Conditionally and Transiently Disordered Proteins: Awakening Cryptic Disorder To Regulate Protein Function

By Ursula Jakob, Richard W. Kriwacki, Vladimir N Uversky. 2014

185 citations recorded by the source corpus.

Cryptic Disorder To Regulate Protein Function Ursula Jakob,† Richard Kriwacki,‡,§ and Vladimir N. Uversky* †Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109-1048, United States ‡Department of Structural Biology, St. Jude Children’s Research Hospital, Memphis, Tennessee 38105, United States Department of Microbiology, Immunology and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163, United States Department of Molecular Medicine, University of South Florida, Tampa, Florida 33612, United States Institute for Biological Instrumentation, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia

Subfields: Cell Biology, Physiology

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. Zsuzsanna Dosztányi
2. Bálint Mészáros
3. Vladimir N Uversky
4. Gábor Erdös
5. A. Keith Dunker
6. Peter Tompa

In Physiology

1. Zsuzsanna Dosztányi
2. Vladimir N Uversky

Citations in the corpus

• IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018, background): “The activities of IDPs can directly emerge from their flexible nature, exhibiting entropic chain functions or serving as linkers between ordered domains.”
• DisProt 7.0: a major update of the database of disordered proteins (2016, neutral): “…functional examples of ‘conditional disor-der’, i.e. instances where a disordered region functions by transitions to or from a folded state (30), or when disorder is only observed in a fraction of similar structures (31), lead to ambiguity and clearly points to the need for carrying out…”
• Intrinsic disorder here, there, and everywhere, and nowhere to escape from it (2017, background): “However, some IDPs/ IDPRs maintain their functional disorder under conditions of macromolecular crowding and even in living cells, indicating that the physiological state of many proteins relies on the absence of ordered structure [15–19], that some functions simply cannot be done by ordered protein”
• Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics (2019, background): “This regulated unfolding [158] or conditional disorder has an induced nature [159] and transient character [160], and may be initiated by several environmental factors, ranging from changes in temperature, pH, mechanical force, redox potential, or light exposure, to specific interactions with ligand”
• Analyzing Protein Disorder with IUPred2A (2020, background): “It is increasingly recognized that in addition to binding, disorder-to-order or order-to-disorder transitions can also be induced by post-translational modifications (PTMs) and various environmental conditions such as pH or change in redox potential (Jakob, Kriwacki, & Uversky, 2014).”
• Prediction of protein disorder based on IUPred (2018, background): “iological conditions such as pH, reducing agents or post-translational modifications.(77) Methods that”