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Yijia Xiong

Researcher at Western University of Health Sciences

Publications -  37
Citations -  1222

Yijia Xiong is an academic researcher from Western University of Health Sciences. The author has contributed to research in topics: Shewanella oneidensis & Fusion protein. The author has an hindex of 20, co-authored 36 publications receiving 1109 citations. Previous affiliations of Yijia Xiong include Chinese Academy of Sciences & Pacific Northwest National Laboratory.

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Extracellular Polymeric Substances from Shewanella sp. HRCR-1 Biofilms: Characterization by Infrared Spectroscopy and Proteomics

TL;DR: C-type cytochromes may contribute to the possible redox activity of the biofilm matrix and play important roles in extracellular electron transfer reactions.
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High-affinity binding and direct electron transfer to solid metals by the Shewanella oneidensis MR-1 outer membrane c-type cytochrome OmcA.

TL;DR: Binding is highly favorable, with a partition coefficient of approximately 2 x 105 (DeltaGo' = -28 kJ/mol), where approximately 1014 OmcA proteins bind per cm2 to the solid metal surface, indicating the utility of using purified OmcC in the construction of a biofuel cell.
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A Red Cy3-Based Biarsenical Fluorescent Probe Targeted to a Complementary Binding Peptide

TL;DR: A red biarsenical fluorescent probe, AsCy3, with good photostability, low pH sensitivity, high absorbance, and good quantum yield is synthesized, directed specifically to a small tetracysteine peptide binding motif, Cy3TAG, in the presence of other tetrACYsteine tags.
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Hsp90 enhances degradation of oxidized calmodulin by the 20 S proteasome.

TL;DR: Results indicate that Hsp90 in association with the 20 S proteasomes can selectively associate with oxidized and partially unfolded CaM to promote degradation by the proteasome.
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Fluorophore-assisted light inactivation of calmodulin involves singlet-oxygen mediated cross-linking and methionine oxidation.

TL;DR: The results provide a rationale for proteomic screens using FALI to inhibit the function of many signaling proteins, which, like CaM, commonly present methionines at binding interfaces.