Area of research
Molecular Biology · Genetics
Research interest
Research interests include Protein Structure and Dynamics, RNA and protein synthesis mechanisms, Bacterial Genetics and Biotechnology, and Heat shock proteins research.
Quantitative insights into processivity of an Hsp100 protein disaggregase on folded proteins
Single turnover transient state kinetics reveals processive protein unfolding catalyzed by Escherichia coli ClpB
The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments
The A12.2 Subunit Plays an Integral Role in Pyrophosphate Release of RNA Polymerase I
AAA+ proteins: one motor, multiple ways to work
RNA Polymerase I Is Uniquely Vulnerable to the Small-Molecule Inhibitor BMH-21
Uncovering the mechanisms of transcription elongation by eukaryotic RNA polymerases I, II, and III
Transient-State Kinetic Analysis of the RNA Polymerase II Nucleotide Incorporation Mechanism
Multi-start Evolutionary Nonlinear OpTimizeR (MENOTR): A hybrid parameter optimization toolbox
The N-terminal domain of the A12.2 subunit stimulates RNA polymerase I transcription elongation
Transient-state kinetic analysis of multi-nucleotide addition catalyzed by RNA polymerase I
Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis
Defining the divergent enzymatic properties of RNA polymerases I and II
Downstream sequence-dependent RNA cleavage and pausing by RNA polymerase I
Hsp104 and Potentiated Variants Can Operate as Distinct Nonprocessive Translocases
Downstream sequence-dependent RNA cleavage and pausing by RNA polymerase I
A Novel Assay for RNA Polymerase I Transcription Elongation Sheds Light on the Evolutionary Divergence of Eukaryotic RNA Polymerases
The A12.2 Subunit Is an Intrinsic Destabilizer of the RNA Polymerase I Elongation Complex
ATP hydrolysis inactivating Walker B mutation perturbs E. coli ClpA self-assembly energetics in the absence of nucleotide
Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions
Multisubunit RNA Polymerase Cleavage Factors Modulate the Kinetics and Energetics of Nucleotide Incorporation: An RNA Polymerase I Case Study
Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures
Examination of ClpB Quaternary Structure and Linkage to Nucleotide Binding
<i>Escherichia coli</i> ClpB is a non-processive polypeptide translocase
Transient-State Kinetic Analysis of the RNA Polymerase I Nucleotide Incorporation Mechanism
Examination of the dynamic assembly equilibrium for <scp><i>E</i></scp><i>. coli</i> ClpB
Examination of polypeptide substrate specificity for <scp><i>E</i></scp><i>scherichia coli</i><scp>C</scp>lp<scp>B</scp>
E. coli ClpA Catalyzed Polypeptide Translocation Is Allosterically Controlled by the Protease ClpP
Mechanisms of Fidelity in Eukaryotic RNA Polymerases
Understanding Architecture Hierarchy of Polymer Networks to Control Mechanical Responses
Reprogramming redox-controlled innate and adaptive immune responses by antioxidant polymer microvesicles
RAPID: Mechanisms of Polymerization Catalyzed by the SARS-CoV-2 RNA Dependent RNA Polymerase
Molecular mechanisms of RNA Polymerase I Transcription Elongation
Mechanisms of Polypeptide Translocation Catalyzed by Class 1 HSP100/Clp Enzymes
Kinetic Mechanisms of ClpA Catalyzed Polypeptide Translocation