Imagerie PI2

@article{nokey,

title = {Tau mRNA Metabolism in Neurodegenerative Diseases: A Tangle Journey},

author = {P. J. Da Costa and M. Hamdane and L. Buee and F. Martin},

url = {https://www.mdpi.com/2227-9059/10/2/241/htm},

doi = {10.3390/biomedicines10020241},

year  = {2022},

date = {2022-01-01},

journal = {Biomedicines},

volume = {10},

number = {2},

pages = {241},

abstract = {Tau proteins are known to be mainly involved in regulation of microtubule dynamics. Besides this function, which is critical for axonal transport and signal transduction, tau proteins also have other roles in neurons. Moreover, tau proteins are turned into aggregates and consequently trigger many neurodegenerative diseases termed tauopathies, of which Alzheimerﾒs disease (AD) is the figurehead. Such pathological aggregation processes are critical for the onset of these diseases. Among the various causes of tau protein pathogenicity, abnormal tau mRNA metabolism, expression and dysregulation of tau post-translational modifications are critical steps. Moreover, the relevance of tau function to general mRNA metabolism has been highlighted recently in tauopathies. In this review, we mainly focus on how mRNA metabolism impacts the onset and development of tauopathies. Thus, we intend to portray how mRNA metabolism of, or mediated by, tau is associated with neurodegenerative diseases.},

keywords = {ERIANI, mRNA metabolism, Neurodegenerative Diseases, tau protein, Translation, Unité ARN},

pubstate = {published},

tppubtype = {article}

}

@article{Stupfler2021,

title = {Degradation-independent inhibition of APOBEC3G by HIV-1 Vif protein},

author = {B Stupfler and C Verriez and S Gallois-Montbrun and R Marquet and J C Paillart},

url = {https://www.mdpi.com/1999-4915/13/4/617},

doi = {10.3390/v13040617},

year  = {2021},

date = {2021-01-01},

journal = {Viruses},

volume = {13},

number = {4},

pages = {617},

abstract = {The ubiquitin–proteasome system plays an important role in the cell under normal physiological conditions but also during viral infections. Indeed, many auxiliary proteins from the (HIV-1) divert this system to its own advantage, notably to induce the degradation of cellular restriction factors. For instance, the HIV-1 viral infectivity factor (Vif) has been shown to specifically counteract several cellular deaminases belonging to the apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like (APOBEC3 or A3) family (A3A to A3H) by recruiting an E3-ubiquitin ligase complex and inducing their polyubiquitination and degradation through the proteasome. Although this pathway has been extensively characterized so far, Vif has also been shown to impede A3s through degradation-independent processes, but research on this matter remains limited. In this review, we describe our current knowledge regarding the degradation-independent inhibition of A3s, and A3G in particular, by the HIV-1 Vif protein, the molecular mechanisms involved, and highlight important properties of this small viral protein.},

keywords = {APOBEC3G, deamination, encapsidation, HIV, MARQUET, PAILLART, proteasome, RNP granules, Translation, ubiquitin, Unité ARN, vif},

pubstate = {published},

tppubtype = {article}

}

@article{,

title = {Biomedicine. Do G quartets orchestrate fragile X pathology?},

author = { H. Moine and J. L. Mandel},

year  = {2001},

date = {2001-01-01},

journal = {Science},

volume = {294},

number = {5551},

pages = {2487-8},

note = {0036-8075 

Journal Article},

keywords = {Acid, Analysis, Animals, Array, Binding, Brain/metabolism, Conformation, Crystallography, Expression, Fragile, Gene, Genetic, Human, Messenger/*chemistry/genetics/*metabolism, Mice, Nerve, Nucleic, Oligonucleotide, Protein, Proteins/chemistry/genetics/*metabolism, Regions, Regulation, RNA, Sequence, Sites, structure, Synapses/physiology, Syndrome/genetics/*metabolism, Tertiary, Tissue, Translation, Untranslated, X, X-Ray},

pubstate = {published},

tppubtype = {article}

}