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Jeffrey S. Isenberg

Researcher at University of Pittsburgh

Publications -  87
Citations -  9264

Jeffrey S. Isenberg is an academic researcher from University of Pittsburgh. The author has contributed to research in topics: Thrombospondin 1 & Matricellular protein. The author has an hindex of 36, co-authored 85 publications receiving 8184 citations. Previous affiliations of Jeffrey S. Isenberg include National Institutes of Health.

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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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Nitric oxide regulates angiogenesis through a functional switch involving thrombospondin-1

TL;DR: A triphasic regulation of TSP1 mediated by a slow and prolonged release of NO that depends on ERK phosphorylation is demonstrated, suggesting that dose-dependent positive- and negative-feedback loops exist between NO and T SP1.
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Regulation of nitric oxide signalling by thrombospondin 1: implications for anti-angiogenic therapies

TL;DR: The first identified endogenous angiogenesis inhibitor, thrombospondin 1, also controls tissue perfusion, haemostasis and radiosensitivity by antagonizing NO signalling and is examined in cancer.
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The biphasic nature of nitric oxide responses in tumor biology

TL;DR: The biphasic nature of NO in cancer biology and the implications of NO-driven redox flux for modulation of tumor-stimulated angiogenesis, growth, and metastasis are discussed.
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Nitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathways

TL;DR: It is suggested that NO regulation of MMP-9 secreted from macrophages may occur chemically by reactive nitrogen species-mediated protein modification, biologically through soluble guanylyl-cyclase-dependent modulation of the M MP-9/TIMP-1 balance, or proteolytically through regulation ofMMP-1 and -13, which can cleave the prodomain of Mmp-9.