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ABUNDANT DISORDER. "That it is essential to understand the interaction patterns of proteins with large intrinsically disordered segments becomes evident in the light of their abundance in higher eukaryotes (about 30–40% of their proteins contain large disordered segments) and the finding that proteins enriched in disorder are crucial for cellular processes such as transcription and signal transduction." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

PERPETUAL EMERGENCE. "Substantial effort in the genetic programming community is dedicated to exploring avenues for designing solutions to hard problems. In an ideal situation the solution would adapt to unseen new problems in a satisfactory manner. In our view, this can be achieved to a great extent if mechanisms for allowing perpetual emergence and autonomous response to emerging properties, not requiring external intervention, are put in place." http://eprints.aston.ac.uk/20778/1/Emergence_in_genetic_programming.pdf View in LinkedIn

SYNERGY CREATES PLASTICITY. "The notion that disordered regions are largely passive is being actively challenged by the idea that they perform diverse functions, and that synergy between structured and disordered regions expands the functional repertoires of proteins." http://science.sciencemag.org/content/337/6101/1460 View in LinkedIn

TWO ORDERS. "Many protein functions can be attributed to segments (domains) that fold independently and adopt specific three-dimensional structures. Intrinsically disordered regions are unstructured segments whose amino acid compositions prevent autonomous folding. Some eukaryotic proteins are either fully disordered (intrinsically disordered proteins) or structured, but most have both types of regions." https://lnkd.in/dKEH6Bf View in LinkedIn

INTRINSICALLY DISORDERED (ID) REGIONS. "Proteins containing ID regions tend to take a central role in protein interaction networks; specifically, they act as hubs, interacting with multiple different partners across time and space, allowing for the co-ordination of many cellular activities. Especially critical in determining this role is their ability to bind more than one partner using the same region." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

DISEASE ASSOCIATIONS. "Proteins with long intrinsically disordered segments have been associated with several human disease conditions. For instance, overexpression of the intrinsically disordered Stathmin has been linked to cancer, whereas the overexpression of tau, ataxin-1, α-synuclein and huntingtin is associated with various neurodegenerative disorders." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

COSTS. "However, the use of promiscuity does not come without a cost: a number of diseases that have been associated with intrinsically disordered-containing proteins seem to be caused by undesirable interactions occurring upon altered expression of the intrinsically disordered-containing protein." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

FUNCTION OF PROMISCUOUS ID SEGMENTS. "Their use in assembling dynamic, macromolecular structures, their role as interaction switches in regulation and signalling, and their role as recognition elements in the PQC (protein quality control) system." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

INTER- AND INTRADIGM-MODULARITY. "Patil et al., concluded that transient hubs are more likely to interact intermodularly, allowing communication between different modules (a module simply being a highly interconnected process, like the transcription initiation machinery), whereas the stable hubs are more likely to interact intramodularly, allowing for the formation of the modules." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn

HUB GROUPINGS. "Numerous studies have broken the hub proteins into two separate categories: those that form simultaneous stable complexes with their many interaction partners (party/multi-interface/stable hubs), and those that interact transiently with their partners at separate times (date/singlish-interface/transient hubs). Of these two hub types, only the transiently interacting hubs were found to be enriched in disorder." http://www.biochemj.org/content/454/3/361?sa=X&ved=0CDkQ9QEwEWoVChMIzdjAo5n2xgIVovRyCh0HSAum View in LinkedIn