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Marina K. Holz

Researcher at New York Medical College

Publications -  42
Citations -  9250

Marina K. Holz is an academic researcher from New York Medical College. The author has contributed to research in topics: PI3K/AKT/mTOR pathway & Estrogen receptor. The author has an hindex of 21, co-authored 39 publications receiving 8291 citations. Previous affiliations of Marina K. Holz include Harvard University & Yeshiva University.

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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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mTOR and S6K1 Mediate Assembly of the Translation Preinitiation Complex through Dynamic Protein Interchange and Ordered Phosphorylation Events

TL;DR: The eIF3 preinitiation complex acts as a scaffold to coordinate a dynamic sequence of events in response to stimuli that promote efficient protein synthesis.
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RAS/ERK Signaling Promotes Site-specific Ribosomal Protein S6 Phosphorylation via RSK and Stimulates Cap-dependent Translation

TL;DR: Evidence is provided that activation of the p90 ribosomal S6 kinases (RSKs) by serum, growth factors, tumor promoting phorbol esters, and oncogenic Ras provides an mTOR-independent pathway linking the Ras/ERK signaling cascade to the translational machinery.
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The therapeutic potential of resveratrol: a review of clinical trials.

TL;DR: It is found that for neurological disorders, cardiovascular diseases, and diabetes, the current clinical trials show that resveratrol was well tolerated and beneficially influenced disease biomarkers, however resver atrol had ambiguous and sometimes even detrimental effects in certain types of cancers and in NAFLD.
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Identification of S6 Kinase 1 as a Novel Mammalian Target of Rapamycin (mTOR)-phosphorylating Kinase

TL;DR: It is shown that S6 kinase 1 (S6K1), but not Akt, directly phosphorylates mTOR in cell-free in vitro system and in cells, and phosphorylated at threonine 2446/serine 2448, which has been shown previously to be part of a regulatory repressor domain.