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Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization.
USP7/HAUSP is a key regulator of p53 and Mdm2 and is targeted by the Epstein-Barr nuclear antigen 1 (EBNA1) protein of Epstein-Barr virus (EBV). We have determined the crystal structure of the p53… Expand
Solution structure of the tetrameric minimum transforming domain of p53
- W. Lee, T. Harvey, Y. Yin, P. Yau, D. Litchfield, C. Arrowsmith
- Biology, Medicine
- Nature Structural Biology
- 7 February 1995
We report the solution structure of the minimum transforming domain (residues 303–366) of human p53 (p53tet) determined by multidimensional NMR spectroscopy. This domain contains a number of… Expand
Chemical structure and biological activity of the Caenorhabditis elegans dauer-inducing pheromone
Pheromones are cell type-specific signals used for communication between individuals of the same species. When faced with overcrowding or starvation, Caenorhabditis elegans secrete the pheromone… Expand
A Suite of Triple Resonance NMR Experiments for the Backbone Assignment of 15N, 13C, 2H Labeled Proteins with High Sensitivity
An NMR approach to structural proteomics.
Adelinda Yee*, Xiaoqing Chang*, Antonio Pineda-Lucena*, Bin Wu*, Anthony Semesi*, Brian Le*, Theresa Ramelot†, Gregory M. Lee‡, Sudeepa Bhattacharyya§, Pablo Gutierrez¶, Aleksej Denisov¶, Chang-Hun… Expand
Structure of an Atypical Orphan Response Regulator Protein Supports a New Phosphorylation-independent Regulatory Mechanism*
- E. Hong, Hyang Mi Lee, +10 authors W. Lee
- Biology, Medicine
- Journal of Biological Chemistry
- 13 July 2007
Two-component signal transduction systems, commonly found in prokaryotes, typically regulate cellular functions in response to environmental conditions through a phosphorylation-dependent process. A… Expand
An NMR approach to structural proteomics
- A. Yee, X. Chang, +21 authors C. Arrowsmith
- Medicine, Biology
- Proceedings of the National Academy of Sciences…
- 19 February 2002
The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural… Expand
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by site-directed mutagenesis and comparative modelling studies.
The active site and substrate-binding mode of MD-ACO1 (Malus domestica Borkh. 1-aminocyclopropane-1-carboxylate oxidase) have been determined using site-directed mutagenesis and comparative modelling… Expand
Lys296 and Arg299 residues in the C-terminus of MD-ACO1 are essential for a 1-aminocyclopropane-1-carboxylate oxidase enzyme activity.
- Ahrim Yoo, Y. S. Seo, +4 authors D. Yang
- Medicine, Chemistry
- Journal of structural biology
- 1 December 2006
The 1-aminocyclopropane-1-carboxylate (ACC) oxidase catalyzes the last step in the biosynthesis of ethylene from ACC in higher plants. The complex structure of ACC oxidase/Fe(2+)/H(2)O derived from… Expand
Crystal Structures of RbsD Leading to the Identification of Cytoplasmic Sugar-binding Proteins with a Novel Folding Architecture*
RbsD is the only protein whose biochemical function is unknown among the six gene products of the rbs operon involved in the active transport of ribose. FucU, a paralogue of RbsD conserved from… Expand