
PMID: 32569518
Folding of polypeptides begins during their synthesis on ribosomes. This process has evolved as a means for the cell to maintain proteostasis, by mitigating the risk of protein misfolding and...
14.
Wang X, Kirkpatrick J, Launay H, De Simone A, Haussinger D, Dobson C, et al.
Sci Rep
. 2019 Sep;
9(1):13528.
PMID: 31537834
We describe an NMR approach based on the measurement of residual dipolar couplings (RDCs) to probe the structural and motional properties of the dynamic regions of the ribosome. Alignment of...
15.
Waudby C, Wlodarski T, Karyadi M, Cassaignau A, Chan S, Wentink A, et al.
Proc Natl Acad Sci U S A
. 2018 Sep;
115(39):9744-9749.
PMID: 30201720
Cotranslational folding (CTF) is a fundamental molecular process that ensures efficient protein biosynthesis and minimizes the formation of misfolded states. However, the complexity of this process makes it extremely challenging...
16.
Javed A, Christodoulou J, Cabrita L, Orlova E
Acta Crystallogr D Struct Biol
. 2017 Jun;
73(Pt 6):509-521.
PMID: 28580913
Protein folding, a process that underpins cellular activity, begins co-translationally on the ribosome. During translation, a newly synthesized polypeptide chain enters the ribosomal exit tunnel and actively interacts with the...
17.
Cassaignau A, Launay H, Karyadi M, Wang X, Waudby C, Deckert A, et al.
Nat Protoc
. 2016 Jul;
11(8):1492-507.
PMID: 27466710
During biosynthesis on the ribosome, an elongating nascent polypeptide chain can begin to fold, in a process that is central to all living systems. Detailed structural studies of co-translational protein...
18.
Waudby C, Ramos A, Cabrita L, Christodoulou J
Sci Rep
. 2016 Apr;
6:24826.
PMID: 27109776
NMR titration experiments are a rich source of structural, mechanistic, thermodynamic and kinetic information on biomolecular interactions, which can be extracted through the quantitative analysis of resonance lineshapes. However, applications...
19.
Deckert A, Waudby C, Wlodarski T, Wentink A, Wang X, Kirkpatrick J, et al.
Proc Natl Acad Sci U S A
. 2016 Apr;
113(18):5012-7.
PMID: 27092002
The ribosome is increasingly becoming recognized as a key hub for integrating quality control processes associated with protein biosynthesis and cotranslational folding (CTF). The molecular mechanisms by which these processes...
20.
Cabrita L, Cassaignau A, Launay H, Waudby C, Wlodarski T, Camilloni C, et al.
Nat Struct Mol Biol
. 2016 Mar;
23(4):278-285.
PMID: 26926436
Although detailed pictures of ribosome structures are emerging, little is known about the structural and cotranslational folding properties of nascent polypeptide chains at the atomic level. Here we used solution-state...