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Full-Text Articles in Medicine and Health Sciences
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 …
The Pathophysiological Significance Of Fibulin-3, Imogen Livingstone, Vladimir N. Uversky, Dominic Furniss, Akira Wiberg
The Pathophysiological Significance Of Fibulin-3, Imogen Livingstone, Vladimir N. Uversky, Dominic Furniss, Akira Wiberg
Molecular Medicine Faculty Publications
Fibulin-3 (also known as EGF-containing fibulin extracellular matrix protein 1 (EFEMP1)) is a secreted extracellular matrix glycoprotein, encoded by the EFEMP1 gene that belongs to the eight-membered fibulin protein family. It has emerged as a functionally unique member of this family, with a diverse array of pathophysiological associations predominantly centered on its role as a modulator of extracellular matrix (ECM) biology. Fibulin-3 is widely expressed in the human body, especially in elastic-fibre-rich tissues and ocular structures, and interacts with enzymatic ECM regulators, including tissue inhibitor of metalloproteinase-3 (TIMP-3). A point mutation in EFEMP1 causes an inherited early-onset form of macular …
Zooming Into The Dark Side Of Human Annexin-S100 Complexes: Dynamic Alliance Of Flexible Partners, Judith Weisz, Vladimir N. Uversky
Zooming Into The Dark Side Of Human Annexin-S100 Complexes: Dynamic Alliance Of Flexible Partners, Judith Weisz, Vladimir N. Uversky
Molecular Medicine Faculty Publications
Annexins and S100 proteins form two large families of Ca2+-binding proteins. They are quite different both structurally and functionally, with S100 proteins being small (10–12 kDa) acidic regulatory proteins from the EF-hand superfamily of Ca2+-binding proteins, and with annexins being at least three-fold larger (329 ± 12 versus 98 ± 7 residues) and using non-EF-hand-based mechanism for calcium binding. Members of both families have multiple biological roles, being able to bind to a large cohort of partners and possessing a multitude of functions. Furthermore, annexins and S100 proteins can interact with each other in either a Ca2+-dependent or Ca2+-independent manner, …