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Structure of C3PO and Mechanism of Human RISC Activation
- X. Ye, Nian Huang, +6 authors H. Zhang
- Biology, Medicine
- Nature Structural &Molecular Biology
- 24 February 2011
A Dicer-independent mechanism for human RISC activation is supported, in which Ago2 directly binds duplex siRNA and nicks the passenger strand, and then C3PO activates RISC by degrading the Ago2-nicked passenger strand. Expand
Identification of a candidate therapeutic autophagy-inducing peptide
Through the characterization of a domain of beclin 1 that interacts with HIV-1 Nef, an autophagy-inducing peptide is developed that has potential efficacy in the treatment of human diseases. Expand
Structural basis for substrate binding and the catalytic mechanism of type III pantothenate kinase.
Comparison of substrate binding and catalytic sites of PanK-III with that of eukaryotic panK-II revealed drastic differences in the binding modes for both ATP and pantothenate substrates, and suggests that these differences may be exploited in the development of new inhibitors specifically targeting PanK -III. Expand
Structure and mechanism of a eukaryotic FMN adenylyltransferase.
- C. Huerta, D. Borek, M. Machius, N. Grishin, H. Zhang
- Biology, Medicine
- Journal of molecular biology
- 5 June 2009
Comparison of the bacterial and eukaryotic FMNATs provides a structural basis for understanding the convergent evolution of the same FMNAT activity from different protein ancestors and reveals a novel flavin-binding mode and a unique enzyme-bound FAD conformation. Expand
Characterization of novel small-molecule NRF2 activators: Structural and biochemical validation of stereospecific KEAP1 binding.
- C. Huerta, Xin Jiang, +9 authors W. C. Wigley
- Chemistry, Medicine
- Biochimica et biophysica acta
- 1 November 2016
This work demonstrates that reversible cyanoenone Michael acceptors, such as the tpAIMs and sA IMs, can be specifically tuned to regulate redox sensitive cysteine residues on key signaling molecules, an approach with significant promise for innovative drug development. Expand
Structural Basis and Kinetic Pathway of RBM39 Recruitment to DCAF15 by a Sulfonamide Molecular Glue E7820.
The structural and kinetic studies confirm aryl sulfonamides as molecular glues in the recruitment of RBM39 and provide a framework for future efforts to utilize DCAF15 to degrade other proteins of interest. Expand
The "super mutant" of yeast FMN adenylyltransferase enhances the enzyme turnover rate by attenuating product inhibition.
A structure-based mutagenesis and steady-state kinetic analysis of yeast FMNAT unexpectedly revealed that mutant D181A had a much faster turnover rate than the wild-type enzyme, suggesting that product release may be the rate-limiting step of the reaction. Expand
Crystal Structure of Candida glabrata FMN Adenylyltransferase in complex with FAD and Inorganic Pyrophosphate
Type III pantothenate kinase from Thermotoga maritima complexed with pantothenate and ADP
Crystal Structure of Candida glabrata FMN Adenylyltransferase