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Benjamin L. Schulz

Researcher at University of Queensland

Publications -  360
Citations -  25967

Benjamin L. Schulz is an academic researcher from University of Queensland. The author has contributed to research in topics: Galaxy & Glycosylation. The author has an hindex of 84, co-authored 348 publications receiving 24069 citations. Previous affiliations of Benjamin L. Schulz include ETH Zurich & University of Hawaii.

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The post-translational modification landscape of commercial beers

TL;DR: This paper used DIA/SWATH-MS data to investigate the proteomic complexity and diversity of 23 commercial Australian beers and found that proteins in darker beers tended to have low glycation and high proteolysis.
Posted ContentDOI

Post-translational modifications drive protein stability to control the dynamic beer brewing proteome

TL;DR: Correlation analysis of temperature-dependent abundance showed that sequence and structure were the main features that controlled protein abundance profiles and were preferentially lost at high mash temperatures, while intact proteins remained soluble.
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Serum proteomes of Santa Gertrudis cattle before and after infestation with Rhipicephalus australis ticks

TL;DR: In this article, the authors applied genomics and transcriptomics to identify immune and genetic markers as key indicator traits for cattle tick susceptibility/resistance; however, results differed between breeds, and there is lack of information on the use of host proteomics.
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Resonance Raman scattering of relaxors PbSc0.5Ta0.5O3 and PbSc0.5Nb0.5O3

TL;DR: In this article, the phonon modes associated with O localized BO6 vibrations in ferroic clusters strongly resonate in the vicinity of the maximum of the optical dielectric response function at 371eV Resonance Raman spectroscopy can be used to estimate the fraction and the average size of polar nanoclusters in the relaxor state.
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Glycoproteomic measurement of site-specific polysialylation.

TL;DR: This method measures site-specific PSA modification by using mild acid hydrolysis to eliminate PSA and sialic acids while leaving the glycan backbone intact, together with protease digestion followed by LC-ESI-MS/MS glycopeptide detection.