Moro F - Search Results

1

A Targetable N-Terminal Motif Orchestrates α-Synuclein Oligomer-to-Fibril Conversion.

Santos J, Cuellar J, Pallarès I, Byrd EJ, Lends A, Moro F, Abdul-Shukkoor MB, Pujols J, Velasco-Carneros L, Sobott F, Otzen DE, Calabrese AN, Muga A, Pedersen JS, Loquet A, Valpuesta JM, Radford SE, Ventura S. Santos J, et al. Among authors: moro f. J Am Chem Soc. 2024 May 8;146(18):12702-12711. doi: 10.1021/jacs.4c02262. Epub 2024 Apr 29. J Am Chem Soc. 2024. PMID: 38683963 Free PMC article.

2

Interdomain interaction through helices A and B of DnaK peptide binding domain.

Moro F, Fernández V, Muga A. Moro F, et al. FEBS Lett. 2003 Jan 2;533(1-3):119-23. doi: 10.1016/s0014-5793(02)03752-3. FEBS Lett. 2003. PMID: 12505170 Free article.

3

The lid subdomain of DnaK is required for the stabilization of the substrate-binding site.

Moro F, Fernández-Sáiz V, Muga A. Moro F, et al. J Biol Chem. 2004 May 7;279(19):19600-6. doi: 10.1074/jbc.M400921200. Epub 2004 Feb 25. J Biol Chem. 2004. PMID: 14985342 Free article.

4

Conformational properties of bacterial DnaK and yeast mitochondrial Hsp70. Role of the divergent C-terminal alpha-helical subdomain.

Moro F, Fernández-Sáiz V, Slutsky O, Azem A, Muga A. Moro F, et al. FEBS J. 2005 Jun;272(12):3184-96. doi: 10.1111/j.1742-4658.2005.04737.x. FEBS J. 2005. PMID: 15955075 Free article.

5

The allosteric transition in DnaK probed by infrared difference spectroscopy. Concerted ATP-induced rearrangement of the substrate binding domain.

Moro F, Fernández-Sáiz V, Muga A. Moro F, et al. Protein Sci. 2006 Feb;15(2):223-33. doi: 10.1110/ps.051732706. Epub 2005 Dec 29. Protein Sci. 2006. PMID: 16384998 Free PMC article.

6

Ionic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics.

Fernández-Sáiz V, Moro F, Arizmendi JM, Acebrón SP, Muga A. Fernández-Sáiz V, et al. Among authors: moro f. J Biol Chem. 2006 Mar 17;281(11):7479-88. doi: 10.1074/jbc.M512744200. Epub 2006 Jan 16. J Biol Chem. 2006. PMID: 16415343 Free article.

7

Thermal adaptation of the yeast mitochondrial Hsp70 system is regulated by the reversible unfolding of its nucleotide exchange factor.

Moro F, Muga A. Moro F, et al. J Mol Biol. 2006 May 19;358(5):1367-77. doi: 10.1016/j.jmb.2006.03.027. Epub 2006 Mar 29. J Mol Biol. 2006. PMID: 16600294

8

GrpE N-terminal domain contributes to the interaction with Dnak and modulates the dynamics of the chaperone substrate binding domain.

Moro F, Taneva SG, Velázquez-Campoy A, Muga A. Moro F, et al. J Mol Biol. 2007 Dec 7;374(4):1054-64. doi: 10.1016/j.jmb.2007.10.002. Epub 2007 Oct 5. J Mol Biol. 2007. PMID: 17976642

9

DnaJ recruits DnaK to protein aggregates.

Acebrón SP, Fernández-Sáiz V, Taneva SG, Moro F, Muga A. Acebrón SP, et al. Among authors: moro f. J Biol Chem. 2008 Jan 18;283(3):1381-1390. doi: 10.1074/jbc.M706189200. Epub 2007 Nov 5. J Biol Chem. 2008. PMID: 17984091 Free article.

10

The structure of CCT-Hsc70 NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin.

Cuéllar J, Martín-Benito J, Scheres SH, Sousa R, Moro F, López-Viñas E, Gómez-Puertas P, Muga A, Carrascosa JL, Valpuesta JM. Cuéllar J, et al. Among authors: moro f. Nat Struct Mol Biol. 2008 Aug;15(8):858-64. doi: 10.1038/nsmb.1464. Epub 2008 Jul 27. Nat Struct Mol Biol. 2008. PMID: 18660820 Free PMC article.

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