Intrinsically Disordered Proteins

Known as: Intrinsically Disordered Proteins [Chemical/Ingredient], Natively Unfolded Proteins, Unstructured Proteins 
Functional proteins that do not have unique, stable, folded, three-dimensional native structures or that possess non-ordered regions under… (More)
National Institutes of Health

Papers overview

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Review
2014
Review
2014
Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities… (More)
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Review
2014
Review
2014
Intrinsically disordered proteins (IDPs) are important components of the cellular signalling machinery, allowing the same… (More)
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Review
2011
Review
2011
Intrinsically disordered proteins (IDPs) are enriched in signaling and regulatory functions because disordered segments permit… (More)
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Highly Cited
2010
Highly Cited
2010
Protein intrinsic disorder is becoming increasingly recognized in proteomics research. While lacking structure, many regions of… (More)
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Review
2008
Review
2008
Intrinsically disordered proteins (IDPs) lack stable tertiary and/or secondary structures under physiological conditions in vitro… (More)
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Highly Cited
2007
Highly Cited
2007
The Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs… (More)
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Review
2005
Review
2005
Many gene sequences in eukaryotic genomes encode entire proteins or large segments of proteins that lack a well-structured three… (More)
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Highly Cited
2005
Highly Cited
2005
The structural stability of a protein requires a large number of interresidue interactions. The energetic contribution of these… (More)
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Highly Cited
2002
Highly Cited
2002
The number of intrinsically disordered proteins known to be involved in cell-signaling and regulation is growing rapidly. To test… (More)
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Review
1999
Review
1999
A major challenge in the post-genome era will be determination of the functions of the encoded protein sequences. Since it is… (More)
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