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Full-Text Articles in Medicine and Health Sciences
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
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 …
Simple Approach For Ranking Structure Determining Residues, Oscar D. Luna-Martínez, Abraham Vidal-Limón, Miryam I. Villalba-Velázquez, Rosalba Sánchez-Alcalá, Ramón Garduño-Juárez, Vladimir N. Uversky, Baltazar Becerril
Simple Approach For Ranking Structure Determining Residues, Oscar D. Luna-Martínez, Abraham Vidal-Limón, Miryam I. Villalba-Velázquez, Rosalba Sánchez-Alcalá, Ramón Garduño-Juárez, Vladimir N. Uversky, Baltazar Becerril
Molecular Medicine Faculty Publications
Mutating residues has been a common task in order to study structural properties of the protein of interest. Here, we propose and validate a simple method that allows the identification of structural determinants; i.e., residues essential for preservation of the stability of global structure, regardless of the protein topology. This method evaluates all of the residues in a 3D structure of a given globular protein by ranking them according to their connectivity and movement restrictions without topology constraints. Our results matched up with sequence-based predictors that look up for intrinsically disordered segments, suggesting that protein disorder can also be described …
Identifying Similar Patterns Of Structural Flexibility In Proteins By Disorder Prediction And Dynamic Programming, Aidan Petrovich, Adam Borne, Vladimir N. Uversky, Bin Xue
Identifying Similar Patterns Of Structural Flexibility In Proteins By Disorder Prediction And Dynamic Programming, Aidan Petrovich, Adam Borne, Vladimir N. Uversky, Bin Xue
Molecular Medicine Faculty Publications
Computational methods are prevailing in identifying protein intrinsic disorder. The results from predictors are often given as per-residue disorder scores. The scores describe the disorder propensity of amino acids of a protein and can be further represented as a disorder curve. Many proteins share similar patterns in their disorder curves. The similar patterns are often associated with similar functions and evolutionary origins. Therefore, finding and characterizing specific patterns of disorder curves provides a unique and attractive perspective of studying the function of intrinsically disordered proteins. In this study, we developed a new computational tool named IDalign using dynamic programming. This …
Malleable Ribonucleoprotein Machine: Protein Intrinsic Disorder In The Saccharomyces Cerevisiae Spliceosome, Maria De Lourdes Coelho Ribeiro, Julio Espinosa, Sameen Islam, Osvaldo Martinez, Jayesh Jamnadas Thanki, Stephanie Mazariegos, Tam Nguyen, Maya Larina, Bin Xue, Vladimir N. Uversky
Malleable Ribonucleoprotein Machine: Protein Intrinsic Disorder In The Saccharomyces Cerevisiae Spliceosome, Maria De Lourdes Coelho Ribeiro, Julio Espinosa, Sameen Islam, Osvaldo Martinez, Jayesh Jamnadas Thanki, Stephanie Mazariegos, Tam Nguyen, Maya Larina, Bin Xue, Vladimir N. Uversky
Molecular Medicine Faculty Publications
Recent studies revealed that a significant fraction of any given proteome is presented by proteins that do not have unique 3D structures as a whole or in significant parts. These intrinsically disordered proteins possess dramatic structural and functional variability, being especially enriched in signaling and regulatory functions since their lack of fixed structure defines their ability to be involved in interaction with several proteins and allows them to be re-used in multiple pathways. Among recognized disorder-based protein functions are interactions with nucleic acids and multi-target binding; i.e., the functions ascribed to many spliceosomal proteins. Therefore, the spliceosome, a multimegadalton ribonucleoprotein …