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Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption.
De Los Rios P, Barducci A. De Los Rios P, et al. Among authors: barducci a. Elife. 2014 May 27;3:e02218. doi: 10.7554/eLife.02218. Elife. 2014. PMID: 24867638 Free PMC article.
70-kDa Heat shock proteins are ATP-driven molecular chaperones that perform a myriad of essential cellular tasks. Although structural and biochemical studies have shed some light on their functional mechanism, the fundamental issue of the role of energy consumption, due to …
70-kDa Heat shock proteins are ATP-driven molecular chaperones that perform a myriad of essential cellular tasks. Although structural …
Free-energy landscape of protein oligomerization from atomistic simulations.
Barducci A, Bonomi M, Prakash MK, Parrinello M. Barducci A, et al. Proc Natl Acad Sci U S A. 2013 Dec 3;110(49):E4708-13. doi: 10.1073/pnas.1320077110. Epub 2013 Nov 18. Proc Natl Acad Sci U S A. 2013. PMID: 24248370 Free PMC article.
In the realm of protein-protein interactions, the assembly process of homooligomers plays a fundamental role because the majority of proteins fall into this category. A comprehensive understanding of this multistep process requires the characterization of the drivin …
In the realm of protein-protein interactions, the assembly process of homooligomers plays a fundamental role because the majority of …
Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.
Kellner R, Hofmann H, Barducci A, Wunderlich B, Nettels D, Schuler B. Kellner R, et al. Among authors: barducci a. Proc Natl Acad Sci U S A. 2014 Sep 16;111(37):13355-60. doi: 10.1073/pnas.1407086111. Epub 2014 Aug 27. Proc Natl Acad Sci U S A. 2014. PMID: 25165400 Free PMC article.
We find that in a first step the ATP-independent binding of DnaJ to denatured rhodanese results in a compact denatured ensemble of the substrate protein. The following ATP-dependent binding of multiple DnaK molecules, however, leads to a surprisingly large ex …
We find that in a first step the ATP-independent binding of DnaJ to denatured rhodanese results in a compact denatured ensembl …
Non-equilibrium conformational dynamics in the function of molecular chaperones.
Barducci A, De Los Rios P. Barducci A, et al. Curr Opin Struct Biol. 2015 Feb;30:161-169. doi: 10.1016/j.sbi.2015.02.008. Epub 2015 Mar 13. Curr Opin Struct Biol. 2015. PMID: 25771489 Review.
We argue here that energy consumption must be fully taken into account to understand the mechanism of these intrinsically non-equilibrium machines and we propose a novel perspective in the way the relation between function and ATP hydrolysis is viewed....
We argue here that energy consumption must be fully taken into account to understand the mechanism of these intrinsically non-equilibrium ma …
Quantifying the role of chaperones in protein translocation by computational modeling.
Assenza S, De Los Rios P, Barducci A. Assenza S, et al. Among authors: barducci a. Front Mol Biosci. 2015 Mar 23;2:8. doi: 10.3389/fmolb.2015.00008. eCollection 2015. Front Mol Biosci. 2015. PMID: 25988176 Free PMC article.
The molecular chaperone Hsp70 plays a central role in the import of cytoplasmic proteins into organelles, driving their translocation by binding them from the organellar interior. ...
The molecular chaperone Hsp70 plays a central role in the import of cytoplasmic proteins into organelles, driving their translocation …
Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones.
Malinverni D, Marsili S, Barducci A, De Los Rios P. Malinverni D, et al. Among authors: barducci a. PLoS Comput Biol. 2015 Jun 5;11(6):e1004262. doi: 10.1371/journal.pcbi.1004262. eCollection 2015 Jun. PLoS Comput Biol. 2015. PMID: 26046683 Free PMC article.
Hsp70s are a class of ubiquitous and highly conserved molecular chaperones playing a central role in the regulation of proteostasis in the cell. Hsp70s assist a myriad of cellular processes by binding unfolded or misfolded substrates during a complex b …
Hsp70s are a class of ubiquitous and highly conserved molecular chaperones playing a central role in the regulation of proteos …
Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysis.
Malinverni D, Jost Lopez A, De Los Rios P, Hummer G, Barducci A. Malinverni D, et al. Among authors: barducci a. Elife. 2017 May 12;6:e23471. doi: 10.7554/eLife.23471. Elife. 2017. PMID: 28498104 Free PMC article.
The integration of these complementary approaches resulted in a novel structural model that rationalizes previous experimental observations. We identify an evolutionarily conserved interaction surface formed by helix II of the DnaJ J-domain and a structurally contig …
The integration of these complementary approaches resulted in a novel structural model that rationalizes previous experimental observ …
Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes.
Nillegoda NB, Stank A, Malinverni D, Alberts N, Szlachcic A, Barducci A, De Los Rios P, Wade RC, Bukau B. Nillegoda NB, et al. Among authors: barducci a. Elife. 2017 May 15;6:e24560. doi: 10.7554/eLife.24560. Elife. 2017. PMID: 28504929 Free PMC article.
Hsp70 participates in a broad spectrum of protein folding processes extending from nascent chain folding to protein disaggregation. This versatility in function is achieved through a diverse family of J-protein cochaperones that select substrates for Hsp70. ...
Hsp70 participates in a broad spectrum of protein folding processes extending from nascent chain folding to protein disaggregation. T …
Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins.
Goloubinoff P, Sassi AS, Fauvet B, Barducci A, De Los Rios P. Goloubinoff P, et al. Among authors: barducci a. Nat Chem Biol. 2018 Apr;14(4):388-395. doi: 10.1038/s41589-018-0013-8. Epub 2018 Mar 5. Nat Chem Biol. 2018. PMID: 29507388
Function, evolution, and structure of J-domain proteins.
Kampinga HH, Andreasson C, Barducci A, Cheetham ME, Cyr D, Emanuelsson C, Genevaux P, Gestwicki JE, Goloubinoff P, Huerta-Cepas J, Kirstein J, Liberek K, Mayer MP, Nagata K, Nillegoda NB, Pulido P, Ramos C, De Los Rios P, Rospert S, Rosenzweig R, Sahi C, Taipale M, Tomiczek B, Ushioda R, Young JC, Zimmermann R, Zylicz A, Zylicz M, Craig EA, Marszalek J. Kampinga HH, et al. Among authors: barducci a. Cell Stress Chaperones. 2019 Jan;24(1):7-15. doi: 10.1007/s12192-018-0948-4. Epub 2018 Nov 26. Cell Stress Chaperones. 2019. PMID: 30478692 Free PMC article.
J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recen …
J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying …
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