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Shuangluo Xia
Researcher at University of Texas at Austin
Publications - 6
Citations - 156
Shuangluo Xia is an academic researcher from University of Texas at Austin. The author has contributed to research in topics: Relaxase & Origin of transfer. The author has an hindex of 5, co-authored 6 publications receiving 150 citations.
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Journal ArticleDOI
The Structure of the Minimal Relaxase Domain of MobA at 2.1 Å Resolution
TL;DR: A model of the oriT substrate complexed with minMobA has been made, based on observed substrate binding to TrwC and TraI, and provides a rationalization for elements of the likely enzyme mechanism.
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Structure of NS1A effector domain from the influenza A/Udorn/72 virus
TL;DR: Structural comparison with the NS1 effector domain from mouse-adapted influenza A/Puerto Rico/8/34 (PR8) virus strain reveals a similar monomer conformation but a different dimer interface, and analysis and evaluation shows that theDimer interface observed in the structure of the PR8 NS1Effector domain is likely to be a crystallographic packing effect.
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Identification of Influenza Virus Inhibitors Targeting NS1A Utilizing Fluorescence Polarization–Based High-Throughput Assay:
Eun Jeong Cho,Shuangluo Xia,Li-Chung Ma,Jon D. Robertus,Robert M. Krug,Eric V. Anslyn,Gaetano T. Montelione,Andrew D. Ellington +7 more
TL;DR: A simple and robust fluorescence polarization (FP)–based binding assay and adaptation to high-throughput identification of small molecules blocking dsRNA binding to NS1A protein (nonstructural protein 1 from type A influenza strains).
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X-ray structures of NS1 effector domain mutants.
Shuangluo Xia,Jon D. Robertus +1 more
TL;DR: Two mutant effector domains, W187Y and W187A, of influenza A/Udorn/72 virus behave exclusively as monomers in solution based on gel filtration data and light scattering, which suggests this monomeric mutant protein could serve as a drug target for a high throughput inhibitor screening assays.
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Effect of divalent ions on the minimal relaxase domain of MobA
Shuangluo Xia,Jon D. Robertus +1 more
TL;DR: Investigation of the effects of different divalent metallic cations on minMobA activity measuring DNA binding, DNA nicking, and protein denaturation experiments shows that divalent cations are not required for DNA binding but are required forDNA nicking.