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A mechanism for memory storage insensitive to molecular turnover: a bistable autophosphorylating kinase.

作者信息

Lisman J E

出版信息

Proc Natl Acad Sci U S A. 1985 May;82(9):3055-7. doi: 10.1073/pnas.82.9.3055.

DOI:10.1073/pnas.82.9.3055
PMID:2986148
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC397705/
Abstract

A mechanism is proposed for a molecular switch that can store information indefinitely, despite the complete turnover of the molecules that make up the switch. The design of the switch is based on known types of biochemical reactions. Central to the mechanism is a kinase that is activated by phosphorylation and capable of intermolecular autophosphorylation. It is shown that such a kinase and an associated phosphatase form a bistable chemical switch that can be turned on by an external stimulus and that is not reset by protein turnover.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ff6/397705/ccac891cf674/pnas00349-0511-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ff6/397705/ccac891cf674/pnas00349-0511-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ff6/397705/ccac891cf674/pnas00349-0511-a.jpg

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本文引用的文献

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Priestia megaterium cells are primed for surviving lethal doses of antibiotics and chemical stress.巨大芽孢杆菌细胞能够在致死剂量的抗生素和化学应激下存活。
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