Emerging fields in chaperone proteins: A French workshop.
暂无分享,去创建一个
A. Barducci | F. Ochsenbein | E. Mileo | R. Gillet | P. Genevaux | B. Gontero | C. Garnier | P. Goloubinoff | M. Castanié-Cornet | P. Bordes | M. Ilbert | M. Giudici-Orticoni | G. Richarme | C. Iobbi-Nivol | Olivier Genest
[1] A. Barducci,et al. Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins , 2018, Nature Chemical Biology.
[2] R. Gillet,et al. The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors , 2018, Nucleic acids research.
[3] G. Gerbaud,et al. A Bioresistant Nitroxide Spin Label for In-Cell EPR Spectroscopy: In Vitro and In Oocytes Protein Structural Dynamics Studies. , 2018, Angewandte Chemie.
[4] R. Gillet,et al. A Genetic Tool to Quantify trans-Translation Activity in Vivo. , 2017, Journal of molecular biology.
[5] L. Mourey,et al. Directed evolution of SecB chaperones toward toxin-antitoxin systems , 2017, Proceedings of the National Academy of Sciences.
[6] P. Bouloc,et al. Guanine glycation repair by DJ-1/Park7 and its bacterial homologs , 2017, Science.
[7] G. Hummer,et al. Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysis , 2017, eLife.
[8] V. Méjean,et al. Hsp90 Is Essential under Heat Stress in the Bacterium Shewanella oneidensis. , 2017, Cell reports.
[9] J. Buchner,et al. The HSP90 chaperone machinery , 2017, Nature Reviews Molecular Cell Biology.
[10] O. Lemaire,et al. Chaperones in maturation of molybdoenzymes: Why specific is better than general? , 2017, Bioengineered.
[11] L. Mourey,et al. Chaperone addiction of toxin–antitoxin systems , 2016, Nature Communications.
[12] O. Decaux,et al. Hsp90 directly interacts, in vitro, with amyloid structures and modulates their assembly and disassembly. , 2016, Biochimica et biophysica acta.
[13] P. Forterre,et al. DJ-1 family Maillard deglycases prevent acrylamide formation. , 2016, Biochemical and biophysical research communications.
[14] P. Prevelige,et al. Identification of the Calmodulin-Binding Domains of Fas Death Receptor , 2016, PloS one.
[15] Simone Marsili,et al. Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones , 2015, PLoS Comput. Biol..
[16] R. Guérois,et al. Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork , 2015, Nucleic acids research.
[17] A. Lamouri,et al. Parkinsonism-associated Protein DJ-1/Park7 Is a Major Protein Deglycase That Repairs Methylglyoxal- and Glyoxal-glycated Cysteine, Arginine, and Lysine Residues , 2014, The Journal of Biological Chemistry.
[18] C. Dickey,et al. Targeting Hsp90 and its co-chaperones to treat Alzheimer’s disease , 2014, Expert opinion on therapeutic targets.
[19] P. Genevaux,et al. Chaperone networking facilitates protein targeting to the bacterial cytoplasmic membrane. , 2014, Biochimica et biophysica acta.
[20] L. Gierasch,et al. Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs) , 2014, Chemical reviews.
[21] A. Barducci,et al. Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption , 2014, eLife.
[22] R. Gillet,et al. Trans-translation exposed: understanding the structures and functions of tmRNA-SmpB , 2014, Front. Microbiol..
[23] V. Méjean,et al. Quality control of a molybdoenzyme by the Lon protease , 2013, FEBS letters.
[24] Dana Reichmann,et al. The roles of conditional disorder in redox proteins. , 2013, Current opinion in structural biology.
[25] U. Jakob,et al. Conditional disorder in chaperone action. , 2012, Trends in biochemical sciences.
[26] M. Lorenzi,et al. Conformational Selection Underlies Recognition of a Molybdoenzyme by Its Dedicated Chaperone , 2012, PloS one.
[27] S. Maberly,et al. An intrinsically disordered protein, CP12: jack of all trades and master of the Calvin cycle. , 2012, Biochemical Society transactions.
[28] R. Guérois,et al. Surprising complexity of the Asf1 histone chaperone-Rad53 kinase interaction , 2012, Proceedings of the National Academy of Sciences.
[29] J. Buchner. Bacterial Hsp90 – desperately seeking clients , 2010, Molecular microbiology.
[30] J. Erales,et al. CP12 from Chlamydomonas reinhardtii, a Permanent Specific “Chaperone-like” Protein of Glyceraldehyde-3-phosphate Dehydrogenase , 2009, Journal of Biological Chemistry.
[31] U. Jakob,et al. Bleach Activates a Redox-Regulated Chaperone by Oxidative Protein Unfolding , 2008, Cell.
[32] H. Lilie,et al. The redox-switch domain of Hsp33 functions as dual stress sensor , 2007, Nature Structural &Molecular Biology.
[33] F. Ochsenbein,et al. The histone chaperone Asf1 at the crossroads of chromatin and DNA checkpoint pathways , 2007, Chromosoma.
[34] Jean-Michel Camadro,et al. The small protein CP12: a protein linker for supramolecular complex assembly. , 2003, Biochemistry.
[35] E. Mandelkow,et al. Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[36] J. Finch,et al. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA , 1978, Nature.
[37] R. Guérois,et al. Structural insight into how the human helicase subunit MCM 2 may act as a histone chaperone together with ASF 1 at the replication fork , 2019 .
[38] SchemaGc representaGon. The HSP 90 chaperone machinery , 2019 .
[39] S. Leimkühler,et al. Bacterial molybdoenzymes: old enzymes for new purposes. , 2016, FEMS microbiology reviews.
[40] J. Erales,et al. CP 12 from Chlamydomonas reinhardtii : a permanent specific “ chaperone-like ” protein of glyceraldehyde-3-phosphate dehydrogenase , 2009 .
[41] J. Ellis. Proteins as molecular chaperones , 1987, Nature.