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July 1, 1996BioEssays

Modulation by nitric oxide of metalloprotein regulatory activities

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Key result

Nitric oxide modulates metalloregulatory proteins, such as the iron regulatory protein, by interacting with metal clusters at critical allosteric sites during cellular stress responses.

Population

Cells with inducible nitric oxide synthase and metalloregulatory proteins

Design

Review

Authors

JDJean‐Claude DrapierCentre National de la Recherche ScientifiqueCBCécile BoutonEngelhardt Institute of Molecular Biology

Discussion

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Overview

May position NO as cellular stress signal in metal regulation; leaves open cardiovascular translation pending targeted studies.

Structured PICO

P
Population
Cells with inducible nitric oxide synthase and metalloregulatory proteins
E
Exposure
Nitric oxide (NO) or NO-derived molecules
O
Outcome
Modulation of metalloprotein regulatory activities (e.g., disruption of metal-thiolate clusters, switching of iron regulatory protein function)

Nitric oxide may act as a crucial cellular stress signal by modulating the function of metalloregulatory proteins via interaction with metal clusters.

Cite This Study

Drapier et al. (1996) reported a review. Nitric oxide was evaluated. Nitric oxide modulates metalloregulatory proteins, such as the iron regulatory protein, by interacting with metal clusters at critical allosteric sites during cellular stress responses.

synapsesocial.com/papers/6a9c9cf11bc549bb5bf7b8e4https://doi.org/10.1002/bies.950180706
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