233 South 10th Street
BLSB 804
Philadelphia, PA 19107
(215) 503-4596
(215) 923-2117 fax
BLSB 804
Philadelphia, PA 19107
(215) 503-4596
(215) 923-2117 fax
Most Recent Peer-reviewed Publications
- Structural biology of the writers, readers, and erasers in mono- and poly(ADP-ribose) mediated signaling
- Unstructured to structured transition of an intrinsically disordered protein peptide in coupling Ca2+-sensing and SK channel activation
- PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis
- Dual roles of PARP-1 promote cancer growth and progression
- Identification of the functional binding pocket for compounds targeting small-conductance Ca 2+ -activated potassium channels
- Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1
- Structural basis for calmodulin as a dynamic calcium sensor
- Autoregulation of kinase dephosphorylation by ATP binding to AGC protein kinases
- Adaptation to tRNA acceptor stem structure by flexible adjustment in the catalytic domain of class I tRNA synthetases
- Resistance of Akt kinases to dephosphorylation through ATP-dependent conformational plasticity
- Purification of human PARP-1 and PARP-1 domains from escherichia coli for structural and biochemical analysis
- Crystal structures of poly(ADP-ribose) polymerase-1 (PARP-1) zinc fingers bound to DNA: Structural and functional insights into DNA-dependent PARP-1 activity
- The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction
- The DNA binding domain of human DNA ligase I interacts with both nicked DNA and the DNA sliding clamps, PCNA and hRad9-hRad1-hHus1
- A third zinc-binding domain of human poly(ADP-ribose) polymerase-1 coordinates DNA-dependent enzyme activation (Journal of Biological Chemistry (2008) 283, (4105-4114))
- A third zinc-binding domain of human poly(ADP-ribose) polymerase-1 coordinates DNA-dependent enzyme activation
- DNA and RNA ligases: structural variations and shared mechanisms
- RNA ligase does the AMP shuffle
- A Flexible Interface between DNA Ligase and PCNA Supports Conformational Switching and Efficient Ligation of DNA
- Human DNA Ligases I, III, and IV-Purification and New Specific Assays for These Enzymes