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Zhicheng Pan

Researcher at University of California, Los Angeles

Publications -  20
Citations -  840

Zhicheng Pan is an academic researcher from University of California, Los Angeles. The author has contributed to research in topics: Gene & RNA splicing. The author has an hindex of 12, co-authored 19 publications receiving 633 citations. Previous affiliations of Zhicheng Pan include University of California, Berkeley & University of Science and Technology of China.

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Journal ArticleDOI

The Expanding Landscape of Alternative Splicing Variation in Human Populations.

TL;DR: Technological advances that have greatly increased the speed and scale at which discoveries are made about the genetic variation of alternative splicing are described.
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CPLM: a database of protein lysine modifications

TL;DR: The various PLM crosstalks suggested that a considerable proportion of lysines were competitively and dynamically regulated in a complicated manner and can serve as a useful resource for further research of PLMs.
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Deep-learning augmented RNA-seq analysis of transcript splicing.

TL;DR: DARTS first uses public domain data to train a deep neural network to predict differential alternativesplicing; the predictions are then combined with observed RNA-seq data in a Bayesian framework to infer changes in alternative splicing between biological samples.
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EKPD: a hierarchical database of eukaryotic protein kinases and protein phosphatases

TL;DR: A hierarchical database of eukaryotic protein kinases (PKs) and protein phosphatases (PPs), the key molecules responsible for the reversible phosphorylation of proteins that are involved in almost all aspects of biological processes, is presented.
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Systematic analysis of the in situ crosstalk of tyrosine modifications reveals no additional natural selection on multiply modified residues.

TL;DR: The systematic analyses provided a better understanding of the in situ crosstalk among PTMs and suggested that sulfation and nitration preferentially co-occur with phosphorylation at specific positions in proteins, and participate in distinct biological processes and functions.