Results 241 to 250 of about 1,786,374 (279)

Sizes, conformational fluctuations, and SAXS profiles for intrinsically disordered proteins. [PDF]

Protein Sci
Mugnai ML, Chakraborty D, Nguyen HT, Maksudov F, Kumar A, Zeno W, Stachowiak JC, Straub JE, Thirumalai D.   +8 more
europepmc   +1 more source

Correction to 'DisProt in 2024: improving function annotation of intrinsically disordered proteins'. [PDF]

Nucleic Acids Res
europepmc   +1 more source

Intrinsically disordered proteins and proteins with intrinsically disordered regions in neurodegenerative diseases [PDF]

Biophysical Reviews, 2022
Many different intrinsically disordered proteins and proteins with intrinsically disordered regions are associated with neurodegenerative diseases. These types of proteins including amyloid-β, tau, α-synuclein, CHCHD2, CHCHD10, and G-protein coupled ...
Orkid Coskuner Weber, Vladimir Uversky
exaly   +6 more sources

Intrinsically Disordered Proteins: An Overview

International Journal of Molecular Sciences, 2022
Many proteins and protein segments cannot attain a single stable three-dimensional structure under physiological conditions; instead, they adopt multiple interconverting conformational states.
Hampapathalu Adimurthy Nagarajaram, Rakesh Trivedi   +1 more
exaly   +4 more sources

Intrinsically disordered proteins and biomineralization [PDF]

Matrix Biology, 2016
In vertebrates and invertebrates, biomineralization is controlled by the cell and the proteins they produce. A large number of these proteins are intrinsically disordered, gaining some secondary structure when they interact with their binding partners.
Adele Boskey, Eduardo Villarreal-Ramírez   +1 more
exaly   +3 more sources

Classification of Intrinsically Disordered Regions and Proteins

Chemical Reviews, 2014
1.1. Uncharacterized Protein Segments Are a Source of Functional Novelty Over the past decade, we have observed a massive increase in the amount of information describing protein sequences from a variety of organisms.1,2 While this may reflect the diversity in sequence space, and possibly also in function space,3 a large proportion of the sequences ...
Benjamin Lang, Robin van der Lee, Peter Tompa   +2 more
exaly   +4 more sources

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Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions

Annual Review of Biochemistry, 2014
Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and structural instability are encoded by their amino acid sequences. They recognize proteins, nucleic acids, and other types of partners; they accelerate interactions and chemical reactions between
Christopher J, Oldfield, A Keith, Dunker
openaire   +2 more sources

Intrinsically disordered protein

Journal of Molecular Graphics and Modelling, 2001
Proteins can exist in a trinity of structures: the ordered state, the molten globule, and the random coil. The five following examples suggest that native protein structure can correspond to any of the three states (not just the ordered state) and that protein function can arise from any of the three states and their transitions.
A K, Dunker, J D, Lawson, C J, Brown, R M, Williams, P, Romero, J S, Oh, C J, Oldfield, A M, Campen, C M, Ratliff, K W, Hipps, J, Ausio, M S, Nissen, R, Reeves, C, Kang, C R, Kissinger, R W, Bailey, M D, Griswold, W, Chiu, E C, Garner, Z, Obradovic   +19 more
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Intrinsic disorder in S100 proteins

Molecular BioSystems, 2011
Abstract 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 ...
Sergei E, Permyakov, Ramis G, Ismailov, Bin, Xue, Alexander I, Denesyuk, Vladimir N, Uversky, Eugene A, Permyakov   +5 more
openaire   +3 more sources

Intrinsically Disordered Proteins: An Update

2007 IEEE 7th International Symposium on BioInformatics and BioEngineering, 2007
Just over 10 years ago, in June, 1997, in the Proceedings of the IEEE International Conference on Neural Networks, we published our first predictor of intrinsically disordered protein. Since then, we have substantially improved our predictors, and more than 20 other laboratory groups have joined in efforts to improve the prediction of protein disorder.
A. Keith Dunker, Christopher J. Oldfield, Jingwei Meng, Pedro Romero, Jack Y. Yang, Zoran Obradovic, Vladimir N. Uversky   +6 more
openaire   +1 more source