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Protein intrinsic disorder and network connectivity. The case of 14-3-3 proteins
(Frontiers, 2014-02)
The understanding of networks is a common goal of an unprecedented array of traditional disciplines. One of the protein network properties most influenced by the structural contents of its nodes is the inter-connectivity. ...
Chasing coevolutionary signals in intrinsically disordered proteins complexes
(Nature, 2020-10)
Intrinsically disordered proteins/regions (IDPs/IDRs) are crucial components of the cell, they are highly abundant and participate ubiquitously in a wide range of biological functions, such as regulatory processes and cell ...
Intrinsic disorder is a key characteristic in partners that bind 14-3-3 proteins
(Wiley-liss, Div John Wiley & Sons Inc, 2006-04)
Proteins named 14-3-3 can bind more than 200 different proteins, mostly (but not exclusively) when they are at a phosphorylated state. These partner proteins are involved in different cellular processes, such as cell ...
Hidden Structural Codes in Protein Intrinsic Disorder
(American Chemical Society, 2017-10)
Intrinsic disorder is a major structural category in biology, accounting for more than 30% of coding regions across the domains of life, yet consists of conformational ensembles in equilibrium, a major challenge in protein ...
MobiDB 3.0: More annotations for intrinsic disorder, conformational diversity and interactions in proteins
(Oxford University Press, 2018-01)
The MobiDB (URL: mobidb.bio.unipd.it) database of protein disorder and mobility annotations has been significantly updated and upgraded since its last major renewal in 2014. Several curated datasets for intrinsic disorder ...
Intrinsic Disorder in the human papillomavirus E7 protein
(John Wiley & Sons Inc, 2012)
Papillomaviruses (PVs) are a group of small, nonenveloped, double-stranded DNA viruses, which infect the skin and mucous epithelia of reptiles, birds, and mammals, and have recently been classified as a separate virus ...
Protein conformational dynamics and phenotypic switching
(2021-01-01)
Intrinsically disordered proteins (IDPs) are proteins that lack rigid 3D structure but exist as conformational ensembles. Because of their structural plasticity, they can interact with multiple partners. The protein ...
Intrinsic disorder associated with 14-3-3 proteins and their partners
(Elsevier, 2019-01)
Protein-protein interactions (PPIs) mediate a variety of cellular processes and form complex networks, where connectivity is achieved owing to the “hub” proteins whose interaction with multiple protein partners is facilitated ...
Phosphorylation regulates the bound structure of an intrinsically disordered protein: The p53-TAZ2 case
(Public Library of Science, 2016-01-07)
Disordered regions and Intrinsically Disordered Proteins (IDPs) are involved in critical cellular processes and may acquire a stable three-dimensional structure only upon binding to their partners. IDPs may follow a ...
Intrinsic Disorder to Order Transitions in the Scaffold Phosphoprotein P from the Respiratory Syncytial Virus RNA Polymerase Complex
(American Chemical Society, 2016-03)
Intrinsic disorder is at the center of biochemical regulation and is particularly overrepresented among the often multifunctional viral proteins. Replication and transcription of the respiratory syncytial virus (RSV) relies ...