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Shang-Te Danny Hsu

Researcher at Academia Sinica

Publications -  119
Citations -  4293

Shang-Te Danny Hsu is an academic researcher from Academia Sinica. The author has contributed to research in topics: Protein folding & Protein structure. The author has an hindex of 33, co-authored 104 publications receiving 3481 citations. Previous affiliations of Shang-Te Danny Hsu include University of Cambridge & National Yang-Ming University.

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The Nisin-Lipid II Complex Reveals a Pyrophosphate Cage that Provides a Blueprint for Novel Antibiotics

TL;DR: The structure shows a novel lipid II–binding motif in which the pyrophosphate moiety of lipid II is primarily coordinated by the N-terminal backbone amides of nisin via intermolecular hydrogen bonds, which provides a rationale for the conservation of the lanthionine rings among several lipid II-binding lantibiotics.
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A G-rich sequence within the c-kit oncogene promoter forms a parallel G-quadruplex having asymmetric G-tetrad dynamics

TL;DR: A structural study using solution state NMR spectroscopy of a second G-quadruplex-forming motif (c-kit2) that has been recently identified in the promoter region of the c-kit oncogene suggests the coexistence of at least two structurally similar but dynamically distinct substates, which undergo slow interconversion on the NMR timescale.
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Structure and Properties of a Complex of alpha-Synuclein and a Single-Domain Camelid Antibody

TL;DR: Results give strong support to the conjecture that the C-terminal region of the protein is not directly involved in the mechanism of aggregation and suggest that binding of NbSyn2 could be a useful probe for the identification of α-synuclein aggregation in vitro and possibly in vivo.
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Diarylethynyl amides that recognize the parallel conformation of genomic promoter DNA G-quadruplexes.

TL;DR: B bis-phenylethynyl amide derivatives are reported as a potent G-quadruplex binding small molecule scaffold and recognition of the c-kit2 quadruplex by these ligands is achieved through groove binding, which favors the formation of a parallel conformation.
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NMR Study of Mersacidin and Lipid II Interaction in Dodecylphosphocholine Micelles. Conformational Changes are a Key to Antimicrobial Activity

TL;DR: In this paper, solution NMR studies of mersacidin-lipid II interaction in dodecylphosphocholine (DPC) micelles were performed and the structures in various sample conditions reveal remarkable conformational changes in which the junction between Ala-12 and Abu-13 effectively serves as the hinge for the opening and closure of the ring structures.