Results 301 to 310 of about 66,315 (318)

Intrinsic disorder in S100 proteins

Molecular BioSystems, 2011
Although the members of the largest subfamily of the EF-hand proteins, S100 proteins, are evolutionarily young, their functional diversity is extremely broad, partly due to their ability to adapt to various targets. This feature is a hallmark of intrinsically disordered proteins (IDPs), but none of the S100 proteins are recognized as IDPs.
Sergei E, Permyakov, Ramis G, Ismailov, Bin, Xue, Alexander I, Denesyuk, Vladimir N, Uversky, Eugene A, Permyakov   +5 more
openaire   +3 more sources

Frustration-induced protein intrinsic disorder

The Journal of Chemical Physics, 2013
Spontaneous folding into a specific native structure is the most important property of protein to perform their biological functions within organisms. Spontaneous folding is understood on the basis of an energy landscape picture based on the minimum frustration principle.
Katsuyoshi, Matsushita, Macoto, Kikuchi
openaire   +2 more sources

Exploring Protein Intrinsic Disorder with MobiDB

2020
Nowadays, it is well established that many proteins or regions under physiological conditions lack a fixed three-dimensional structure and are intrinsically disordered. MobiDB is the main repository of protein disorder and mobility annotations, combining different data sources to provide an exhaustive overview of intrinsic disorder.
Monzon A. M., Hatos A., Necci M., Piovesan D., Tosatto S. C. E.   +4 more
openaire   +2 more sources

Druggability of Intrinsically Disordered Proteins

2015
Although the proteins in all the current major classes considered to be druggable are folded in their native states, intrinsically disordered proteins (IDPs) are becoming attractive candidates for therapeutic intervention by small drug-like molecules.
Priyanka, Joshi, Michele, Vendruscolo
openaire   +2 more sources

Intrinsically disordered proteins: regulation and disease

Current Opinion in Structural Biology, 2011
Intrinsically disordered proteins (IDPs) are enriched in signaling and regulatory functions because disordered segments permit interaction with several proteins and hence the re-use of the same protein in multiple pathways. Understanding IDP regulation is important because altered expression of IDPs is associated with many diseases. Recent studies show
Babu, M.M., Lee, R.T.J.G. van der, Groot, N.S. de, Gsponer, J.   +3 more
openaire   +2 more sources

Intrinsically Disordered Proteins

2022
Emily M. Grasso, David Eliezer
openaire   +1 more source

Intrinsically disordered proteins

Journal of Molecular Graphics and Modelling, 2000
A.A Keith Dunker, Jeong Oh, Christopher Oldfield, Pedro Romero, Catherine Ratliff, Kerry W. Hipps, Raymond Reeves, Juan Ausio, Charles Kissinger, Robert Bailey, Michael Griswold, Celeste J. Brown, Wah Chiu, Zoran Obradovic   +13 more
openaire   +1 more source

Intrinsically Disordered Proteins

2008
openaire   +2 more sources

Intrinsic Disorder and Protein Function

Biochemistry, 2002
A Keith, Dunker, Celeste J, Brown, J David, Lawson, Lilia M, Iakoucheva, Zoran, Obradović   +4 more
openaire   +2 more sources

Intrinsically Disordered Proteins

2014
openaire   +1 more source