Production of 35S-labeled proteins in E. coli and their use as molecular probes
- PMID: 7921035
- DOI: 10.1385/0-89603-258-2:389
Production of 35S-labeled proteins in E. coli and their use as molecular probes
Similar articles
-
Metabolically 35S-labeled recombinant calmodulin as a ligand for the detection of calmodulin-binding proteins.Anal Biochem. 1989 Apr;178(1):141-7. doi: 10.1016/0003-2697(89)90370-9. Anal Biochem. 1989. PMID: 2658683
-
Selective isotope labeling of recombinant proteins in Escherichia coli.Methods Mol Biol. 2012;896:439-48. doi: 10.1007/978-1-4614-3704-8_30. Methods Mol Biol. 2012. PMID: 22821543
-
Production of reagents and optimization of methods for studying calmodulin-binding proteins.Protein Expr Purif. 1999 Feb;15(1):24-33. doi: 10.1006/prep.1998.0983. Protein Expr Purif. 1999. PMID: 10024466
-
In situ hybridization with 35S-labeled probes for retinoid receptors.Methods Mol Biol. 1998;89:247-67. doi: 10.1385/0-89603-438-0:247. Methods Mol Biol. 1998. PMID: 9664333 Review. No abstract available.
-
Labeled glucose analogs in the genomic era.J Nucl Med. 2003 Jul;44(7):1082-6. J Nucl Med. 2003. PMID: 12843225 Review. No abstract available.
Cited by
-
Calmodulin and Calmodulin Binding Proteins in Dictyostelium: A Primer.Int J Mol Sci. 2020 Feb 11;21(4):1210. doi: 10.3390/ijms21041210. Int J Mol Sci. 2020. PMID: 32054133 Free PMC article. Review.
-
Two synthetic peptides corresponding to the proximal heme-binding domain and CD1 domain of human endothelial nitric-oxide synthase inhibit the oxygenase activity by interacting with CaM.Arch Biochem Biophys. 2009 Jun 15;486(2):132-40. doi: 10.1016/j.abb.2009.03.015. Epub 2009 Apr 7. Arch Biochem Biophys. 2009. PMID: 19358819 Free PMC article.
-
Binding property of avian skeletal muscle ryanodine receptor isoforms with dihydropyridine receptor and calmodulin.J Muscle Res Cell Motil. 2007;28(1):59-66. doi: 10.1007/s10974-007-9106-9. Epub 2007 May 16. J Muscle Res Cell Motil. 2007. PMID: 17505897
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources