A complex equilibrium among partially unfolded conformations in monomeric transthyretin

Autor: Xinyi Li, Seyyed Abolghasem Ghadami, Fabrizio Chiti, Francesco Bemporad, Stefano Gianni, Simona Conti, Cristina Cecchi, Joel N. Buxbaum

Publikováno v: Biochemistry
Biochemistry, American Chemical Society, 2014, 53 (27), pp.4381-92. ⟨10.1021/bi500430w⟩
Biochemistry, American Chemical Society, 2014, 53 (27), pp.4381-92. <10.1021/bi500430w>

International audience; Aggregation of transthyretin (TTR) is known to be linked to the development of systemic and localized amyloidoses. It also appears that TTR exerts a protective role against aggregation of the Aβ peptide, a process linked to A

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::485dd4b3a0cf330e3c51540f40f26a11
https://pubmed.ncbi.nlm.nih.gov/24945718

pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins

Autor: A. Keith Dunker, Dmitri I. Svergun, Joel L. Sussman, Michele Vendruscolo, Richard W. Kriwacki, Martin Blackledge, Peter E. Wright, Isabella C. Felli, Roberta Pierattelli, Peter Tompa, Pierre Lebrun, Mihaly Varadi, David S. Wishart, Erica Valentini, Simone Kosol, Julie D. Forman-Kay, Vladimir N. Uversky

Publikováno v: Nucleic Acids Research
Nucleic acids symposium series 42(D1), D326-D335 (2014). doi:10.1093/nar/gkt960
Nucleic Acids Research, Oxford University Press, 2014, 42 (Database issue), pp.D326-35
Nucleic Acids Research, 2014, 42 (Database issue), pp.D326-35

International audience; The goal of pE-DB (http://pedb.vib.be) is to serve as an openly accessible database for the deposition of structural ensembles of intrinsically disordered proteins (IDPs) and of denatured proteins based on nuclear magnetic res

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82947363e525f17d72c4034e488d6527
http://hdl.handle.net/2158/836169

High-speed force spectroscopy unfolds titin at the velocity of molecular dynamics simulations.: Experiment meets simulation: HS-FS

Autor: Rico, Felix, Gonzalez, Laura, Casuso, Ignacio, Puig-Vidal, Manel, Scheuring, Simon

Publikováno v: Science
Science, American Association for the Advancement of Science, 2013, 342 (6159), pp.741-3. ⟨10.1126/science.1239764⟩

International audience; The mechanical unfolding of the muscle protein titin by atomic force microscopy was a landmark in our understanding of single-biomolecule mechanics. Molecular dynamics simulations offered atomic-level descriptions of the force

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______212::178b5f0c694fc736eead8721c776301a
https://www.hal.inserm.fr/inserm-01309044/document

The folding pathway of a functionally competent C-terminal domain of nucleophosmin: protein stability and denatured state residual structure

Autor: Chiarella, Federici, Di Matteo, Brunori, Gianni

Publikováno v: Biochemical and Biophysical Research Communications
Biochemical and Biophysical Research Communications, Elsevier, 2013, 435 (1), pp.64-8. ⟨10.1016/j.bbrc.2013.04.038⟩
Biochemical and biophysical research communications
435 (2013): 64–68. doi:10.1016/j.bbrc.2013.04.038
info:cnr-pdr/source/autori:Chiarella, S., Federici, L., Di Matteo, A., Brunori, M., Gianni, S./titolo:The folding pathway of a functionally competent C-terminal domain of nucleophosmin: Protein stability and denatured state residual structure/doi:10.1016%2Fj.bbrc.2013.04.038/rivista:Biochemical and biophysical research communications (Print)/anno:2013/pagina_da:64/pagina_a:68/intervallo_pagine:64–68/volume:435
Biochemical and Biophysical Research Communications, Elsevier, 2013, 435 (1), pp.64-8. <10.1016/j.bbrc.2013.04.038>

International audience; Nucleophosmin (NPM1) is a nucleolar protein implicated in ribosome biogenesis, centrosome duplication and cell cycle control; the NPM1 gene is the most frequent target for mutations in Acute Myeloid Leukemia. Mutations map to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::825f7558afed41997942e37762ccccc5
http://hdl.handle.net/11573/554291

Swapping FAD binding motifs between plastidic and bacterial ferredoxin-NADP(H) reductases

Autor: Alejandro Buschiazzo, Horacio Botti, Eduardo A. Ceccarelli, Matías A. Musumeci

Publikováno v: Biochemistry
Biochemistry, American Chemical Society, 2011, 50 (12), pp.2111-22. ⟨10.1021/bi101772a⟩
Biochemistry, 2011, 50 (12), pp.2111-22. ⟨10.1021/bi101772a⟩

International audience; Plant-type ferredoxin-NADP(H) reductases (FNRs) are grouped in two classes, plastidic with an extended FAD conformation and high catalytic rates and bacterial with a folded flavin nucleotide and low turnover rates. The 112-123

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bdfc6d69dd75582a2dcaa56eaa12a73
https://hal-riip.archives-ouvertes.fr/pasteur-00685048