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• Protein Folding and Role of Molecular Chaperones

• Inhibition of the Human Hsc70 System by Small Ligands as a Potential Anticancer Approach

  L. Dublang, J. Underhaug, M. I. Flydal, L. Velasco-Carneros, J.-D. Maréchal, F. Moro, M. D. Boyano, A. Martinez, A. Muga

  Cancers (Basel). 2021, 13, DOI 10.3390/cancers13122936 (2021)

• Extraction and Refolding Determinants of Chaperone-Driven Aggregated Protein Reactivation

  Fernández-Higuero JA, Muga A, Vilar JMG.

  J Mol Biol. 432(10):3239-3250. (2020) doi: 10.1016/j.jmb.2020.03.002. (2020)

• 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)

• Structural insights into the ability of nucleoplasmin to assemble and chaperone histone octamers for DNA deposition

  Franco A, Arranz R, Fernández-Rivero N, Velázquez-Campoy A, Martín-Benito J, Segura J, Prado A, Valpuesta JM, Muga A.

  Sci Rep. 9(1):9487. doi: 10.1038/s41598-019-45726-7. (2019)

• 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)

• Structural and functional insights on the roles of molecular chaperones in the mistargeting and aggregation phenotypes associated with primary hyperoxaluria type I

  Fernández-Higuero JÁ, Betancor-Fernández I, Mesa-Torres N, Muga A, Salido E, Pey AL

  Adv Protein Chem Struct Biol 114:119-152. doi:10.1016/bs.apcsb.2018.09.003. (2019)

• 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)

• 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)

• A quantitative characterization of nucleoplasmin/histone complexes reveals chaperone versatility

  N. Fernandez-Rivero, A. Franco, A, Velazquez-Campoy, E. Alonso, A. Muga and A. Prado

  Sci Rep. 6, 32114 doi.10.1038/srep 32114 (2016)

• 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)

• 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)

• 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)

• 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)

• 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).

• The intrinsically disordered distal face of nucleoplasmin recognizes distinct oligomerization states of histones.

  I. Ramos, N. Fernández-Rivero, R. Arranz, K. Aloria, R. Finn, J.M. Arizmendi, J. Ausió, J.M. Valpuesta, A. Muga and A. Prado.

  Nucleic Acids Res. 42, 1311-1325 (2014).

• 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).

• 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).

• The effect of amyloidogenic peptides on bacterial aging correlates with their intrinsic aggregation propensity.

  A. Villar-Pique, N.S. de Groot, R. Sabaté, S.P. Acebrón, G. Celaya, X. Fernández-Busquets, A. Muga and S. Ventura.

  J. Mol. Biol. 421, 270-281 (2012).