Lina Wang
Indiana University
9 Papers
17 Citations
Lina Wang is an academic researcher from Indiana University. The author has contributed to research in topics: Protein tyrosine phosphatase & Proto-oncogene tyrosine-protein kinase Src. The author has an hindex of 8, co-authored 8 publications.
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Papers
Salicylic acid based small molecule inhibitor for the oncogenic Src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2).
Xian Zhang,Yantao He,Sijiu Liu,Zhi-Hong Yu,Zhong Xing Jiang,Zhenyun Yang,Yuanshu Dong,Sarah C. Nabinger,Li Wu,Andrea M. Gunawan,Lina Wang,Rebecca J. Chan,Zhong Yin Zhang +12 more
TL;DR: A salicylic acid based combinatorial library approach aimed at binding both active site and unique nearby subpockets for enhanced affinity and selectivity led to the identification of a SHP2 inhibitor II-B08 (compound 9) with highly efficacious cellular activity, providing supporting evidence that chemical inhibition ofSHP2 may be therapeutically useful for anticancer and antileukemia treatment.
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Structural and Mechanistic Insights into LEOPARD Syndrome-Associated SHP2 Mutations.
Zhi-Hong Yu,Jie Xu,Chad D. Walls,Lan Chen,Sheng Zhang,Ruo-Yu Zhang,Li Wu,Lina Wang,Sijiu Liu,Zhong Yin Zhang +9 more
TL;DR: This study reveals that LEOPARD syndrome mutations weaken the intramolecular interaction between the N-SH2 and phosphatase domains, leading to a change in SHP2 molecular switching mechanism, which binds preferentially to upstream activators to prolong substrate turnover, thus engender gain-of-function phenotypes.
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A highly selective and potent PTP-MEG2 inhibitor with therapeutic potential for type 2 diabetes.
Sheng Zhang,Sijiu Liu,Rongya Tao,Dan Wei,Lan Chen,Weihua Shen,Zhi-Hong Yu,Lina Wang,David R. Jones,Xiaocheng C. Dong,Zhong Yin Zhang +10 more
TL;DR: The results indicate that F(2)Pmp can be converted into highly potent and selective PTP inhibitory agents with excellent in vivo efficacy and should be applicable to other members of the PTP superfamily.
SHP2 is a target of the immunosuppressant tautomycetin.
Sijiu Liu,Zhi-Hong Yu,Xiao Yu,Sheng-Xiong Huang,Yinggang Luo,Li Wu,Weihua Shen,Zhenyun Yang,Lina Wang,Andrea M. Gunawan,Rebecca J. Chan,Ben Shen,Zhong Yin Zhang +12 more
TL;DR: The data support the notion that SHP2 is a cellular target for TTN and provide a potential mechanism for the immunosuppressive activity of TTN, and the structure furnishes molecular insights upon which therapeutics targetingSHP2 can be developed on the basis of the TTN scaffold.
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Small molecule inhibitors of SHP2 tyrosine phosphatase discovered by virtual screening.
TL;DR: A structure-based approach to identify SHP2 inhibitors with a novel scaffold reveals the molecular determinants for further optimization based on the new scaffold and proposes a most likely binding mode of C21 with SHp2, consistent with the observed potency and specificity.
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