Results 11 to 20 of about 156,443 (294)
Protein intrinsic disorder in plants
Frontiers in Plant Science, 2013 To some extent contradicting the classical paradigm of the relationship between protein 3D structure and function, now it is clear that large portions of the proteomes, especially in higher organisms, lack a fixed structure and still perform very ...
Florencio ePazos +3 more
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Intrinsic Disorder in Transcription Factors [PDF]
Biochemistry, 2006 Intrinsic disorder (ID) is highly abundant in eukaryotes, which reflect the greater need for disorder-associated signaling and transcriptional regulation in nucleated cells. Although several well-characterized examples of intrinsically disordered proteins in transcriptional regulation have been reported, no systematic analysis has been reported so far.
Liu, Jiangang +5 more
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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 microtubules.
Guha Roy, Mainak +4 more
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SnapShot: Intrinsic Structural Disorder
Cell, 2015 Many proteins (intrinsically disordered proteins, IDPs) or regions of proteins (intrinsically disordered regions, IDRs) lack a well-defined 3D structure under physiological conditions. Albeit unfolded and highly dynamic, these proteins are not denatured; rather, intrinsic structural disorder is their native, functional state.
Guharoy, M., Pauwels, K., Tompa, Péter
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Troponins, intrinsic disorder, and cardiomyopathy
Biological Chemistry, 2016 AbstractCardiac troponin is a dynamic complex of troponin C, troponin I, and troponin T (TnC, TnI, and TnT, respectively) found in the myocyte thin filament where it plays an essential role in cardiac muscle contraction. Mutations in troponin subunits are found in inherited cardiomyopathies, such as hypertrophic cardiomyopathy (HCM) and dilated ...
Insung Na +4 more
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Intrinsic disorder in putative protein sequences [PDF]
Proteome Science, 2011 Intrinsically disordered proteins (IDPs) and regions (IDRs) perform a variety of crucial biological functions despite lacking stable tertiary structure under physiological conditions in vitro. State-of-the-art sequence-based predictors of intrinsic disorder are achieving per-residue accuracies over 80%.
Uros Midic, Zoran Obradovic
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Intrinsic disorder of the extracellular matrix
Molecular BioSystems, 2011 Abstract The extracellular matrix is very well organized at the supramolecular and tissue levels and little is known on the potential role of intrinsic disorder in promoting its organization. We predicted the amount of disorder and identified disordered regions in the human extracellular proteome with established computational tools ...
Peysselon, Franck +3 more
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Intrinsic Disorder in the Human Spliceosomal Proteome
PLoS Computational Biology, 2012 The spliceosome is a molecular machine that performs the excision of introns from eukaryotic pre-mRNAs. This macromolecular complex comprises in human cells five RNAs and over one hundred proteins. In recent years, many spliceosomal proteins have been found to exhibit intrinsic disorder, that is to lack stable native three-dimensional structure in ...
Korneta, Iga, Bujnicki, Janusz M.
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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. +4 more
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