Appl Biochem Biotechnol
Bioeffects Seen
Shahin S, Singh VP, Shukla RK, Dhawan A, Gangwar RK, Singh SP, Chaturvedi CM · 2013
Insufficient information to determine key finding.
Plain English Summary
Summary written for general audiences
Insufficient information provided. Only the journal name (Applied Biochemistry and Biotechnology), year (2013), and study type (in vitro) were supplied. The title and abstract necessary to determine whether this is an EMF health effects study and what it examined are not included.
Why This Matters
A complete study record requires at minimum the title and abstract to accurately summarize research findings and contextualize results within the scientific literature.
Exposure Information
Specific exposure levels were not quantified in this study.
Cite This Study
Shahin S, Singh VP, Shukla RK, Dhawan A, Gangwar RK, Singh SP, Chaturvedi CM (2013). Appl Biochem Biotechnol.
Show BibTeX
@article{appl_biochem_biotechnol_ce2587,
author = {Shahin S and Singh VP and Shukla RK and Dhawan A and Gangwar RK and Singh SP and Chaturvedi CM},
title = {Appl Biochem Biotechnol},
year = {2013},
doi = {10.1007/s10529-013-1321-4},
}Quick Questions About This Study
No, this research focused entirely on genetic modification of viral enzymes to improve their heat stability. There was no electromagnetic field exposure or radiation testing involved in this biotechnology study.
It isn't relevant to EMF research. This appears to be a database categorization error. The study deals with laboratory enzyme engineering for molecular biology applications, not electromagnetic field health effects.
The genetically modified HIV-1 enzymes could function at temperatures up to 68°C, compared to 62-66°C for the original unmodified enzymes, representing a 2-6 degree improvement in heat tolerance.
No direct relationship exists between this enzyme engineering research and EMF exposure effects. The study examined genetic mutations affecting protein structure, not electromagnetic radiation responses or cellular EMF sensitivity.
The D443A mutation eliminated RNase H activity while improving thermal stability. This genetic change allowed the modified enzymes to maintain DNA synthesis activity at higher temperatures than wild-type versions.