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Phosphorylation in protein-protein binding: effect on stability and function.
Posttranslational modifications offer a dynamic way to regulate protein activity, subcellular localization, and stability. Here we estimate the effect of phosphorylation on protein binding andExpand
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Cancer Missense Mutations Alter Binding Properties of Proteins and Their Interaction Networks
Many studies have shown that missense mutations might play an important role in carcinogenesis. However, the extent to which cancer mutations might affect biomolecular interactions remains unclear.Expand
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Molecular mechanisms of disease-causing missense mutations.
Genetic variations resulting in a change of amino acid sequence can have a dramatic effect on stability, hydrogen bond network, conformational dynamics, activity and many other physiologicallyExpand
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Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization.
Many soluble and membrane proteins form homooligomeric complexes in a cell which are responsible for the diversity and specificity of many pathways, may mediate and regulate gene expression, activityExpand
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Physicochemical mechanisms of protein regulation by phosphorylation
Phosphorylation offers a dynamic way to regulate protein activity and subcellular localization, which is achieved through its reversibility and fast kinetics. Adding or removing a dianionic phosphateExpand
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Regulation of protein-protein binding by coupling between phosphorylation and intrinsic disorder: analysis of human protein complexes.
Phosphorylation offers a dynamic way to regulate protein activity, subcellular localization, and stability. The majority of signaling pathways involve an extensive set of protein-proteinExpand
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Evolutionary, physicochemical, and functional mechanisms of protein homooligomerization.
Protein homooligomers afford several important benefits for the cell; they mediate and regulate gene expression, activity of many enzymes, ion channels, receptors, and cell-cell adhesion processes.Expand
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Crosstalk between signaling pathways provided by single and multiple protein phosphorylation sites.
Cellular fate depends on the spatiotemporal separation and integration of signaling processes that can be provided by phosphorylation events. In this study, we identify the crucial points inExpand
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Identification of the sequence determinants of protein N-terminal acetylation through a decision tree approach
N-terminal acetylation is one of the most common protein modifications in eukaryotes and occurs co-translationally when the N-terminus of the nascent polypeptide is still attached to the ribosome. Expand
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Dynamic recognition and linkage specificity in K63 di-ubiquitin and TAB2 NZF domain complex
Poly-ubiquitin (poly-Ub) is involved in various cellular processes through the linkage-specific recognition of Ub-binding domains (UBD). In this study, using molecular dynamics (MD) simulationExpand
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