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2017. Long noncoding RNA LINC00673 is activated by SP1 and exerts oncogenic properties by interacting with LSD1 and EZH2 in gastric cancer. M Huang, J Hou, Y Wang, M Xie, C Wei, F Nie, Z Wang, M Sun. Molecular Therapy 25 (4), 1014-1026. , 2017.
- Introduction
- Results
- Discussion
- Materials and Methods
- Acknowledgements
- Funding
Evolution has fine-tuned the ability of venoms in many venomous animals, such as snakes, spiders, centipedes and scorpions, to rapidly incapacitate both prey and predators—especially for fast-moving targets—as a mechanism for hunting prey or deterring predators [1–4]. To achieve a paralytic envenomation, targeting skeletal muscle sodium channel NaV...
Significant tolerance of frog-to-scorpion stings and α-toxin
As shown in Fig. 1A and Supplementary Movie S1 (available as Supplementary Data at NSR online), although the scorpion displayed a powerful chemical defense via several toxic stings, these stings had no impact on the frog during the predatory process. By contrast, scorpion stings exhibited a successful defensive role in laboratory mice (Supplementary Movie S2, available as Supplementary Data at NSR online). Therefore, frogs may possess some molecular strategies to diminish the physiological ef...
Domain IV of fNaV1.4 and BgNaV1 determines the sensitivity to α-toxin
To test our hypothesis, we first cloned fNaV1.4 from a frog (Pyxicephalus adspersus) and expressed it in HEK293 cells. As shown in Supplementary Fig. S2A (available as Supplementary Data at NSR online), the steady activation of fNaV1.4 (Va1/2 = −28.1 mV) is similar to that of the BgNaV1 channel (Va1/2 = −26.5 mV). By comparing the fraction of remaining current at 5 milliseconds after the peak versus the peak current amplitude (Table S2, available as Supplementary Data at NSR online), fNaV1.4...
A point mutation bestows fNaV1.4 with resistance to paralytic α-toxin
Additionally, glycine/alanine screening revealed the key residues in the toxin-channel interaction. Two residues (42Y and 62K) were identified as the key sites of the toxin by the washing-out time-course analysis, yielding τ-off values of 25.82 and 15.07 seconds, respectively (Fig. 3A). Asp/Lys-Tyrmotif was identified as the binding pocket of BmK-M9, given that the three residues located in this motif of mammalian DIV-VSD were found to be important for the toxin-channel interaction (Fig. 3B–D...
Venomous animals are consistently excellent predators due to possession of formidable venom biochemical armaments and thereby often occupy dominant positions in food chains [36,37]. To be higher-level predators of these venomous animals, evolutionary game processes at the molecular level are necessary to equip several crucial detoxification mechani...
Ethics statement
All of the animal experiments were performed in accordance with recommendations in the Guide for the Care and Use of Laboratory Animals of Kunming Institute of Zoology, Chinese Academy of Sciences. Experimental protocols using animals in this study were approved by the Institutional Animal Care and Use Committees at Kunming Institute of Zoology, Chinese Academy of Sciences (approval ID: SMKX-2018029).
Purification and protein sequencing of BmK-M9
A total of 1,000 (both sexes) adults Mesobuthus martensii were purchased from Shandong Province, China. As previously reported , crude venom was collected by stimulating the venom glands with a 3 V alternating current. BmK-M9 was purified from the crude venom by using a combination of a Sephadex G-50 gel filtration column and reverse-phase (RP)-HPLC. The purity and molecular weight of the toxin were analysed using a matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF). T...
Preparation of recombinant toxin and fluorescent-labeled BmK-M9
Expression vector construction, protein expression and purification were performed as described previously [49,50] with fine tuning. In summary, the cDNA encoding BmK-M9 was synthesized with codons optimized for expression in Escherichia coli, and it was cloned into the modified expression vector pet32a (+) (Novagen). This vector (pet32a) encodes a His6 tag for affinity purification, a Trx-Tag for improving the solubility and activity of the expressed peptide, and a tobacco etch virus (TEV) p...
We thank Prof. Ke Dong for providing BgNaV1 plasmid; Prof. Yan-Ai Mei for providing NaV1.2 plasmid; we also thank Eve Angsutararux and Wandi Zhu in Dr. Jonathan R. Silva's lab for their help on cut-open VCF experiments. We thank our laboratory members, Yalan Han, James Mwangi and Panpan Hou in Prof. Jianmin Cui's lab, for discussion.
This work was supported by the National Natural Science Foundation of China (NSFC) (31930015) and the Chinese Academy of Sciences (XDB31000000 and SAJC201606) to R.L., the NSFC (31770835), the Chinese Academy of Sciences grants for Youth Innovation Promotion Association and CAS ‘Light of West China’ Program and Yunnan Province (2018FA003 and 2017FA...
- Bowen Li, Jonathan R Silva, Xiancui Lu, Xiancui Lu, Lei Luo, Yunfei Wang, Lizhen Xu, Aerziguli Aierk...
- 2019
Jack Yi, MD. Resident Research Fellow ... Department of Surgery. 660 S. Euclid Avenue. St. Louis, MO 63110. Facebook; Twitter ©2024 Washington University in St ...
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