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Now showing items 11-20 of 3127
Controllability of protein-protein interaction phosphorylation-based networks: Participation of the hub 14-3-3 protein family
(Nature Publishing Group, 2016-05)
Posttranslational regulation of protein function is an ubiquitous mechanism in eukaryotic cells. Here, we analyzed biological properties of nodes and edges of a human protein-protein interaction phosphorylation-based ...
Collective variable driven molecular dynamics to improve protein protein docking scoring
(Elsevier, 2013-12-28)
In biophysics, the structural prediction of protein–protein complexes starting from the unbound form of the two interacting monomers is a major difficulty. Although current computational docking protocols are able to ...
H-bond refinement for electron transfer membrane-bound protein-protein complexes: cytochrome c oxidase and cytochrome c552
(Elsevier, 2013-06)
In this study we propose a protocol to evaluate membrane-bound cytochrome c oxidase–cytochrome c552 docking candidates. An initial rigid docking algorithm generates docking poses of the cytochrome c oxidase–cytochrome c552, ...
The Protein Interactome Of Collapsin Response Mediator Protein-2 (crmp2/dpysl2) Reveals Novel Partner Proteins In Brain Tissue
(WILEY-V C H VERLAG GMBHWEINHEIM, 2015)
Evidence for the interaction of the regulatory protein Ki-1/57 with p53 and its interacting proteins
(Academic Press Inc Elsevier ScienceSan DiegoEUA, 2006)
Integrative meta-analysis identifies microRNA-regulated networks in infantile hemangioma
(2016-01-15)
Background: Hemangioma is a common benign tumor in the childhood; however our knowledge about the molecular mechanisms of hemangioma development and progression are still limited. Currently, microRNAs (miRNAs) have been ...
The fragility of protein-protein interaction networks
(2011)
The capacity to resist perturbations from the environment is crucial to the survival of all organisms. We quantitatively analyze the susceptibility of protein interaction networks of numerous organisms to random and targeted ...