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Feng Wang

Researcher at Chinese Academy of Sciences

Publications -  96
Citations -  5171

Feng Wang is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Antibody & Fusion protein. The author has an hindex of 34, co-authored 96 publications receiving 4315 citations. Previous affiliations of Feng Wang include Texas A&M University & Genomics Institute of the Novartis Research Foundation.

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Switch-mediated activation and retargeting of CAR-T cells for B-cell malignancies

TL;DR: It is shown that switches specific for CD19 govern the activity, tissue-homing, cytokine release, and phenotype of switchable CAR-T cells in a dose-titratable manner using xenograft mouse models of B-cell leukemia.
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Transfer of a point mutation in Mycobacterium tuberculosis inhA resolves the target of isoniazid.

TL;DR: Using specialized linkage transduction, a single point mutation allele (S94A) within the putative target gene inhA was transferred in Mycobacterium tuberculosis and was sufficient to confer clinically relevant levels of resistance to isoniazid killing and inhibition of mycolic acid biosynthesis.
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Two-step nucleation mechanism in solid-solid phase transitions.

TL;DR: It is shown that transitions between square and triangular lattices occur via a two-step diffusive nucleation pathway involving liquid nuclei, suggesting that an intermediate liquid should exist in the nucleation processes of solid-solid transitions of most metals and alloys.
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Auranofin exerts broad-spectrum bactericidal activities by targeting thiol-redox homeostasis

TL;DR: The results suggest that the thioredoxin-mediated redox cascade of Gram-positive pathogens is a valid target for the development of antibacterial drugs, and that the existing clinical agent auranofin may be repurposed to aid in the treatment of several important antibiotic-resistant pathogens.
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Mechanism of thioamide drug action against tuberculosis and leprosy.

TL;DR: Using a cell-based activation method, definitive evidence is provided that both thioamides form covalent adducts with nicotinamide adenine dinucleotide (NAD) and that theseAdducts are tight-binding inhibitors of M. tuberculosis and M. leprae InhA.