Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

MeSH Review:

Fluorescence Resonance Energy Transfer

Alley, S.C. et al., Wieland, G.D. et al., St Croix, C.M. et al., Bettio, A. et al., Sako, Y. et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on Fluorescence Resonance Energy Transfer

Single-molecule fluorescence-resonance energy transfer shows that EGF-EGFR complexes indeed form dimers at the molecular level [1].
In vivo interaction of EGR-4 and EGR-3 with NF-kappaB p65 was demonstrated by immunoprecipitation experiments and fluorescence-resonance-energy transfer (FRET) analysis showing interaction in the nucleus of transfected Jurkat T cells [2].
For the mutants without intrasubunit disulfides, the efficiency of fluorescence-resonance energy transfer was in accord with a model of gp45 being an open complex composed of two closed subunit interfaces and a third open interface separated by a distance of 35-38 A [3].
Fluorescence-labelled analogs of NPY, a 36-amino acid peptide amide, were synthesized by solid-phase peptide synthesis and used for fluorescence-resonance energy transfer studies to investigate the conformation [4].
Furthermore, fluorescence-resonance energy-transfer data showed that overexpression of green fluorescent protein-modified MT prevented NO-induced conformational changes, which are indicative of Zn(2+) release from thiolate clusters [5].

References

Single-molecule imaging of EGFR signalling on the surface of living cells. Sako, Y., Minoghchi, S., Yanagida, T. Nat. Cell Biol. (2000) [Pubmed]
Early growth response proteins EGR-4 and EGR-3 interact with immune inflammatory mediators NF-kappaB p50 and p65. Wieland, G.D., Nehmann, N., Müller, D., Eibel, H., Siebenlist, U., Sühnel, J., Zipfel, P.F., Skerka, C. J. Cell. Sci. (2005) [Pubmed]
Sliding clamp of the bacteriophage T4 polymerase has open and closed subunit interfaces in solution. Alley, S.C., Shier, V.K., Abel-Santos, E., Sexton, D.J., Soumillion, P., Benkovic, S.J. Biochemistry (1999) [Pubmed]
The neuropeptide Y monomer in solution is not folded in the pancreatic-polypeptide fold. Bettio, A., Dinger, M.C., Beck-Sickinger, A.G. Protein Sci. (2002) [Pubmed]
Nitric oxide-induced changes in intracellular zinc homeostasis are mediated by metallothionein/thionein. St Croix, C.M., Wasserloos, K.J., Dineley, K.E., Reynolds, I.J., Levitan, E.S., Pitt, B.R. Am. J. Physiol. Lung Cell Mol. Physiol. (2002) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

Editor

Share