C Cullin
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Explore the profile of C Cullin including associated specialties, affiliations and a list of published articles.
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28
Citations
1029
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Recent Articles
1.
Ewald M, Henry S, Lambert E, Feuillie C, Bobo C, Cullin C, et al.
Nanoscale
. 2019 Mar;
11(15):7229-7238.
PMID: 30924478
Due to an aging population, neurodegenerative diseases have become a major health issue, the most common being Alzheimer's disease. The mechanisms leading to neuronal loss still remain unclear but recent...
2.
Henry S, Bercu N, Bobo C, Cullin C, Molinari M, Lecomte S
Nanoscale
. 2018 Jan;
10(3):936-940.
PMID: 29292465
Toxicity of Aβ peptides involved in Alzheimer's disease is linked to the interaction of intermediate species with membranes. Nanoscale Infrared Spectroscopy enhances the study of the morphology and the secondary...
3.
Mendoza O, Calmet P, Alves I, Lecomte S, Raoux M, Cullin C, et al.
Nanoscale
. 2017 Jul;
9(27):9762-9769.
PMID: 28678234
Control of transport across membranes, whether natural or synthetic, is fundamental in many biotechnology applications, including sensing and drug release. Mutations of naturally existing protein channels, such as hemolysin, have...
4.
Vignaud H, Cullin C, Bouchecareilh M
Rev Mal Respir
. 2015 Sep;
32(10):1059-71.
PMID: 26386628
Chronic obstructive pulmonary disease (COPD) is currently the ninth leading cause of death in France and is predicted to become the third leading cause of worldwide morbidity and mortality by...
5.
Hatin I, Bidou L, Cullin C, Rousset J
Cell Mol Biol (Noisy-le-grand)
. 2002 Apr;
47 Online Pub:OL23-8.
PMID: 11936870
A prion is an infectious, altered form of a cellular protein which can self-propagate and affect normal phenotype. Prion conversion has been observed for mammalian and yeast proteins but molecular...
6.
Cullin C
Cell Mol Life Sci
. 2002 Jan;
58(12-13):1857-78.
PMID: 11766884
The yeast prions represent a very attractive and tractable model for investigating the prion world. The more extensively studied yeast prion [PSI] leads to a propagation model that links auto-aggregation...
7.
Thual C, Bousset L, Komar A, Walter S, Buchner J, Cullin C, et al.
Biochemistry
. 2001 May;
40(6):1764-73.
PMID: 11327838
The [URE3] factor of Saccharomyces cerevisiae propagates by a prion-like mechanism and corresponds to the loss of the function of the cellular protein Ure2. The molecular basis of the propagation...
8.
Guillemet E, Cullin C
EMBO J
. 2000 Jul;
19(13):3215-22.
PMID: 10880435
The non-Mendelian element [URE3] of yeast is considered to be a prion form of the Ure2 protein. The [URE3] phenotype occurs at a frequency of 10(-5) in haploid yeast strains,...
9.
Komar A, Melki R, Cullin C
Biochemistry (Mosc)
. 2000 Jan;
64(12):1401-7.
PMID: 10648964
[URE3] is a non-Mendelian genetic element of the yeast Saccharomyces cerevisiae, an altered prion form of Ure2 protein. We show that recombinant Ure2p is a soluble protein that can assemble...
10.
Thual C, Komar A, Bousset L, Cullin C, Melki R
J Biol Chem
. 1999 May;
274(19):13666-74.
PMID: 10224139
Sacchromyces cerevisiae prion-like protein Ure2 was expressed in Escherichia coli and was purified to homogeneity. We show here that Ure2p is a soluble protein that can assemble into fibers that...