Area of research
Molecular Biology · Cell Biology
Research interest
Research interests include Heat shock proteins research, Protein Structure and Dynamics, Endoplasmic Reticulum Stress and Disease, and Enzyme Structure and Function.
Allosteric control of the bacterial ClpC/ClpP protease and its hijacking by antibacterial peptides
Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP
Balanced activities of Hsp70 and the ubiquitin proteasome system underlie cellular protein homeostasis
The beauty and complexity of the small heat shock proteins: a report on the proceedings of the fourth workshop on small heat shock proteins
Structural basis of aggregate binding by the AAA+ disaggregase ClpG
Structural basis of aggregate binding by the AAA+ disaggregase ClpG
Antibacterial peptide CyclomarinA creates toxicity by deregulating the Mycobacterium tuberculosis ClpC1–ClpP1P2 protease
Total Synthesis and Biological Evaluation of Modified Ilamycin Derivatives
The cytoprotective sequestration activity of small heat shock proteins is evolutionarily conserved
The Diverse Functions of Small Heat Shock Proteins in the Proteostasis Network
Resisting the Heat: Bacterial Disaggregases Rescue Cells From Devastating Protein Aggregation
Basic mechanism of the autonomous ClpG disaggregase
Disassembly of Tau fibrils by the human Hsp70 disaggregation machinery generates small seeding-competent species
Processive extrusion of polypeptide loops by a Hsp100 disaggregase
The HSP110/HSP70 disaggregation system generates spreading‐competent toxic α‐synuclein species
Chaperone-Mediated Protein Disaggregation Triggers Proteolytic Clearance of Intra-nuclear Protein Inclusions
A recently isolated human commensal <i>Escherichia coli</i> ST10 clone member mediates enhanced thermotolerance and tetrathionate respiration on a P1 phage‐derived IncY plasmid
Publisher Correction: Processive extrusion of polypeptide loops by a Hsp100 disaggregase
Cellular Functions and Mechanisms of Action of Small Heat Shock Proteins
Cellular sequestrases maintain basal Hsp70 capacity ensuring balanced proteostasis
Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor
Toxic Activation of an AAA+ Protease by the Antibacterial Drug Cyclomarin A
Disassembly of Tau fibrils by the human Hsp70 disaggregation machinery generates small seeding-competent species
ClpG Provides Increased Heat Resistance by Acting as Superior Disaggregase
HSP110 dependent HSP70 disaggregation machinery mediates prion-like propagation of amyloidogenic proteins in metazoa
Cellular Handling of Protein Aggregates by Disaggregation Machines
A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins
Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase
Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control
Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria