Publicaciones en colaboración con investigadores/as de University of Cambridge (12)

2016

  1. Biosynthesis of the acetyl-coA carboxylase-inhibiting antibiotic, andrimid in Serratia is regulated by hfq and the LysR-type transcriptional regulator, admX

    Environmental Microbiology, Vol. 18, Núm. 11, pp. 3635-3650

  2. Conformational dynamics is key to understanding loss-of-function of NQO1 cancer-associated polymorphisms and its correction by pharmacological ligands

    Scientific Reports, Vol. 6

2004

  1. The long and short flavodoxins: II. The role of the differentiating loop in apoflavodoxin stability and folding mechanism

    Journal of Biological Chemistry, Vol. 279, Núm. 45, pp. 47184-47191

2003

  1. Characterization of single-tryptophan mutants of histidine-containing phosphocarrier protein: Evidence for local rearrangements during folding from high concentrations of denaturant

    Biochemistry, Vol. 42, Núm. 17, pp. 4883-4895

1995

  1. A Calorimetric Study of the Thermal Stability of Barstar and its Interaction with Barnase

    Biochemistry, Vol. 34, Núm. 15, pp. 5224-5233

  2. Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway

    Journal of Molecular Biology, Vol. 254, Núm. 5, pp. 968-979

  3. Folding of a nascent polypeptide chain in vitro: Cooperative formation of structure in a protein module

    Proceedings of the National Academy of Sciences of the United States of America, Vol. 92, Núm. 9, pp. 3683-3686

  4. Protein Fragments as Models for Events in Protein Folding Pathways: Protein Engineering Analysis of the Association of Two Complementary Fragments of the Barley Chymotrypsin Inhibitor 2 (CI-2)

    Biochemistry, Vol. 34, Núm. 5, pp. 1695-1701

  5. Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2

    Journal of Molecular Biology, Vol. 254, Núm. 2, pp. 289-304

1994

  1. A Calorimetric Study of the Thermal Stability of Barnase and Its Interaction with 3′GMP

    Biochemistry, Vol. 33, Núm. 13, pp. 3919-3926

  2. Generation of a Family of Protein Fragments for Structure-Folding Studies. 2. Kinetics of Association of the Two Chymotrypsin Inhibitor-2 Fragments

    Biochemistry, Vol. 33, Núm. 25, pp. 7964-7970

  3. The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: Implications for mechanisms of protein folding

    Proceedings of the National Academy of Sciences of the United States of America, Vol. 91, Núm. 23, pp. 10943-10946