Juliet A. Gerrard

1-11 Short Street
Auckland, AUK 1010, New Zealand

Last Updated: 09/26/2026

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Found 63 publications

The Leptospermum scoparium (Mānuka)-Specific Nectar and Honey Compound 3,6,7-Trimethyllumazine (LepteridineTM) That Inhibits Matrix Metalloproteinase 9 (MMP-9) Activity.

The Leptospermum scoparium (Mānuka)-Specific Nectar and Honey Compound 3,6,7-Trimethyllumazine (LepteridineTM) That Inhibits Matrix Metalloproteinase 9 (MMP-9) Activity.

Journal: Foods (Basel, Switzerland)

Published: September 26, 2023

Insight into the self-assembly and gel formation of a bioactive peptide derived from bovine casein.

Insight into the self-assembly and gel formation of a bioactive peptide derived from bovine casein.

Journal: BBA advances

Published: June 28, 2023

Characterizing lysinoalanine crosslinks in food systems: Discovery of a diagnostic ion in model peptides using MALDI mass spectrometry.

Characterizing lysinoalanine crosslinks in food systems: Discovery of a diagnostic ion in model peptides using MALDI mass spectrometry.

Journal: Food chemistry: X

Published: April 15, 2023

Corrigendum to "Reaction dynamics and residue identification of haemoglobin modification by acrolein, a lipid-peroxidation by-product" [Biochimica et Biophysica Acta (BBA) - General Subjects Volume 1865, Issue 12, December 2021, 130013].

Corrigendum to "Reaction dynamics and residue identification of haemoglobin modification by acrolein, a lipid-peroxidation by-product" [Biochimica et Biophysica Acta (BBA) - General Subjects Volume 1865, Issue 12, December 2021, 130013].

Journal: Biochimica et biophysica acta. General subjects

Published: March 07, 2022

Juliet A. Gerrard.

Juliet A. Gerrard.

Journal: Current biology : CB

Published: May 25, 2021

Reaction dynamics and residue identification of haemoglobin modification by acrolein, a lipid-peroxidation by-product.

Reaction dynamics and residue identification of haemoglobin modification by acrolein, a lipid-peroxidation by-product.

Journal: Biochimica et biophysica acta. General subjects

Published: May 14, 2021

A Case Study of the Response of Immunogenic Gluten Peptides to Sourdough Proteolysis.

A Case Study of the Response of Immunogenic Gluten Peptides to Sourdough Proteolysis.

Journal: Nutrients

Published: April 30, 2021

Oral delivery of self-assembling bioactive peptides to target gastrointestinal tract disease.

Oral delivery of self-assembling bioactive peptides to target gastrointestinal tract disease.

Journal: Food & function

Published: November 06, 2020

The effect of baking time and temperature on gluten protein structure and celiac peptide digestibility.

The effect of baking time and temperature on gluten protein structure and celiac peptide digestibility.

Journal: Food research international (Ottawa, Ont.)

Published: July 28, 2020

The effect of dough mixing speed and work input on the structure, digestibility and celiac immunogenicity of the gluten macropolymer within bread.

The effect of dough mixing speed and work input on the structure, digestibility and celiac immunogenicity of the gluten macropolymer within bread.

Journal: Food chemistry

Published: July 16, 2020

A targeted mass spectrometry method for the accurate label-free quantification of immunogenic gluten peptides produced during simulated digestion of food matrices.

A targeted mass spectrometry method for the accurate label-free quantification of immunogenic gluten peptides produced during simulated digestion of food matrices.

Journal: MethodsX

Published: July 02, 2020

Directed self-assembly of peptide-diketopyrrolopyrrole conjugates - a platform for bio-organic thin film preparation.

Directed self-assembly of peptide-diketopyrrolopyrrole conjugates - a platform for bio-organic thin film preparation.

Journal: Soft matter

Published: June 27, 2020

Showing 1-12 of 63

Last Updated: 09/26/2026