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The SOCS-Box of HIV-1 Vif Interacts with ElonginBC by Induced-Folding to Recruit Its Cul5-Containing Ubiquitin Ligase Complex
The HIV-1 viral infectivity factor (Vif) protein recruits an E3 ubiquitin ligase complex, comprising the cellular proteins elongin B and C (EloBC), cullin 5 (Cul5) and RING-box 2 (Rbx2), to theExpand
Structural insight into the quinolone–DNA cleavage complex of type IIA topoisomerases
Type II topoisomerases alter DNA topology by forming a covalent DNA-cleavage complex that allows DNA transport through a double-stranded DNA break. We present the structures of cleavage complexesExpand
Structural Basis of Gate-DNA Breakage and Resealing by Type II Topoisomerases
Type II DNA topoisomerases are ubiquitous enzymes with essential functions in DNA replication, recombination and transcription. They change DNA topology by forming a transient covalent cleavageExpand
Exploring the active site of herpes simplex virus type‐1 thymidine kinase by X‐ray crystallography of complexes with aciclovir and other ligands
Antiherpes therapies are principally targeted at viral thymidine kinases and utilize nucleoside analogs, the triphosphates of which are inhibitors of viral DNA polymerase or result in toxic effectsExpand
Crystal structures of the thymidine kinase from herpes simplex virus type-I in complex with deoxythymidine and Ganciclovir
The crystal structures of thymidine kinase from herpes simplex virus type-1 complexed with its natural substrate deoxythymidine (dT) and complexed with the guanosine analogue Ganciclovir have beenExpand
Cocrystal structure of an editing complex of Klenow fragment with DNA.
High-resolution crystal structures of editing complexes of both duplex and single-stranded DNA bound to Escherichia coli DNA polymerase I large fragment (Klenow fragment) show four nucleotides ofExpand
Crystal lattice packing is important in determining the bend of a DNA dodecamer containing an adenine tract.
The crystal structure of a DNA duplex dodecamer d(CGCAAAAATGCG) and its complementary strand has been determined at 2.6-A resolution. Although our goal was to deduce the structural features of theExpand
Threonine Phosphorylation of the β3 Integrin Cytoplasmic Tail, at a Site Recognized by PDK1 and Akt/PKB in Vitro, Regulates Shc Binding*
The mechanism of outside-in signaling by integrins parallels that for growth factor receptors. In both pathways, phosphorylation of a cytoplasmic segment on tyrosine generates a docking site forExpand
Structure of an ‘open’ clamp type II topoisomerase-DNA complex provides a mechanism for DNA capture and transport
Type II topoisomerases regulate DNA supercoiling and chromosome segregation. They act as ATP-operated clamps that capture a DNA duplex and pass it through a transient DNA break in a second DNAExpand
Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I.
Site-directed mutagenesis of the large fragment of DNA polymerase I (Klenow fragment) yielded two mutant proteins lacking 3',5'-exonuclease activity but having normal polymerase activity.Expand
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