M
Mo Chen
Researcher at Columbia University
Publications - 12
Citations - 3128
Mo Chen is an academic researcher from Columbia University. The author has contributed to research in topics: Alternative splicing & Exon. The author has an hindex of 9, co-authored 10 publications receiving 2684 citations. Previous affiliations of Mo Chen include Rockefeller University.
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Journal ArticleDOI
Mechanisms of alternative splicing regulation: insights from molecular and genomics approaches
Mo Chen,James L. Manley +1 more
TL;DR: Great progress has been made by studying individual transcripts and through genome-wide approaches, which together provide a better picture of the mechanistic regulation of alternative pre-mRNA splicing.
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HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer
TL;DR: A pathway that regulates an alternative splicing event required for tumour cell proliferation is defined, establishing a relevance to cancer, and it is demonstrated that human gliomas overexpress c-Myc, PTB, hnRNPA1 and hn RNPA2 in a manner that correlates with PKM2 expression.
Journal ArticleDOI
TGF-β Tumor Suppression Through A Lethal EMT
Charles J. David,Yun-Han Huang,Mo Chen,Jie Su,Yilong Zou,Nabeel Bardeesy,Christine A. Iacobuzio-Donahue,Joan Massagué +7 more
TL;DR: It is shown that TGF-β tumor suppression functions through an EMT-mediated disruption of a lineage-specific transcriptional network, including the repression of the gastrointestinal lineage-master regulator Klf5.
Journal ArticleDOI
Turning on a fuel switch of cancer: hnRNP proteins regulate alternative splicing of pyruvate kinase mRNA.
TL;DR: A recent study shows that the alternative splicing event is controlled by heterogeneous nuclear ribonucleoprotein (hnRNP) family members hnRNPA1, hn RNPA2, and polypyrimidine tract binding protein (PTB; also known as hnRNAPI).
Journal ArticleDOI
Phosphorylation switches the general splicing repressor SRp38 to a sequence-specific activator
TL;DR: Analysis of alternative splicing of pre-mRNA encoding the glutamate receptor B revealed that SRp38 alters its splicing pattern in a sequence-specific manner, demonstrating thatSRp38, in addition to its role as a splicing repressor, can function as an unusual sequence- specific splicing activator.