15N Relaxation NMR Studies of Prolyl Oligopeptidase, an 80 kDa Enzyme, Reveal a Pre-existing Equilibrium between Different Conformational States

Induced-fit Mechanism for Prolyl Endopeptidase

(2010) Min Li et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Inhibitors of Prolyl Oligopeptidases for the Therapy of Human Diseases: Defining Diseases and Inhibitors

(2010) Janice Lawandi et al.   JOURNAL OF MEDICINAL CHEMISTRY

Proteins in dynamic equilibrium

(2010) Pau Bernadó et al.   NATURE

A Cost-Effective Labeling Strategy for the NMR Study of Large Proteins: Selective15N-Labeling of the Tryptophan Side Chains of Prolyl Oligopeptidase

(2009) Teresa Tarragó et al.   CHEMBIOCHEM

Issues About the Physiological Functions of Prolyl Oligopeptidase Based on Its Discordant Spatial Association With Substrates and Inconsistencies Among mRNA, Protein Levels, and Enzymatic Activity

(2009) Timo T. Myöhänen et al.   JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY

Prolyl oligopeptidase binds to GAP-43 and functions without its peptidase activity

(2009) Elena Di Daniel et al.   MOLECULAR AND CELLULAR NEUROSCIENCE

NMR analysis of G-protein    subunit complexes reveals a dynamic G -G   subunit interface and multiple protein recognition modes

(2009) A. V. Smrcka et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Recognition Dynamics Up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution

(2008) O. F. Lange et al.   SCIENCE