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Alice C. L. Len

Researcher at University of Sydney

Publications -  11
Citations -  696

Alice C. L. Len is an academic researcher from University of Sydney. The author has contributed to research in topics: Proteome & Membrane protein. The author has an hindex of 10, co-authored 11 publications receiving 647 citations. Previous affiliations of Alice C. L. Len include Millennium Institute & University College London.

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Stress-responsive proteins are upregulated in Streptococcus mutans during acid tolerance

TL;DR: Differential two-dimensional electrophoretic proteome analysis of S. mutans grown at steady state in continuous culture at pH 7.0 or pH 5.0 enabled the resolution of 199 cellular and extracellular protein spots with altered levels of expression and identified 61 protein spots associated with stress-responsive pathways involved in DNA replication, transcription, translation, protein folding and proteolysis.
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Proteome analysis of Streptococcus mutans metabolic phenotype during acid tolerance.

TL;DR: Two-dimensional gel electrophoretic analysis of the proteome of Streptococcus mutans grown at a steady state in a glucose-limited anaerobic continuous culture revealed a number of proteins that were differentially expressed when the growth pH was lowered from pH 7.0 to pH 5.0.
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Identification of membrane‐associated proteins from Campylobacter jejuni strains using complementary proteomics technologies

TL;DR: This study provides a comprehensive analysis of membrane‐associated proteins from C. jejuni and identified 28 proteins that were significantly (>two‐fold) more abundant in, or unique to, JHH1, including eight proteins involved in chemotaxis signal transduction and flagellar motility.
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Characterization of the rat liver membrane proteome using peptide immobilized pH gradient isoelectric focusing.

TL;DR: Utility of 60% (v/v) methanol assisted digestion in conjunction with peptide IPG-IEF as an optimal shotgun proteomics technique for the separation and identification of previously unreported membrane proteins is proved.
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Retromer regulates HIV-1 envelope glycoprotein trafficking and incorporation into virions.

TL;DR: The mammalian retromer complex is identified as a novel and important cellular factor regulating Env trafficking and infectious HIV-1 morphogenesis and shown for the first time a role forretromer in the late-steps of viral replication and assembly of a virus.