"Protein Renaturation" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
The reconstitution of a protein's activity following denaturation.
- Protein Renaturation
- Protein Renaturations
- Renaturations, Protein
- Renaturation, Protein
Below are MeSH descriptors whose meaning is more general than "Protein Renaturation".
Below are MeSH descriptors whose meaning is more specific than "Protein Renaturation".
This graph shows the total number of publications written about "Protein Renaturation" by people in this website by year, and whether "Protein Renaturation" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
|Year||Major Topic||Minor Topic||Total|
To return to the timeline, click here.
Below are the most recent publications written about "Protein Renaturation" by people in Profiles.
De Zoysa Ariyananda L, Antonopoulos C, Currier J, Colman RF. In vitro hybridization and separation of hybrids of human adenylosuccinate lyase from wild-type and disease-associated mutant enzymes. Biochemistry. 2011 Mar 1; 50(8):1336-46.
Bhardwaj A, Walker-Kopp N, Wilkens S, Cingolani G. Foldon-guided self-assembly of ultra-stable protein fibers. Protein Sci. 2008 Sep; 17(9):1475-85.
Lefebvre BG, Comolli NK, Gage MJ, Robinson AS. Pressure dissociation studies provide insight into oligomerization competence of temperature-sensitive folding mutants of P22 tailspike. Protein Sci. 2004 Jun; 13(6):1538-46.
Gage MJ, Robinson AS. C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer. Protein Sci. 2003 Dec; 12(12):2732-47.