Results 11 to 20 of about 29,414 (258)

Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.

PLoS ONE, 2014
An amyloidogenic region (AR) in a protein sequence plays a significant role in protein aggregation and amyloid formation. We have investigated the sequence complexity of AR that is present in intrinsically disordered human proteins.
Swagata Das, Uttam Pal, Supriya Das, Khyati Bagga, Anupam Roy, Arpita Mrigwani, Nakul C Maiti   +6 more
doaj   +3 more sources

Intrinsically disordered proteins and proteins with intrinsically disordered regions in neurodegenerative diseases

Biophysical Reviews, 2022
Many different intrinsically disordered proteins and proteins with intrinsically disordered regions are associated with neurodegenerative diseases. These types of proteins including amyloid-β, tau, α-synuclein, CHCHD2, CHCHD10, and G-protein coupled receptors are increasingly becoming evaluated as potential drug targets in the pharmaceutical-based ...
Orkid Coskuner-Weber, Ozan Mirzanli, Vladimir N. Uversky   +2 more
openaire   +4 more sources

Intrinsically disordered regions in autophagy proteins [PDF]

Proteins: Structure, Function, and Bioinformatics, 2013
ABSTRACTAutophagy is an essential eukaryotic pathway required for cellular homeostasis. Numerous key autophagy effectors and regulators have been identified, but the mechanism by which they carry out their function in autophagy is not fully understood.
Yang, Mei, Minfei, Su, Gaurav, Soni, Saeed, Salem, Christopher L, Colbert, Sangita C, Sinha   +5 more
openaire   +2 more sources

Phosphorylation of Intrinsically Disordered Regions in Remorin Proteins [PDF]

Frontiers in Plant Science, 2012
Plant-specific remorin proteins reside in subdomains of plasma membranes, originally termed membrane rafts. They probably facilitate cellular signal transduction by direct interaction with signaling proteins such as receptor-like kinases and may dynamically modulate their lateral segregation within plasma membranes.
Marín, Macarena, Ott, Thomas
openaire   +5 more sources

Classification of Intrinsically Disordered Regions and Proteins

Chemical Reviews, 2014
1.1. Uncharacterized Protein Segments Are a Source of Functional Novelty Over the past decade, we have observed a massive increase in the amount of information describing protein sequences from a variety of organisms.1,2 While this may reflect the diversity in sequence space, and possibly also in function space,3 a large proportion of the sequences ...
Van Der Lee R., Buljan M., Lang B., Weatheritt R. J., Daughdrill G. W., Dunker A. K., Fuxreiter M., Gough J., Gsponer J., Jones D. T., Kim P. M., Kriwacki R. W., Oldfield C. J., Pappu R. V., Tompa P., Uversky V. N., Wright P. E., Babu M. M.   +17 more
openaire   +5 more sources

Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions

Biomolecules, 2022
Intrinsically disordered regions (IDRs) carry out many cellular functions and vary in length and placement in protein sequences. This diversity leads to variations in the underlying compositional biases, which were demonstrated for the short vs. long IDRs. We analyze compositional biases across four classes of disorder: fully disordered proteins; short
Bi Zhao, Lukasz Kurgan
openaire   +3 more sources

The SARS-CoV-2 nucleocapsid phosphoprotein forms mutually exclusive condensates with RNA and the membrane-associated M protein

Nature Communications, 2021
The SARS-CoV-2 nucleocapsid (N) protein binds the viral RNA genome and contains two ordered domains flanked by three intrinsically-disordered regions. Here, the authors show that RNA binding induces liquid-liquid phase separation of N, which is driven by
Shan Lu, Qiaozhen Ye, Digvijay Singh, Yong Cao, Jolene K. Diedrich, John R. Yates, Elizabeth Villa, Don W. Cleveland, Kevin D. Corbett   +8 more
doaj   +1 more source

Adenosine triphosphate as a modulator of protein interactions and stability. [PDF]

FEBS Open Bio
ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Tan S, Curtis R.
europepmc   +2 more sources

Protein kinases phosphorylate long disordered regions in intrinsically disordered proteins [PDF]

Protein Science, 2019
AbstractPhosphorylation is a major post‐translational modification that plays a central role in signaling pathways. Protein kinases phosphorylate substrates (phosphoproteins) by adding phosphate at Ser/Thr or Tyr residues (phosphosites). A large amount of data identifying and describing phosphosites in phosphoproteins has been reported but the ...
Ryotaro Koike, Mutsuki Amano, Kozo Kaibuchi, Motonori Ota   +3 more
openaire   +2 more sources

Entropy and Information within Intrinsically Disordered Protein Regions [PDF]

Entropy, 2019
Bioinformatics and biophysical studies of intrinsically disordered proteins and regions (IDRs) note the high entropy at individual sequence positions and in conformations sampled in solution. This prevents application of the canonical sequence-structure-function paradigm to IDRs and motivates the development of new methods to extract information from ...
Iva Pritisanac, Robert M. Vernon, Alan M. Moses, Julie D. Forman-Kay   +3 more
openaire   +5 more sources