Results 51 to 60 of about 1,786,374 (279)
mBio, 2020 A distinguishing morphological feature of all herpesviruses is the multiprotein tegument layer located between the nucleocapsid and lipid envelope of the virion. Tegument proteins play multiple roles in viral replication, including viral assembly, but we
Claire M. Metrick +2 more
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Proteins of generalist and specialist pathogens differ in their amino acid composition
Life Science Alliance, 2018 Primitive amino acids and disorder content in secreted proteins are distinctively enriched in generalist compared with host-specific pathogens. Pathogens differ in their host specificities, with species infecting a unique host (specialist pathogens) and ...
Luz P Blanco +3 more
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Entropy, 2019 We propose a framework to convert the protein intrinsic disorder content to structural entropy (H) using Shannon’s information theory (IT). The structural capacity (C), which is the sum of H and structural information (I), is equal to the amino acid ...
Hao-Bo Guo +5 more
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Order, Disorder, and Everything in Between
Molecules, 2016 In addition to the “traditional” proteins characterized by the unique crystal-like structures needed for unique functions, it is increasingly recognized that many proteins or protein regions (collectively known as intrinsically disordered proteins (IDPs)
Shelly DeForte, Vladimir N. Uversky
doaj +1 more source
FEBS Letters, EarlyView.Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura +2 more
wiley +1 more source
Exon-phase symmetry and intrinsic structural disorder promote modular evolution in the human genome [PDF]
, 2013 A key signature of module exchange in the genome is phase symmetry of exons, suggestive of exon shuffling events that occurred without disrupting translation reading frame.
Kalmár, Lajos +2 more
core +1 more source
DisProt in 2024: improving function annotation of intrinsically disordered proteins [PDF]
, 2023 International audienceDisProt (URL: https://disprot.org) is the gold standard database for intrinsically disordered proteins and regions, providing valuable information about their functions. The latest version of DisProt brings significant advancements,
Longhi, Sonia +81 more
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Evolutionarily conserved network properties of intrinsically disordered proteins. [PDF]
PLoS ONE, 2015 Intrinsically disordered proteins (IDPs) lack a stable tertiary structure in isolation. Remarkably, however, a substantial portion of IDPs undergo disorder-to-order transitions upon binding to their cognate partners.
Nivedita Rangarajan +2 more
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Diversity and complexity in neural organoids
FEBS Letters, EarlyView.Neural organoid research aims to expand genetic diversity on one side and increase tissue complexity on the other. Chimeroids integrate multiple donor genomes within single organoids. Self‐organising multi‐identity organoids, exogenous cell seeding, or enforced assembly of region‐specific organoids contribute to tissue complexity.
Ilaria Chiaradia, Madeline A. Lancaster
wiley +1 more source
Abundance of intrinsic disorder in SV-IV, a multifunctional androgen-dependent protein secreted from rat seminal vesicle [PDF]
, 2007 The potent immunomodulatory, anti-inflammatory and procoagulant properties of the protein no. 4 secreted from the rat seminal vesicle epithelium (SV-IV) have been previously found to be modulated by a supramolecular monomer-trimer ...
Silvia Vilasi +4 more
core +1 more source