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Guo-Liang Chew

Researcher at Fred Hutchinson Cancer Research Center

Publications -  20
Citations -  1761

Guo-Liang Chew is an academic researcher from Fred Hutchinson Cancer Research Center. The author has contributed to research in topics: Translation (biology) & Open reading frame. The author has an hindex of 12, co-authored 20 publications receiving 1387 citations. Previous affiliations of Guo-Liang Chew include Massachusetts Institute of Technology & Harvard University.

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Toddler: an embryonic signal that promotes cell movement via Apelin receptors.

TL;DR: Toddler is an essential, short, conserved embryonic signal that promotes cell migration during zebrafish gastrulation and helps explain previous genetic studies that found a broader requirement for APJ/Apelin receptors than for Apelin, and may be one of several uncharacterized embryonic signals.
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Ribosome profiling reveals resemblance between long non-coding RNAs and 5′ leaders of coding RNAs

TL;DR: It is found that dozens of proposed lncRNAs are protein-coding contaminants and that many lnc RNAs have ribosome profiles that resemble the 5′ leaders of coding RNAs.
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Site-Specific N- and C-Terminal Labeling of a Single Polypeptide Using Sortases of Different Specificity

TL;DR: The generality of N-terminal labeling with SrtAstaph is demonstrated by near-quantitative labeling of multiple protein substrates with excellent site specificity.
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Conservation of uORF repressiveness and sequence features in mouse, human and zebrafish

TL;DR: Analysis of transcript sequences and ribosome profiling data from human, mouse and zebrafish finds that uORFs are depleted near coding sequences (CDSes) and have initiation contexts that diminish their translation, suggesting that the prevalence of vertebrate UORFs may be explained by their conserved role in repressing CDS translation.
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A Straight Path to Circular Proteins

TL;DR: It is shown that circular proteins can be made reversibly with excellent efficiency by means of a sortase-catalyzed cyclization reaction, requiring only minimal modification of the protein to be circularized.