Area of research
Molecular Biology · Genetics
Research interest
Research interests include Bacterial Genetics and Biotechnology, RNA and protein synthesis mechanisms, Protein Structure and Dynamics, and Enzyme Structure and Function.
An asymmetric nautilus-like HflK/C assembly controls FtsH proteolysis of membrane proteins
Regulation of the Essential Transmembrane AAA+ Protease FtsH by HflK/C Oligomeric Assembly
How the double-ring ClpAP protease motor grips the substrate to unfold and degrade stable proteins
A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation
Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis
Division of labor between the pore-1 loops of the D1 and D2 AAA+ rings coordinates substrate selectivity of the ClpAP protease
Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate
Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates
Mitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding
The Non-dominant AAA+ Ring in the ClpAP Protease Functions as an Anti-stalling Motor to Accelerate Protein Unfolding and Translocation
Multistep substrate binding and engagement by the AAA+ ClpXP protease
Regulation of Antimycin Biosynthesis Is Controlled by the ClpXP Protease
Roles of the ClpX IGF loops in ClpP association, dissociation, and protein degradation
Interactions between a subset of substrate side chains and AAA+ motor pore loops determine grip during protein unfolding
Mechanical Protein Unfolding and Degradation
Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme
N domain of the Lon AAA+ protease controls assembly and substrate choice
Hinge–Linker Elements in the AAA+ Protein Unfoldase ClpX Mediate Intersubunit Communication, Assembly, and Mechanical Activity
Mutation in human <i>CLPX</i> elevates levels of <i>δ-</i> aminolevulinate synthase and protoporphyrin IX to promote erythropoietic protoporphyria
Effect of directional pulling on mechanical protein degradation by ATP-dependent proteolytic machines
Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation
Two Isoforms of Clp Peptidase in Pseudomonas aeruginosa Control Distinct Aspects of Cellular Physiology
Highly Dynamic Interactions Maintain Kinetic Stability of the ClpXP Protease During the ATP-Fueled Mechanical Cycle
Structural Basis of an N-Degron Adaptor with More Stringent Specificity
A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis
Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines
Mitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis
Coordinated gripping of substrate by subunits of a AAA+ proteolytic machine
Dissection of Axial-Pore Loop Function during Unfolding and Translocation by a AAA+ Proteolytic Machine
Oxidization without substrate unfolding triggers proteolysis of the peroxide-sensor, PerR