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Ji Man Park

Researcher at University of Minnesota

Publications -  21
Citations -  2531

Ji Man Park is an academic researcher from University of Minnesota. The author has contributed to research in topics: Protein kinase A & AMPK. The author has an hindex of 18, co-authored 21 publications receiving 1432 citations. Previous affiliations of Ji Man Park include Ulsan National Institute of Science and Technology & Pohang University of Science and Technology.

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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Daniel J. Klionsky, +2983 more
- 08 Feb 2021 - 
TL;DR: In this article, the authors present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes.
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The ULK1 complex mediates MTORC1 signaling to the autophagy initiation machinery via binding and phosphorylating ATG14

TL;DR: A key molecular event is defined for the starvation-induced activation of the ATG14-containing PtdIns3K complex by ULK1, and hierarchical relations between the ULK 1 activation and other autophagy proteins involved in phagophore formation are demonstrated.
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mTORC1 phosphorylates UVRAG to negatively regulate autophagosome and endosome maturation.

TL;DR: It is demonstrated that mTORC1 engages in late stages of autophagy and endosome maturation, defining a broader range of m TORC1 functions in the membrane-associated processes.
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ULK1 phosphorylates Ser30 of BECN1 in association with ATG14 to stimulate autophagy induction.

TL;DR: It is demonstrated that BECN1 Ser30 is a ULK1 target site whose phosphorylation activates the ATG14-containing PIK3C3 complex and stimulates autophagosome formation in response to amino acid starvation, hypoxia, and MTORC1 inhibition.
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Human mesenchymal stem cell differentiation to the osteogenic or adipogenic lineage is regulated by AMP‐activated protein kinase

TL;DR: It is demonstrated that AMPK is a critical regulatory factor for osteogenic differentiation and suggested that commitment of hAMSC to osteogenic or adipogenic lineage is governed by activation or inhibition of AMPK, respectively.