Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Youhna M. Ayala"'
Autor:
Francisco E. Baralle, James R. Tollervey, Andrea D’Ambrogio, Maurizio Romano, Ashish Dhir, Youhna M. Ayala, Laura De Conti, S. Eréndira Avendaño-Vázquez, Marco Baralle, Jernej Ule, Emanuele Buratti
Publikováno v:
The EMBO Journal. 30:277-288
TAR DNA-binding protein (TDP-43) is an evolutionarily conserved heterogeneous nuclear ribonucleoprotein (hnRNP) involved in RNA processing, whose abnormal cellular distribution and post-translational modification are key markers of certain neurodegen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0d04fbf29246c725c24ba638c37baa51
https://doi.org/10.1038/emboj.2010.310
https://doi.org/10.1038/emboj.2010.310
Autor:
Emanuele Buratti, Youhna M. Ayala, Antonia Brindisi, Francisco E. Baralle, Maurizio Giombi, Sergio Tisminetzky
Publikováno v:
Journal of Biological Chemistry. 280:37572-37584
TDP-43 is a highly conserved nuclear factor of yet unknown function that binds to ug-repeated sequences and is responsible for cystic fibrosis transmembrane conductance regulator exon 9 splicing inhibition. We have analyzed TDP-43 interactions with o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d9455083470fa7e9b8a20f7c7ff87c7d
https://doi.org/10.1074/jbc.m505557200
https://doi.org/10.1074/jbc.m505557200
Autor:
Enrico Di Cera, Youhna M. Ayala
Publikováno v:
Protein Science. 9:1589-1593
A simple method is presented for the determination of individual rate constants for substrate hydrolysis by serine proteases and other enzymes with similar catalytic mechanism. The method does not require solvent perturbation like viscosity changes,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f372876ad1a1b39ec6a424ce9ad3d0d
https://doi.org/10.1110/ps.9.8.1589
https://doi.org/10.1110/ps.9.8.1589
Publikováno v:
Journal of Biological Chemistry. 272:1440-1443
The PhoP/PhoQ two-component regulatory system governs several virulence properties in the Gram-negative bacterium Salmonella typhimurium. The PhoQ protein is a Mg2+ and Ca2+ sensor that modulates transcription of PhoP-regulated genes in response to t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::74cebbcc033c6fce52c77278a9ade786
https://doi.org/10.1074/jbc.272.3.1440
https://doi.org/10.1074/jbc.272.3.1440
Publikováno v:
Molecular and Biochemical Parasitology. 83:247-251
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7b5ee6bdb1740483da6dfd089997bba
https://doi.org/10.1016/s0166-6851(96)02768-5
https://doi.org/10.1016/s0166-6851(96)02768-5
Autor:
Murad Nayal, Alessandro Vindigni, Enrico Di Cera, Youhna M. Ayala, Spolar Rs, Thomas M. Record
Publikováno v:
Journal of Molecular Biology. 253:787-798
Temperature dependent studies of the interaction of the clotting enzyme thrombin with the potent natural inhibitor hirudin reveal a large negative heat capacity change of -1.7(+/- 0.2) kcal/mol per K associated with the formation of the thrombin-hiru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d73a412ffb7e7e8d0acea0111aa20649
https://doi.org/10.1006/jmbi.1995.0591
https://doi.org/10.1006/jmbi.1995.0591
Autor:
Alexander Tulinsky, Enriqueta R. Guinto, Meng Wuyi, Alessandro Vindigni, Quoc D. Dang, Enrico Di Cera, Youhna M. Ayala
Publikováno v:
Journal of Biological Chemistry. 270:22089-22092
Thrombin is an allosteric serine protease existing in two forms, slow and fast, targeted toward anticoagulant and procoagulant activities. The slow --fast transition is induced by Na+ binding to a site contained within a cylindrical cavity formed by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b50848d478ac9fbaade76cd4c088b397
https://doi.org/10.1074/jbc.270.38.22089
https://doi.org/10.1074/jbc.270.38.22089
Autor:
Maurizio Romano, Andrea D’Ambrogio, Emanuele Buratti, Cristiana Stuani, Corrado Guarnaccia, Francisco E. Baralle, Youhna M. Ayala
Publikováno v:
Nucleic Acids Research
Nuclear factor TDP-43 has been reported to play multiple roles in transcription, pre-mRNA splicing, mRNA stability and mRNA transport. From a structural point of view, TDP-43 is a member of the hnRNP protein family whose structure includes two RRM do
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cb7a860e0a6498b8296cd27b8e7e960
https://hdl.handle.net/11368/2288462
https://hdl.handle.net/11368/2288462
Autor:
Leonard Petrucelli, Andrea D’Ambrogio, Youhna M. Ayala, Paola Zago, Emanuele Buratti, Ya Fei Xu, Francisco E. Baralle
Publikováno v:
Journal of cell science. 121(Pt 22)
TDP-43 (also known as TARDBP) regulates different processes of gene expression, including transcription and splicing, through RNA and DNA binding. Moreover, recent reports have shown that the protein interacts with the 3′UTRs of specific mRNAs. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86f59927a976e758da8ca2e35a5d6943
https://pubmed.ncbi.nlm.nih.gov/18957508
https://pubmed.ncbi.nlm.nih.gov/18957508
TDP-43 (for T AR D NA binding p rotein) is a highly conserved heterogeneous nuclear ribonucleoprotein (hnRNP) involved in specific pre-mRNA splicing and transcription events. TDP-43 recently has been identified as the main component of cytoplasmic in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea1b90bcf0f439361309ce65430f8959
https://europepmc.org/articles/PMC2268791/
https://europepmc.org/articles/PMC2268791/