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Full-Text Articles in Medicine and Health Sciences
Editorial: Intrinsically Disordered Proteins And Regions: The Challenge To The Structure-Function Relationship, Angelo Toto, Pietro Sormanni, Cristina Paissoni, Vladimir N. Uversky
Editorial: Intrinsically Disordered Proteins And Regions: The Challenge To The Structure-Function Relationship, Angelo Toto, Pietro Sormanni, Cristina Paissoni, Vladimir N. Uversky
Molecular Medicine Faculty Publications
No abstract provided.
Intrinsic Disorder In Tetratricopeptide Repeat Proteins, Nathan W. Bibber, Cornelia Haerle, Roy Khalifa, Bin Xue, Vladimir N. Uversky
Intrinsic Disorder In Tetratricopeptide Repeat Proteins, Nathan W. Bibber, Cornelia Haerle, Roy Khalifa, Bin Xue, Vladimir N. Uversky
Molecular Medicine Faculty Publications
Among the realm of repeat containing proteins that commonly serve as “scaffolds” promoting protein-protein interactions, there is a family of proteins containing between 2 and 20 tetratricopeptide repeats (TPRs), which are functional motifs consisting of 34 amino acids. The most distinguishing feature of TPR domains is their ability to stack continuously one upon the other, with these stacked repeats being able to affect interaction with binding partners either sequentially or in combination. It is known that many repeat-containing proteins are characterized by high levels of intrinsic disorder, and that many protein tandem repeats can be intrinsically disordered. Furthermore, it seems …
Intrinsic Disorder-Based Emergence In Cellular Biology: Physiological And Pathological Liquid-Liquid Phase Transitions In Cells, April L. Darling, Boris Zaslavsky, Vladimir N. Uversky
Intrinsic Disorder-Based Emergence In Cellular Biology: Physiological And Pathological Liquid-Liquid Phase Transitions In Cells, April L. Darling, Boris Zaslavsky, Vladimir N. Uversky
Molecular Medicine Faculty Publications
The visible outcome of liquid-liquid phase transitions (LLPTs) in cells is the formation and disintegration of various proteinaceous membrane-less organelles (PMLOs). Although LLPTs and related PMLOs have been observed in living cells for over 200 years, the physiological functions of these transitions (also known as liquid-liquid phase separation, LLPS) are just starting to be understood. While unveiling the functionality of these transitions is important, they have come into light more recently due to the association of abnormal LLPTs with various pathological conditions. In fact, several maladies, such as various cancers, different neurodegenerative diseases, and cardiovascular diseases, are known to be …
Expression, Purification, And Characterization Of Interleukin-11 Orthologues, Andrei S. Sokolov, Alexei S. Kazakov, Valery V. Solovyev, Ramis G. Ismailov, Vladimir N. Uversky, Yulia S. Lapteva, Roman V. Mikhailov, Ekaterina V. Pavlova, Iana O. Terletskaya, Ludmila V. Ermolina, Sergei E. Permyakov, Eugene A. Permyakov, Eugene A. Permyakov
Expression, Purification, And Characterization Of Interleukin-11 Orthologues, Andrei S. Sokolov, Alexei S. Kazakov, Valery V. Solovyev, Ramis G. Ismailov, Vladimir N. Uversky, Yulia S. Lapteva, Roman V. Mikhailov, Ekaterina V. Pavlova, Iana O. Terletskaya, Ludmila V. Ermolina, Sergei E. Permyakov, Eugene A. Permyakov, Eugene A. Permyakov
Molecular Medicine Faculty Publications
Interleukin-11 (IL-11) is a multifunctional cytokine implicated in several normal and pathological processes. The decoding of IL-11 function and development of IL-11-targeted drugs dictate the use of laboratory animals and need of the better understanding of species specificity of IL-11 signaling. Here, we present a method for the recombinant interleukin-11 (rIL-11) production from the important model animals, mouse and macaque. The purified mouse and macaque rIL-11 interact with extracellular domain of human IL-11 receptor subunit α and activate STAT3 signaling in HEK293 cells co-expressing human IL-11 receptors with efficacies resembling those of human rIL-11. Hence, the evolutionary divergence does not …
The Alphabet Of Intrinsic Disorder: Ii. Various Roles Of Glutamic Acid In Ordered And Intrinsically Disordered Proteins, Vladimir N. Uversky
The Alphabet Of Intrinsic Disorder: Ii. Various Roles Of Glutamic Acid In Ordered And Intrinsically Disordered Proteins, Vladimir N. Uversky
Molecular Medicine Faculty Publications
The ability of a protein to fold into unique functional state or to stay intrinsically disordered is encoded in its amino acid sequence. Both ordered and intrinsically disordered proteins (IDPs) are natural polypeptides that use the same arsenal of 20 proteinogenic amino acid residues as their major building blocks. The exceptional structural plasticity of IDPs, their capability to exist as heterogeneous structural ensembles and their wide array of important disorder-based biological functions that complements functional repertoire of ordered proteins are all rooted within the peculiar differential usage of these building blocks by ordered proteins and IDPs. In fact, some residues …