W. Tay

发表

1H NMR, mechanism, and mononuclear oxidative activity of the antibiotic metallopeptide bacitracin: the role of D-Glu-4, interaction with pyrophosphate moiety, DNA binding and cleavage, and bioactivity.

J. Epperson, L. Ming, W. Tay, 2010, Journal of the American Chemical Society.

Casein Kinase II Induced Polymerization of Soluble TDP-43 into Filaments Is Inhibited by Heat Shock Proteins

L. Petrucelli, Wen‐lang Lin, Y. Carlomagno, 2014, PloS one.

A plausible role of salivary copper in antimicrobial activity of histatin-5--metal binding and oxidative activity of its copper complex.

A. Angerhofer, L. Ming, W. Tay, 2009, Bioorganic & medicinal chemistry letters.

Metal binding of flavonoids and their distinct inhibition mechanisms toward the oxidation activity of Cu2+-β-amyloid: not just serving as suicide antioxidants!

L. Ming, W. Tay, Giordano F. Z. da Silva, 2013, Inorganic chemistry.

Metallopeptides as model systems for the study of Cu(II)-dependent oxidation chemistry

W. Tay, 2008 .

Catechol oxidase-like oxidation chemistry of the 1-20 and 1-16 fragments of Alzheimer's disease-related beta-amyloid peptide: their structure-activity correlation and the fate of hydrogen peroxide.

L. Ming, W. Tay, Giordano F. Z. da Silva, 2005, The Journal of biological chemistry.

Mechanistic role of each metal ion in Streptomyces dinuclear aminopeptidase: PEPTIDE hydrolysis and 7x10(10)-fold rate enhancement of phosphodiester hydrolysis.

A. Ercan, L. Ming, S. Grossman, 2010, Journal of inorganic biochemistry.

Targeted manipulation of the sortilin–progranulin axis rescues progranulin haploinsufficiency

L. Petrucelli, I. Mackenzie, Jeannie Chew, 2013, Human molecular genetics.

Capturing a Reactive State of Amyloid Aggregates

D. McElheny, Y. Ishii, S. Parthasarathy, 2014, The Journal of Biological Chemistry.

Biophysical analyses of synthetic amyloid-beta(1-42) aggregates before and after covalent cross-linking. Implications for deducing the structure of endogenous amyloid-beta oligomers.

T. Rosenberry, N. Milkovic, Vijayaraghavan Rangachari, 2009, Biochemistry.

The Alzheimer's amyloid-β(1-42) peptide forms off-pathway oligomers and fibrils that are distinguished structurally by intermolecular organization.

T. Rosenberry, A. Paravastu, Anant K. Paravastu, 2013, Journal of molecular biology.

A mass spectrometric approach for characterization of amyloid-β aggregates and identification of their post-translational modifications.

T. Rosenberry, B. Cusack, W. Tay, 2012, Biochemistry.

Catechol Oxidase-like Oxidation Chemistry of the 1–20 and 1–16 Fragments of Alzheimer's Disease-related β-Amyloid Peptide

L. Ming, W. Tay, Giordano F. Z. da Silva, 2005, Journal of Biological Chemistry.