Deciphering the Structural Basis That Guides the Oxidative Folding of Leech-derived Tryptase Inhibitor

Oxidative Folding Pathway of Onconase, a Ribonuclease Homologue: Insight into Oxidative Folding Mechanisms from a Study of Two Homologues†

(2009) Robert F. Gahl et al.   BIOCHEMISTRY

The NMR Structures of the Major Intermediates of the Two-domain Tick Carboxypeptidase Inhibitor Reveal Symmetry in Its Folding and Unfolding Pathways

(2008) Joan L. Arolas et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Structure of a Two-Disulfide Intermediate Assists in Elucidating the Oxidative Folding Pathway of a Cyclic Cystine Knot Protein

(2008) Maša Cemazar et al.   STRUCTURE

Oxidative Folding of Leech-Derived Tryptase Inhibitor Via Native Disulfide-Bonded Intermediates

(2007) Joan L. Arolas et al.   ANTIOXIDANTS & REDOX SIGNALING

Diversity of Folding Pathways and Folding Models of Disulfide Proteins

(2007) Jui-Yoa Chang   ANTIOXIDANTS & REDOX SIGNALING

Solution structure of the rhodanese homology domain At4g01050(175-295) from Arabidopsis thaliana

(2004) David Pantoja-Uceda et al.   PROTEIN SCIENCE