G
Giang K. T. Nguyen
Researcher at Nanyang Technological University
Publications - 29
Citations - 1850
Giang K. T. Nguyen is an academic researcher from Nanyang Technological University. The author has contributed to research in topics: Cyclotide & Cyclotides. The author has an hindex of 18, co-authored 27 publications receiving 1495 citations. Previous affiliations of Giang K. T. Nguyen include Temasek Life Sciences Laboratory & National University of Singapore.
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Journal ArticleDOI
Butelase 1 is an Asx-specific ligase enabling peptide macrocyclization and synthesis
TL;DR: In this article, the highly efficient butelase 1, homologous to proteases but specific for ligations, was proposed as a new method for peptide cyclization, which has attracted increasing attention as tools for research and potential therapeutics.
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Orally Active Peptidic Bradykinin B1 Receptor Antagonists Engineered from a Cyclotide Scaffold for Inflammatory Pain Treatment
Clarence T. T. Wong,Dewi Kenneth Rowlands,Chi Hang Wong,Chi Hang Wong,Theodore W. C. Lo,Giang K. T. Nguyen,Hoi-Yeung Li,James P. Tam +7 more
TL;DR: New evidence suggests that bradykinin (BK) antagonists could be useful in treating chronic pain and inflammatory pain, and suggests that the B1 receptor mediates various chronic pain responses through the activation of phospholipase C, thereby leading to the production of diacylglycerol and inositol triphosphate.
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Discovery and Characterization of Novel Cyclotides Originated from Chimeric Precursors Consisting of Albumin-1 Chain a and Cyclotide Domains in the Fabaceae Family
Giang K. T. Nguyen,Sen Zhang,Ngan Thi Kim Nguyen,Phuong Quoc Thuc Nguyen,Ming Sheau Chiu,Antony Hardjojo,James P. Tam +6 more
TL;DR: It is shown unambiguously that the cliotides are cyclotides and not A1bs, as determined by their sequence homology, disulfide connectivity, and membrane active properties indicated by their antimicrobial activities against Escherichia coli and cytotoxicities to HeLa cells.
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Engineering a Catalytically Efficient Recombinant Protein Ligase
TL;DR: The structure-based engineering of OaAEP1 described here provides a unique and novel recombinant tool that can now be used to conduct various protein labeling and modifications that were extremely challenging before.
Journal ArticleDOI
Butelase 1: A Versatile Ligase for Peptide and Protein Macrocyclization.
TL;DR: A highly efficient method using butelase 1 to macrocyclize peptides and proteins ranging in sizes from 26 to >200 residues, achieving cyclizations that are 20,000 times faster than sortase A, the most widely used ligase for protein cyclization.