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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-3
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pubmed:dateCreated |
2003-5-19
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pubmed:abstractText |
Exposure to microwave radiation enhances the aggregation of bovine serum albumin in vitro in a time- and temperature-dependent manner. Microwave radiation also promotes amyloid fibril formation by bovine insulin at 60 degrees C. These alterations in protein conformation are not accompanied by measurable temperature changes, consistent with estimates from field modelling of the specific absorbed radiation (15-20 mW kg(-1)). Limited denaturation of cellular proteins could explain our previous observation that modest heat-shock responses are induced by microwave exposure in Caenorhabditis elegans. We also show that heat-shock responses both to heat and microwaves are suppressed after RNA interference ablating heat-shock factor function.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
543
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
93-7
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:12753912-Amyloid,
pubmed-meshheading:12753912-Caenorhabditis elegans Proteins,
pubmed-meshheading:12753912-Heat-Shock Proteins,
pubmed-meshheading:12753912-Hot Temperature,
pubmed-meshheading:12753912-Insulin,
pubmed-meshheading:12753912-Microwaves,
pubmed-meshheading:12753912-Protein Conformation,
pubmed-meshheading:12753912-RNA Interference,
pubmed-meshheading:12753912-Serum Albumin, Bovine,
pubmed-meshheading:12753912-Transcription Factors
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pubmed:year |
2003
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pubmed:articleTitle |
Microwave radiation can alter protein conformation without bulk heating.
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pubmed:affiliation |
School of Life and Environmental Sciences, University of Nottingham, University Park, NG7 2RD, Nottingham, UK. david.depomerai@nottingham.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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