Natively unfolded proteins.

@article{Fink2005NativelyUP,
  title={Natively unfolded proteins.},
  author={Anthony L. Fink},
  journal={Current opinion in structural biology},
  year={2005},
  volume={15 1},
  pages={
          35-41
        }
}
It is now clear that a significant fraction of eukaryotic genomes encode proteins with substantial regions of disordered structure. In spite of the lack of structure, these proteins nevertheless are functional; many are involved in critical steps of the cell cycle and regulatory processes. In general, intrinsically disordered proteins interact with a target ligand (often DNA) and undergo a structural transition to a folded form when bound. Several features of intrinsically disordered proteins… CONTINUE READING
Highly Influential
This paper has highly influenced 15 other papers. REVIEW HIGHLY INFLUENTIAL CITATIONS
Highly Cited
This paper has 371 citations. REVIEW CITATIONS

From This Paper

Figures, tables, and topics from this paper.

Explore Further: Topics Discussed in This Paper

Citations

Publications citing this paper.
Showing 1-10 of 203 extracted citations

Off-pathway status for the alkali molten globule of horse ferricytochrome C.

Biochemistry • 2010
View 4 Excerpts
Method Support
Highly Influenced

Protein Misfolding and Cellular Stress in Disease and Aging

Methods in Molecular Biology • 2010
View 10 Excerpts
Highly Influenced

371 Citations

0204060'07'10'13'16'19
Citations per Year
Semantic Scholar estimates that this publication has 371 citations based on the available data.

See our FAQ for additional information.