Results 11 to 20 of about 3,587,930 (291)

Intrinsic structural disorder in cytoskeletal proteins. [PDF]

Cytoskeleton, 2013
Cytoskeleton, the internal scaffold of the cell, displays an exceptional combination of stability and dynamics. It is composed of three major filamentous networks, microfilaments (actin filaments), intermediate filaments (neurofilaments), and ...
Szabó, Beáta, Guharoy, Majnak, Martos, Sara Contreras, Tompa, Péter   +3 more
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Structural and functional studies of intrinsically disordered fibronectin-binding proteins [PDF]

, 2009
Bacterial fibronectin-binding proteins (FnBPs) mediate adhesion of bacteria to host tissues through binding to the human protein fibronectin (Fn). FnBPs are predicted to contain a series of intrinsically disordered Fn-binding repeats (FnBRs), which ...
Norris, Nicole Catherine
core   +6 more sources

Databases for intrinsically disordered proteins [PDF]

Acta Crystallographica Section D Structural Biology, 2022
Intrinsically disordered regions (IDRs) lacking a fixed three-dimensional protein structure are widespread and play a central role in cell regulation. Only a small fraction of IDRs have been functionally characterized, with heterogeneous experimental evidence that is largely buried in the literature.
Piovesan, Damiano, Monzon, Alexander Miguel, Quaglia, Federica, Tosatto, Silvio C. E.   +3 more
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Intrinsically disordered proteins and proteins with intrinsically disordered regions in neurodegenerative diseases

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 receptors are increasingly becoming evaluated as potential drug targets in the pharmaceutical-based ...
Orkid Coskuner-Weber, Ozan Mirzanli, Vladimir N. Uversky   +2 more
openaire   +4 more sources

Introducing Protein Intrinsic Disorder [PDF]

Chemical Reviews, 2014
Central to this model is the notion that the correct shape of the substrate can fit into the active site of the enzyme for enabling an efficient and specific catalysis, as observed for enzymes that hydrolyze β-but not α-glycosidic bonds. 1 Throughout the 20 th century, tens of thousands of structures have been solved and deposited in the Protein Data ...
Habchi, Johnny, Tompa, Peter, Longhi, Sonia, Uversky, Vladimir   +3 more
openaire   +4 more sources

Protein flexibility and intrinsic disorder [PDF]

Protein Science, 2004
AbstractComparisons were made among four categories of protein flexibility: (1) low‐B‐factor ordered regions, (2) high‐B‐factor ordered regions, (3) short disordered regions, and (4) long disordered regions. Amino acid compositions of the four categories were found to be significantly different from each other, with high‐B‐factor ordered and short ...
Radivojac, P., Obradovic, Z., Smith, DK, Zhu, G., Vucetic, S., Brown, CJ, Lawson, JD, Dunker, AK   +7 more
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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 L, Boskey, Eduardo, Villarreal-Ramirez   +1 more
openaire   +2 more sources

MobiDB: intrinsically disordered proteins in 2021 [PDF]

Nucleic Acids Research, 2020
AbstractThe MobiDB database (URL: https://mobidb.org/) provides predictions and annotations for intrinsically disordered proteins. Here, we report recent developments implemented in MobiDB version 4, regarding the database format, with novel types of annotations and an improved update process.
Damiano Piovesan, Marco Necci, Nahuel Escobedo, Alexander Miguel Monzon, András Hatos, Ivan Micetic, Federica Quaglia, Lisanna Paladin, Pathmanaban Ramasamy, Zsuzsanna Dosztányi, Wim F. Vranken, Norman E. Davey, Gustavo D. Parisi, Mónika Fuxreiter, Silvio C. E. Tosatto   +14 more
openaire   +9 more sources

Influence of sequence changes and environment on intrinsically disordered proteins. [PDF]

PLoS Computational Biology, 2009
Many large-scale studies on intrinsically disordered proteins are implicitly based on the structural models deposited in the Protein Data Bank. Yet, the static nature of deposited models supplies little insight into variation of protein structure and ...
Amrita Mohan, Vladimir N Uversky, Predrag Radivojac   +2 more
doaj   +1 more source

Folding factors and partners for the intrinsically disordered protein Micro-Exon Gene 14 (MEG-14) [PDF]

, 2013
The micro-exon genes (MEG) of Schistosoma mansoni, a parasite responsible for the second most widely spread tropical disease, code for small secreted proteins with sequences unique to the Schistosoma genera.
Orcia, Debora, Araujo, A.P.U., Wallace, Bonnie A., Araújo, Ana Paula Ulian de, De Marco, Ricardo, Araujo, Ana Paula U., Debora Orcia, Wallace, B. A., Lopes, Jose Luiz S., DeMarco, Ricardo, Lopes, J.L.S., Ricardo DeMarco, Ana Paula U. Araujo, Orcia, D., B.A. Wallace, Wallace, B.A., Jose Luiz S. Lopes, DeMarco, R.   +17 more
core   +1 more source