Manju M. Hingorani

On the specificity of interaction between the Saccharomyces cerevisiae clamp loader replication factor C and primed DNA templates during DNA replication.

Mechanism of loading the Escherichia coli DNA polymerase III beta sliding clamp on DNA. Bona fide primer/templates preferentially trigger the gamma complex to hydrolyze ATP and load the clamp.

Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-bound state at the initiation of DNA repair.

Overproduction and analysis of eukaryotic multiprotein complexes in Escherichia coli using a dual-vector strategy.

Replication factor C clamp loader subunit arrangement within the circular pentamer and its attachment points to proliferating cell nuclear antigen.

Dual functions, clamp opening and primer-template recognition, define a key clamp loader subunit.

Asymmetric ATP binding and hydrolysis activity of the Thermus aquaticus MutS dimer is key to modulation of its interactions with mismatched DNA.

Role of a conserved glutamate residue in the Escherichia coli SecA ATPase mechanism.

Contribution of Msh2 and Msh6 subunits to the asymmetric ATPase and DNA mismatch binding activities of Saccharomyces cerevisiae Msh2-Msh6 mismatch repair protein.

The effects of nucleotides on MutS-DNA binding kinetics clarify the role of MutS ATPase activity in mismatch repair.

TIRF(ing) reveals Msh2-Msh6 surfing on DNA.

Conserved residues in the delta subunit help the E. coli clamp loader, gamma complex, target primer-template DNA for clamp assembly.

Mechanism of MutS searching for DNA mismatches and signaling repair.

Structure of a mutant form of proliferating cell nuclear antigen that blocks translesion DNA synthesis.

Mechanism of ATP-driven PCNA clamp loading by S. cerevisiae RFC.

Mechanism of cadmium-mediated inhibition of Msh2-Msh6 function in DNA mismatch repair.

Model-based global analysis of heterogeneous experimental data using gfit.

Saccharomyces cerevisiae Msh2-Msh6 DNA binding kinetics reveal a mechanism of targeting sites for DNA mismatch repair.

Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6.

Dynamical allosterism in the mechanism of action of DNA mismatch repair protein MutS.

A Central Swivel Point in the RFC Clamp Loader Controls PCNA Opening and Loading on DNA.

ATP Binding and Hydrolysis-Driven Rate-Determining Events in the RFC-Catalyzed PCNA Clamp Loading Reaction.