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pro vyhledávání: '"Fourier Transform IR (FTIR)"'
Akademický článek
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Autor:
Tzu-Chun Tang, Stefan N. Constantinescu, Florian Perrin, Jean-Noël Octave, Pascal Kienlen-Campard, Steven O. Smith, Rémi Opsomer, Yi Hu
Publikováno v:
The Journal of biological chemistry, Vol. 294, no. 15, p. 5854-5866 (2019)
Extracellular deposition of β-amyloid (Aβ) peptides in the brain is a hallmark of Alzheimer's disease (AD). Upon β-secretase–mediated cleavage of the β C-terminal fragment (β-CTF) from the Aβ precursor protein, the γ-secretase complex produc
Autor:
Erika Ponzini, Frank Sobott, Antonino Natalello, Rossana Rossi, Rita Grandori, Antonella De Palma, Lucilla Cerboni, Carlo Santambrogio, Pierluigi Mauri, Giuseppe Legname, Rani Moons, Joanna Narkiewicz, Albert Konijnenberg
Publikováno v:
Journal of biological chemistry
The Journal of biological chemistry
Apr 5;294(14) (2019): 5657–5665. doi:10.1074/jbc.RA118.001907
info:cnr-pdr/source/autori:Erika Ponzini1, Antonella De Palma2, Lucilla Cerboni1, Antonino Natalello3, Rossana Rossi4, Rani Moons5, Albert Konijnenberg5, Joanna Narkiewicz6, Giuseppe Antonio Legname7, Frank Sobott8, Pierluigi Mauri4, Carlo Santambrogio1* and Rita Grandori9/titolo:Methionine oxidation in ?-synuclein inhibits its propensity for ordered secondary structure/doi:10.1074%2Fjbc.RA118.001907/rivista:The Journal of biological chemistry (Print)/anno:2019/pagina_da:5657/pagina_a:5665/intervallo_pagine:5657–5665/volume:Apr 5;294(14)
Journal of biological chemistry (Online) 294 (2019): 5657–5665. doi:10.1074/jbc.RA118.001907
info:cnr-pdr/source/autori:Ponzini E, De Palma A, Cerboni L, Natalello A, Rossi R, Moons R, Konijnenberg A, Narkiewicz J, Legname G, Sobott F, Mauri P, Santambrogio C, Grandori R./titolo:Methionine oxidation in ?-synuclein inhibits its propensity for ordered secondary structure/doi:10.1074%2Fjbc.RA118.001907/rivista:Journal of biological chemistry (Online)/anno:2019/pagina_da:5657/pagina_a:5665/intervallo_pagine:5657–5665/volume:294
The Journal of biological chemistry
Apr 5;294(14) (2019): 5657–5665. doi:10.1074/jbc.RA118.001907
info:cnr-pdr/source/autori:Erika Ponzini1, Antonella De Palma2, Lucilla Cerboni1, Antonino Natalello3, Rossana Rossi4, Rani Moons5, Albert Konijnenberg5, Joanna Narkiewicz6, Giuseppe Antonio Legname7, Frank Sobott8, Pierluigi Mauri4, Carlo Santambrogio1* and Rita Grandori9/titolo:Methionine oxidation in ?-synuclein inhibits its propensity for ordered secondary structure/doi:10.1074%2Fjbc.RA118.001907/rivista:The Journal of biological chemistry (Print)/anno:2019/pagina_da:5657/pagina_a:5665/intervallo_pagine:5657–5665/volume:Apr 5;294(14)
Journal of biological chemistry (Online) 294 (2019): 5657–5665. doi:10.1074/jbc.RA118.001907
info:cnr-pdr/source/autori:Ponzini E, De Palma A, Cerboni L, Natalello A, Rossi R, Moons R, Konijnenberg A, Narkiewicz J, Legname G, Sobott F, Mauri P, Santambrogio C, Grandori R./titolo:Methionine oxidation in ?-synuclein inhibits its propensity for ordered secondary structure/doi:10.1074%2Fjbc.RA118.001907/rivista:Journal of biological chemistry (Online)/anno:2019/pagina_da:5657/pagina_a:5665/intervallo_pagine:5657–5665/volume:294
alpha-Synuclein (AS) is an intrinsically disordered protein highly expressed in dopaminergic neurons. Its amyloid aggregates are the major component of Lewy bodies, a hallmark of Parkinson's disease (PD). AS is particularly exposed to oxidation of it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8415707babbd98a8f4da97e49c9f805f
http://hdl.handle.net/10281/270132
http://hdl.handle.net/10281/270132
Publikováno v:
Journal of Biological Chemistry. 292:20046-20057
In photosynthetic water oxidation, two water molecules are converted into one oxygen molecule and four protons at the Mn4CaO5 cluster in photosystem II (PSII) via the S-state cycle. Efficient proton exit from the catalytic site to the lumen is essent
Autor:
Ponzini, E, Santambrogio, C, Bianchi, G, Brocca, S, Natalello, A, Rossi, R, De Palma, A, Mauri, PL, Grandori, R
Mass spectrometry (MS) has developed into a central tool of biochemistry and structural biology. The so-called “native” MS, based on nano-electrospray-ionization (nano-ESI), has paved the way to protein folding and binding studies by MS technique
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______1299::42b0e16cf3a52e41941ac7fcc800724d
http://hdl.handle.net/10281/279828
http://hdl.handle.net/10281/279828
Autor:
Yamazaki, Yoichi, Nagata, Tomoko, Terakita, Akihisa, Kandori, Hideki, Shichida, Yoshinori, Imamoto, Yasushi
Publikováno v:
The Journal of biological chemistry. 289(20):13792-13800
Rhodopsin undergoes rearrangements of its transmembrane helices after photon absorption to transfer a light signal to the G-protein transducin. To investigate the mechanism by which rhodopsin adopts the transducin-activating conformation, the local e
Autor:
Natalello, Antonino, Mangione, P. Patrizia, Giorgetti, Sofia, Porcari, Riccardo, Marchese, Loredana, Zorzoli, Irene, Relini, Annalisa, Ami, Diletta, Faravelli, Giulia, Valli, Maurizia, Stoppini, Monica, Doglia, Silvia M., Bellotti, Vittorio, Raimondi, Sara
Publikováno v:
The Journal of Biological Chemistry
The amyloidogenic variant of β2-microglobulin, D76N, can readily convert into genuine fibrils under physiological conditions and primes in vitro the fibrillogenesis of the wild-type β2-microglobulin. By Fourier transformed infrared spectroscopy, we
Autor:
Langlois, Chantal, Ramboarina, Stéphanie, Cukkemane, Abhishek, Auzat, Isabelle, Chagot, Benjamin, Gilquin, Bernard, Ignatiou, Athanasios, Petitpas, Isabelle, Kasotakis, Emmanouil, Paternostre, Maïté, White, Helen E., Orlova, Elena V., Baldus, Marc, Tavares, Paulo, Zinn-Justin, Sophie, Sub NMR Spectroscopy, NMR Spectroscopy
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (6), pp.3836-49. ⟨10.1074/jbc.M114.613166⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (6), pp.3836-49. 〈10.1074/jbc.M114.613166〉
Journal of Biological Chemistry, 2015, 290 (6), pp.3836-49. ⟨10.1074/jbc.M114.613166⟩
Journal of Biological Chemistry, 290(6), 3836. American Society for Biochemistry and Molecular Biology Inc.
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (6), pp.3836-49. ⟨10.1074/jbc.M114.613166⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (6), pp.3836-49. 〈10.1074/jbc.M114.613166〉
Journal of Biological Chemistry, 2015, 290 (6), pp.3836-49. ⟨10.1074/jbc.M114.613166⟩
Journal of Biological Chemistry, 290(6), 3836. American Society for Biochemistry and Molecular Biology Inc.
International audience; The majority of known bacteriophages have long tails that serve for bacterial target recognition and viral DNA delivery into the host. These structures form a tube from the viral capsid to the bacterial cell. The tube is forme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba83a58262b0a3f3c80a8a020d0500b8
https://hal.archives-ouvertes.fr/hal-01449521
https://hal.archives-ouvertes.fr/hal-01449521
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Akademický článek
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