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Xinjian Yan

Researcher at National Institutes of Health

Publications -  15
Citations -  696

Xinjian Yan is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Ricin & Peptide synthesis. The author has an hindex of 10, co-authored 14 publications receiving 687 citations. Previous affiliations of Xinjian Yan include University of Texas at Austin.

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Journal ArticleDOI

Small Molecule Interactions with Protein−Tyrosine Phosphatase PTP1B and Their Use in Inhibitor Design†

TL;DR: The X-ray structure of [1, 1-difluoro-1-(2-naphthalenyl)-methyl]phosphonic acid complexed within the catalytic site of PTP1B, solved to 2.3 A resolution, revealed extensive hydrophobic interactions with the naphthalene ring system, beyond that possible with an analog bearing a single phenyl ring.
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Discovery of novel, non-peptide HIV-1 protease inhibitors by pharmacophore searching

TL;DR: Fifteen novel non-peptide HIV-1 protease inhibitors were identified by flexible 3D database pharmacophore searching of the NCI DIS3D database by using X-ray determined structures of protease/inhibitor complexes.
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Structure-based identification of a ricin inhibitor.

TL;DR: Computer-assisted searches indicated that pterins might bind in the RTA active site which normally recognizes a specific adenine base on rRNA, and models observed suggest alterations to the pterin moiety which may produce more potent and specific RTA inhibitors.
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4'-O-[2-(2-fluoromalonyl)]-L-tyrosine : a phosphotyrosyl mimic for the preparation of signal transduction inhibitory peptides

TL;DR: New fluorine-containing nonphosphorus pTyr mimetic reported, which can be incorporated into peptides that exhibit good PTP and Src homology 2 (SH2) domain inhibitory potency, and would appear to have particular potential for the development of PTP inhibitors.
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Conformationally constrained phosphotyrosyl mimetics designed as monomeric Src homology 2 domain inhibitors

TL;DR: It was observed that capping pTyr as its N alpha-acetyl carboxamide [(L)-1] provided a roughly 2-3-fold increase in potency relative to free pT Tyr, which could potentially result in small molecule inhibitors having greater potency.