Fernando Moro
Researcher (UPV/EHU)
Publications
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The Complex Phosphorylation Patterns that Regulate the Activity of Hsp70 and Its Cochaperones
Velasco L, Dublang L, Moro F, Muga A.
Int J Mol Sci 20(17). (2019) pii: E4122. doi: 10.3390/ijms20174122. (2019)
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Regulation of Human Hsc70 ATPase and Chaperone Activities by Apg2: Role of the Acidic Subdomain
Y Cabrera, L Dublang, JA Fernández-Higuero, D Albesa-Jové, M Lucas, AR Viguera, ME Guerin, JMG Vilar, A Muga , F Moro.
J Mol Biol ;431(2):444-461. doi: 10.1016/j.jmb.2018.11.026 (2019)
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Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate
Fernández-Higuero JA, Aguado A, Perales-Calvo J, Moro F, Muga A.
Sci Rep. 2018;8(1):5796. doi: 10.1038/s41598-018-24140-5 (2018)
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Label-Free, Multiplexed, Single-Molecule Analysis of Protein-DNA Complexes with Nanopores
G. Celaya, J. Perales-Calvo, A. Muga, F. Moro and D. Rodriguez-Larrea
ACS Nano 11, 5815-5825 doi: 10.1021/acsnano.7b01434 (2017)
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Crowding modulates the conformation, affinity, and activity of the components of the bacterial disaggregase machinery
G. Celaya, J. A. Fernandez-Higuero, I. Martin, G. Rivas, F. Moro and A. Muga
J Mol Biol. 428, 2474-2487 (2016)
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Chaperone-assisted protein aggregate reactivation: Different solutions for the same problem
Aguado A, Fernandez-Higuero JA, Moro F, Muga A
Arch Biochem Biophys 580: 121-34 (2015)
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Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE
Melero R, Moro F, Perez-Calvo MA, Perales-Calvo J, Quintana-Gallardo L, Llorca O, Muga A, Valpuesta JM
J Biol Chem. 290:10083-92 (2015)
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ClpB dynamics is driven by its ATPase cycle and regulated by the DnaK system and substrate proteins
Aguado A, Fernandez-Higuero JA, Cabrera Y, Moro F, Muga A
Biochem J. 466:561-70 (2015)
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Crowding activates ClpB and enhances its association with DnaK for efficient protein aggregate reactivation
I. Martín, G. Celaya, C. Alfonso, F. Moro, G. Rivas and A. Muga.
Biophys J. 106, 2017-2027 (2014).
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Screening and evaluation of small organic molecules as ClpB inhibitors and potential antimicrobials.
I. Martin, J. Underhaug, G. Celaya, F. Moro, K. Teigen, A. Martinez and A. Muga.
J. Med. Chem. 56, 7177-7189 (2013).
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Structural insights into the chaperone activity of the 40-kDa heat shock protein DnaJ: binding and remodeling of a native substrate.
J. Cuéllar, J. Perales-Calvo, A. Muga, J.M. Valpuesta and F. Moro.
J. Biol. Chem. 288, 15065-15074 (2013).