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University of South Florida

Molecular Medicine Faculty Publications

2017

Intrinsically disordered proteins

Articles 1 - 3 of 3

Full-Text Articles in Medicine and Health Sciences

Electronegativity And Intrinsic Disorder Of Preeclampsia-Related Proteins, Carlos Polanco, Jorge Alberto Castañón-González, Vladimir N. Uversky, Thomas Buhse, José Lino Mendoza, Juan J. Calva Jan 2017

Electronegativity And Intrinsic Disorder Of Preeclampsia-Related Proteins, Carlos Polanco, Jorge Alberto Castañón-González, Vladimir N. Uversky, Thomas Buhse, José Lino Mendoza, Juan J. Calva

Molecular Medicine Faculty Publications

Preeclampsia, hemorrhage, and infection are the leading causes of maternal death in underdeveloped countries. Since several proteins associated with preeclampsia are known, we conducted a computational study in which evaluated the commonness and potential functionality of intrinsic disorder in these proteins and also made an attempt to characterize their origin. To this end, we used a several supervised techniques, as a Polarity Index Method (PIM), which evaluates the electronegativity of proteins from their sequence alone. Peculiarities of resulting polar profile of the group of preeclampsia-related proteins were then compared with profiles of a group of lipoproteins, antimicrobial peptides, angiogenesis-related proteins, …


Calreticulin: Challenges Posed By The Intrinsically Disordered Nature Of Calreticulin To The Study Of Its Function, Lilian Varricchio, Mario Falchi, Massimiliano Dall'ora, Benedittis, Caterina De Benedittis, Alessandra Ruggeri, Vladimir N. Uversky, Anna Rita Migliaccio Jan 2017

Calreticulin: Challenges Posed By The Intrinsically Disordered Nature Of Calreticulin To The Study Of Its Function, Lilian Varricchio, Mario Falchi, Massimiliano Dall'ora, Benedittis, Caterina De Benedittis, Alessandra Ruggeri, Vladimir N. Uversky, Anna Rita Migliaccio

Molecular Medicine Faculty Publications

Calreticulin is a Ca2+-binding chaperone protein, which resides mainly in the endoplasmic reticulum but also found in other cellular compartments including the plasma membrane. In addition to Ca2+, calreticulin binds and regulates almost all proteins and most of the mRNAs deciding their intracellular fate. The potential functions of calreticulin are so numerous that identification of all of them is becoming a nightmare. Still the recent discovery that patients affected by the Philadelphia-negative myeloproliferative disorders essential thrombocytemia or primary myelofibrosis not harboring JAK2 mutations carry instead calreticulin mutations disrupting its C-terminal domain has highlighted the clinical need …


Functional Analysis Of Human Hub Proteins And Their Interactors Involved In The Intrinsic Disorder-Enriched Interactions, Gang Hu, Zhonghua Wu, Vladimir N. Uversky, Lukasz Kurgan Jan 2017

Functional Analysis Of Human Hub Proteins And Their Interactors Involved In The Intrinsic Disorder-Enriched Interactions, Gang Hu, Zhonghua Wu, Vladimir N. Uversky, Lukasz Kurgan

Molecular Medicine Faculty Publications

Some of the intrinsically disordered proteins and protein regions are promiscuous interactors that are involved in one-to-many and many-to-one binding. Several studies have analyzed enrichment of intrinsic disorder among the promiscuous hub proteins. We extended these works by providing a detailed functional characterization of the disorder-enriched hub protein-protein interactions (PPIs), including both hubs and their interactors, and by analyzing their enrichment among disease-associated proteins. We focused on the human interactome, given its high degree of completeness and relevance to the analysis of the disease-linked proteins. We quantified and investigated numerous functional and structural characteristics of the disorder-enriched hub PPIs, including …