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Articles by Mark Larance
Feeding-regulated glycogen metabolism drives rhythmic liver protein secretion - Nature Metabolism
Abstract The liver has a key role in inter-organ communication by secreting most circulating plasma proteins. However, the mechanisms governing hepatic protein secretion remain unclear. Here we show that hepatic protein secretion follows a diurnal rhythm regulated by food intake in humans and mice.
Uncovering bacterial pseudaminylation with pan-specific antibody tools - Nature Chemical Biology
Abstract Pseudaminic acids (Pse) are a family of carbohydrates found within bacterial lipopolysaccharides, capsular polysaccharides and glycoproteins that are critical for the virulence of human pathogens. However, a dearth of effective tools for detecting and enriching Pse has restricted study to only the most abundant Pse-containing glycoconjugates.
ClpC1-targeting peptide natural products differentially dysregulate the proteome of Mycobacterium tuberculosis - Nature Communications
Abstract Targeting the protein quality control system in Mycobacterium tuberculosis represents a promising and underexplored opportunity for antibiotic development. The ClpC1:ClpP1P2 protease is an essential component of the system that mediates both regulatory and stress-related protein degradation.
Chronic diseases alter the platelet rheostat to promote hyperreactivity and thrombosis
Abstract Platelet hyperreactivity, defined as enhanced sensitivity to activation in response to classical agonists, contributes to the increased risk of arterial thrombosis associated with chronic inflammatory diseases. In this issue of the JCI, Kong and colleagues used an unbiased proteomic approach to identify elevated SEC61B in platelets from patients with diabetes and from hyperglycemic mice.
Integrated liver-secreted and plasma proteomics identify a predictive model that stratifies MASH
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ArticleOnline now102085Open access 1Department of Anatomy and Physiology, School of Biomedical Sciences, Faculty of Medicine, Dentistry & Health Sciences, The University of Melbourne, Melbourne, VIC 3010, Australia 2Department of Surgery, School of Translational Medicine, Monash University, Melbourne, VIC 3004, Australia 3Bariatric Unit, Department of General Surgery, The Alfred Hospital, Melbourne, VIC 3004, Australia 4TissuPath, Mount Waverley, VIC 3149, Australia 5Department of Oncology,...
By William De Nardo, Olivia Lee, Jacqueline A. Bayliss, Paula M. Miotto, Stacey Keenan, Andrew Ryan, Amber Rucinski, Geraldine Ooi, Wendy Brown, William P. Kemp, Stuart Roberts, BENJAMIN Parker, Magdalene K. Montgomery, Mark Larance, Paul Burton, Matthew J. Watt, Yazmin Johari, Marcus Pensa, Tessa M. Svinos
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Cell Reports Medicine
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Protein O-Fucosyltransferases: Biological Functions and Molecular Mechanisms in Mammals
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FUT10 and FUT11 are protein O-fucosyltransferases that modify protein EMI domains - Nature Chemical Biology
Abstract O-Fucosylation plays crucial roles in various essential biological events. Alongside the well-established O-fucosylation of epidermal growth factor-like repeats by protein O-fucosyltransferase 1 (POFUT1) and thrombospondin type 1 repeats by POFUT2, we recently identified a type of O-fucosylation on the elastin microfibril interface (EMI) domain of Multimerin-1 (MMRN1).
GDF15 increases insulin action in the liver and adipose tissue via a β-adrenergic receptor-mediated mechanism
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Site-selective photocatalytic functionalization of peptides and proteins at selenocysteine - Nature Communications
Abstract The importance of modified peptides and proteins for applications in drug discovery, and for illuminating biological processes at the molecular level, is fueling a demand for efficient methods that facilitate the precise modification of these biomolecules. Herein, we describe the development of a photocatalytic method for the rapid and efficient dimerization and site-specific functionalization of peptide and protein diselenides.
Chemical Synthesis of Phosphorylated Insulin-like Growth Factor Binding Protein 2
Chemical protein synthesis is a powerful avenue for accessing homogeneously modified proteins. While a significant number of small modified proteins bearing native post-translational modifications and non-natural modifications have been generated to date, access to larger targets has proved challenging.
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