Results 1 to 10 of about 30,328 (116)

An intrinsically disordered region mediates RNA-binding selectivity and cellular activities of LARP6 [PDF]

Nature Communications
Intrinsically disordered regions (IDRs) are prevalent in RNA-binding proteins (RBPs), yet their roles in RNA interactions remain poorly defined. We examined RNA-binding regulation by structured and disordered regions of LARP6, an RBP with a diverse RNA ...
Federica Capraro, Giancarlo Abis, Alessio Incocciati, Peter J. Simpson, Mehran Karimzadeh, Laura Masino, Alexander Barley, Tam T. T. Bui, Geoff Kelly, Hani Goodarzi, Maria R. Conte, Faraz K. Mardakheh   +11 more
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Liquid-liquid phase separation and its regulation of the BACH2 intrinsically disordered region [PDF]

Biophysics and Physicobiology
Intrinsically disordered regions (IDRs) are vital for several cellular processes. They play a significant role in liquid-liquid phase separation (LLPS). LLPS enhances reaction efficiency by locally concentrating proteins and nucleic acids.
Hironori Hayashi, Miyuki Kato-Murayama, Takeshi Kurasawa, Eiichi N. Kodama, Mikako Shirouzu, Kazuhiko Igarashi, Kazutaka Murayama   +6 more
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Cross-species rescue reveals sequence requirements for a rapidly evolving intrinsically disordered region. [PDF]

PLoS Biology
Many proteins contain intrinsically disordered regions (IDRs) that are essential for their function but do not adopt a stable structure; instead, they exist as an ensemble of conformations.
Sang On Park, Rishad Khondker, Ariel Blank, Annie Dyatel, Corey Frazer, Richard J Bennett, Robert J D Reid, Rodney Rothstein, Luke E Berchowitz   +8 more
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A Dimerization Function in the Intrinsically Disordered N-Terminal Region of Src

Cell Reports, 2018
Summary: The mode of regulation of Src kinases has been elucidated by crystallographic studies identifying conserved structured protein modules involved in an orderly set of intramolecular associations and ligand interactions.
Danislav S. Spassov, Ana Ruiz-Saenz, Amit Piple, Mark M. Moasser   +3 more
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Testing the length limit of loop grafting in a helical repeat protein

Current Research in Structural Biology, 2021
Alpha-helical repeat proteins such as consensus-designed tetratricopeptide repeats (CTPRs) are exceptionally stable molecules that are able to tolerate destabilizing sequence alterations and are therefore becoming increasingly valued as a modular ...
Juliane F. Ripka, Albert Perez-Riba, Piyush K. Chaturbedy, Laura S. Itzhaki   +3 more
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Looking at the Pathogenesis of the Rabies Lyssavirus Strain Pasteur Vaccins through a Prism of the Disorder-Based Bioinformatics

Biomolecules, 2022
Rabies is a neurological disease that causes between 40,000 and 70,000 deaths every year. Once a rabies patient has become symptomatic, there is no effective treatment for the illness, and in unvaccinated individuals, the case-fatality rate of rabies is ...
Surya Dhulipala, Vladimir N. Uversky
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Adenoviral E1A Exploits Flexibility and Disorder to Target Cellular Proteins

Biomolecules, 2020
Direct interaction between intrinsically disordered proteins (IDPs) is often difficult to characterize hampering the elucidation of their binding mechanism.
Maria Grazia Murrali, Isabella C. Felli, Roberta Pierattelli   +2 more
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Theater in the Self-Cleaning Cell: Intrinsically Disordered Proteins or Protein Regions Acting with Membranes in Autophagy

Membranes, 2022
Intrinsically disordered proteins and protein regions (IDPs/IDPRs) are mainly involved in signaling pathways, where fast regulation, temporal interactions, promiscuous interactions, and assemblies of structurally diverse components including membranes ...
Hana Popelka, Vladimir N. Uversky
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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
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Intrinsic Disorder as a Natural Preservative: High Levels of Intrinsic Disorder in Proteins Found in the 2600-Year-Old Human Brain

Biology, 2022
Proteomic analysis revealed the preservation of many proteins in the Heslington brain (which is at least 2600-year-old brain tissue uncovered within the skull excavated in 2008 from a pit in Heslington, Yorkshire, England).
Aaron S. Mohammed, Vladimir N. Uversky
doaj   +1 more source