C
Carlos Huerta
Researcher at University of Texas Southwestern Medical Center
Publications - 7
Citations - 918
Carlos Huerta is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Flavin mononucleotide & FMN adenylyltransferase. The author has an hindex of 5, co-authored 6 publications receiving 806 citations. Previous affiliations of Carlos Huerta include Reata Pharmaceuticals.
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Journal ArticleDOI
Identification of a candidate therapeutic autophagy-inducing peptide
Sanae Shoji-Kawata,Rhea Sumpter,Matthew J Leveno,Grant R. Campbell,Grant R. Campbell,Zhongju Zou,Zhongju Zou,Lisa N. Kinch,Lisa N. Kinch,Angela D. Wilkins,Qihua Sun,Kathrin Pallauf,Donna A. MacDuff,Carlos Huerta,Carlos Huerta,Herbert W. Virgin,J. Bernd Helms,Ruud Eerland,Sharon A. Tooze,Ramnik J. Xavier,Ramnik J. Xavier,Deborah J. Lenschow,Ai Yamamoto,David S. King,Olivier Lichtarge,Nick V. Grishin,Stephen A. Spector,Stephen A. Spector,Dora V. Kaloyanova,Beth Levine +29 more
TL;DR: 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.
Journal ArticleDOI
Structure of C3PO and mechanism of human RISC activation.
Xuecheng Ye,Nian Huang,Ying Liu,Zain Paroo,Carlos Huerta,Peng Li,She Chen,Qinghua Liu,Hong Zhang +8 more
TL;DR: 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.
Journal ArticleDOI
Structure and mechanism of a eukaryotic FMN adenylyltransferase.
TL;DR: 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.
Journal ArticleDOI
Characterization of novel small-molecule NRF2 activators: Structural and biochemical validation of stereospecific KEAP1 binding.
Carlos Huerta,Carlos Huerta,Xin Jiang,Isaac Trevino,Bender Christopher F,Deborah A. Ferguson,Brandon L. Probst,Kerren K. Swinger,Vincent S. Stoll,Philip Thomas,Irina Dulubova,Melean Visnick,W. Christian Wigley +12 more
TL;DR: 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.
Journal ArticleDOI
Structural basis for substrate binding and the catalytic mechanism of type III pantothenate kinase.
TL;DR: 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.