Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities

Processive Degradation of Unstructured Protein by Escherichia coli Lon Occurs via the Slow, Sequential Delivery of Multiple Scissile Sites Followed by Rapid and Synchronized Peptide Bond Cleavage Events

(2013) Natalie Mikita et al.   BIOCHEMISTRY

Utilization of positional isotope exchange experiments to evaluate reversibility of ATP hydrolysis catalyzed by Escherichia coli Lon proteaseThis paper is one of a selection of papers published in this special issue entitled 8th International Conference on AAA Proteins and has undergone the Journal's usual peer review process.

(2010) Jennifer Thomas et al.   Biochemistry and Cell Biology

Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber

(2010) Sun-Shin Cha et al.   EMBO JOURNAL

Crystal Structures of Bacillus subtilis Lon Protease

(2010) Ramona E. Duman et al.   JOURNAL OF MOLECULAR BIOLOGY

Utilization of synthetic peptides to evaluate the importance of substrate interaction at the proteolytic site of Escherichia coli Lon protease

(2009) Jessica Patterson-Ward et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates

(2008) Irene Lee et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Recent developments in the MAFFT multiple sequence alignment program

(2008) K. Katoh et al.   BRIEFINGS IN BIOINFORMATICS

GROMACS 4:  Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation

(2008) Berk Hess et al.   Journal of Chemical Theory and Computation