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Hui Kuan Lin

Researcher at Wake Forest University

Publications -  127
Citations -  14265

Hui Kuan Lin is an academic researcher from Wake Forest University. The author has contributed to research in topics: Phosphorylation & Cancer. The author has an hindex of 55, co-authored 120 publications receiving 12543 citations. Previous affiliations of Hui Kuan Lin include Asia University (Taiwan) & Wake Forest Baptist Medical Center.

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Crucial role of p53-dependent cellular senescence in suppression of Pten-deficient tumorigenesis

TL;DR: It is shown that conditional inactivation of Trp53 in the mouse prostate fails to produce a tumour phenotype, whereas complete Pten inactivation in the prostate triggers non-lethal invasive prostate cancer after long latency, and support a model for cooperative tumour suppression in which p53 is an essential failsafe protein of Pten-deficient tumours.
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BCR-ABL independence and LYN kinase overexpression in chronic myelogenous leukemia cells selected for resistance to STI571.

TL;DR: Comparison of samples from patients taken prior to and following STI571 failure suggested that expression and/or activation of LYN/HCK occurs during disease progression, and results suggest that acquired STi571 resistance may be associated with BCR-ABL independence and mediated in part through overexpression of other tyrosine kinases.
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From HER2/Neu signal cascade to androgen receptor and its coactivators: A novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells

TL;DR: It is demonstrated that the growth of prostate cancer LNCaP cells can also be increased by the stable transfection of HER2/Neu, and this may represent one of the reasons for the PSA re-elevation and hormone resistance during androgen ablation therapy in prostate cancer patients.
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The E3 Ligase TRAF6 Regulates Akt Ubiquitination and Activation

TL;DR: It is found that the protein kinase Akt undergoes lysine-63 chain ubiquitination, which is important for Akt membrane localization and phosphorylation, and is an important step for oncogenic Akt activation.
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The Mechanisms of PML-Nuclear Body Formation

TL;DR: It is demonstrated that PML contains a SUMO binding motif that is independent of its SUMOylation sites and is surprisingly necessary for PML-NB formation, and it is proposed that the PML RING domain is critical forPML SUMoylation and PML -NB formation.