Anne Fourest-Lieuvin
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Explore the profile of Anne Fourest-Lieuvin including associated specialties, affiliations and a list of published articles.
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16
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477
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Recent Articles
1.
Serre L, Delaroche J, Vinit A, Schoehn G, Denarier E, Fourest-Lieuvin A, et al.
J Cell Sci
. 2022 Dec;
136(2).
PMID: 36541084
Adenomatous polyposis coli (APC) is a scaffold protein with tumour suppressor properties. Mutations causing the loss of its C-terminal domain (APC-C), which bears cytoskeleton-regulating sequences, correlate with colorectal cancer. The...
2.
Fourest-Lieuvin A, Vinit A, Blot B, Perrot A, Denarier E, Saudou F, et al.
Neuroscience
. 2022 Aug;
518:162-177.
PMID: 35995336
In several forms of dementia, such as Alzheimer's disease, the cytoskeleton-associated protein tau undergoes proteolysis, giving rise to fragments that have a toxic impact on neuronal homeostasis. How these fragments...
3.
Sebastien M, Giannesini B, Aubin P, Brocard J, Chivet M, Pietrangelo L, et al.
Skelet Muscle
. 2018 Sep;
8(1):30.
PMID: 30231928
Background: The skeletal muscle fiber has a specific and precise intracellular organization which is at the basis of an efficient muscle contraction. Microtubules are long known to play a major...
4.
Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles
Prezel E, Elie A, Delaroche J, Stoppin-Mellet V, Bosc C, Serre L, et al.
Mol Biol Cell
. 2017 Nov;
29(2):154-165.
PMID: 29167379
In neurons, microtubule networks alternate between single filaments and bundled arrays under the influence of effectors controlling their dynamics and organization. Tau is a microtubule bundler that stabilizes microtubules by...
5.
Ramirez-Rios S, Serre L, Stoppin-Mellet V, Prezel E, Vinit A, Courriol E, et al.
Methods Cell Biol
. 2017 Sep;
141:179-197.
PMID: 28882301
Tau is a major microtubule-associated protein (MAP) mainly expressed in the brain. Tau binds the lattice of microtubules and favors their elongation and bundling. Recent studies have shown that tau...
6.
Osseni A, Sebastien M, Sarrault O, Baudet M, Coute Y, Faure J, et al.
J Cell Sci
. 2016 Aug;
129(20):3744-3755.
PMID: 27562070
In skeletal muscle, the triad is a structure comprising a transverse (T)-tubule and sarcoplasmic reticulum (SR) cisternae. Triads constitute the basis of excitation-contraction coupling as the cradle of the Ca...
7.
Ramirez-Rios S, Denarier E, Prezel E, Vinit A, Stoppin-Mellet V, Devred F, et al.
Mol Biol Cell
. 2016 Jul;
27(19):2924-34.
PMID: 27466319
Proper regulation of microtubule dynamics is essential for cell functions and involves various microtubule-associated proteins (MAPs). Among them, end-binding proteins (EBs) accumulate at microtubule plus ends, whereas structural MAPs bind...
8.
Elie A, Prezel E, Guerin C, Denarier E, Ramirez-Rios S, Serre L, et al.
Sci Rep
. 2015 May;
5:9964.
PMID: 25944224
The crosstalk between microtubules and actin is essential for cellular functions. However, mechanisms underlying the microtubule-actin organization by cross-linkers remain largely unexplored. Here, we report that tau, a neuronal microtubule-associated...
9.
Rendu J, Brocard J, Denarier E, Monnier N, Pietri-Rouxel F, Beley C, et al.
Hum Gene Ther
. 2013 Jun;
24(7):702-13.
PMID: 23805838
Central core disease is a myopathy often arising from mutations in the type 1 ryanodine receptor (RYR1) gene, encoding the sarcoplasmic reticulum calcium release channel RyR1. No treatment is currently...
10.
Fourest-Lieuvin A, Rendu J, Osseni A, Pernet-Gallay K, Rossi D, Oddoux S, et al.
J Cell Sci
. 2012 Apr;
125(Pt 14):3443-53.
PMID: 22505613
The terminal cisternae represent one of the functional domains of the skeletal muscle sarcoplasmic reticulum (SR). They are closely apposed to plasma membrane invaginations, the T-tubules, with which they form...