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Sze-Kwan Lam

Researcher at University of Hong Kong

Publications -  53
Citations -  1618

Sze-Kwan Lam is an academic researcher from University of Hong Kong. The author has contributed to research in topics: Apoptosis & Viability assay. The author has an hindex of 19, co-authored 49 publications receiving 1440 citations. Previous affiliations of Sze-Kwan Lam include Li Ka Shing Faculty of Medicine, University of Hong Kong & The Chinese University of Hong Kong.

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Lectins: production and practical applications

TL;DR: Lectins manifest a diversity of activities including antitumor, immunomodulatory, antifungal, HIV-1 reverse transcriptase inhibitory, and anti-insect activities, which may find practical applications.
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First simultaneous isolation of a ribosome inactivating protein and an antifungal protein from a mushroom (Lyophyllum shimeji) together with evidence for synergism of their antifungal effects.

TL;DR: A synergism in antifungal activities of LAP and lyophyllin against P. piricola was demonstrable and an N-terminal sequence somewhat analogous to those of angiosperm thaumatin-like proteins and thaumatins and an inactive variant of the ubiquitin-conjugating enzyme was demonstrated.
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Hypsin, a novel thermostable ribosome-inactivating protein with antifungal and antiproliferative activities from fruiting bodies of the edible mushroom Hypsizigus marmoreus.

TL;DR: A novel ribosome-inactivating protein with a molecular weight of 20 kDa was isolated from fruiting bodies of the mushroom Hypsizigus marmoreus and demonstrated an inhibitory action against mycelial growth in various fungal species.
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Erlotinib-induced autophagy in epidermal growth factor receptor mutated non-small cell lung cancer.

TL;DR: Erlotinib can induce both apoptosis and autophagy in sensitive NSCLC cell lines with activating EGFR mutation (exon 19 del) and inhibition of autophagic proteins can further enhance sensitivity to erlot inib in EGFR-mutatedNSCLC, suggesting that autophamy may serve as a protective mechanism.
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A protein with antiproliferative, antifungal and HIV-1 reverse transcriptase inhibitory activities from caper (Capparis spinosa) seeds.

TL;DR: A protein exhibiting an N-terminal amino acid sequence with some similarity to imidazoleglycerol phosphate synthase was purified from fresh Capparis spinosa melon seeds and demonstrated a molecular mass of 38 kDa in gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, indicating that it was monomeric.