Protein-protein interaction sites are hot spots for disease-associated nonsynonymous SNPs.
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How do oncoprotein mutations rewire protein-protein interaction networks?Cancer missense mutations alter binding properties of proteins and their interaction networksCharacterizing changes in the rate of protein-protein dissociation upon interface mutation using hotspot energy and organizationDeriving a mutation index of carcinogenicity using protein structure and protein interfacesTowards structural systems pharmacology to study complex diseases and personalized medicineThe structural pathway of interleukin 1 (IL-1) initiated signaling reveals mechanisms of oncogenic mutations and SNPs in inflammation and cancerCombining structural modeling with ensemble machine learning to accurately predict protein fold stability and binding affinity effects upon mutationHOMCOS: an updated server to search and model complex 3D structuresMutation-Structure-Function Relationship Based Integrated Strategy Reveals the Potential Impact of Deleterious Missense Mutations in Autophagy Related Proteins on Hepatocellular Carcinoma (HCC): A Comprehensive Informatics ApproachProtein modeling: what happened to the "protein structure gap"?An association-adjusted consensus deleterious scheme to classify homozygous Mis-sense mutations for personal genome interpretationSDS, a structural disruption score for assessment of missense variant deleteriousness.Mechismo: predicting the mechanistic impact of mutations and modifications on molecular interactions.Conformational dynamics of nonsynonymous variants at protein interfaces reveals disease association.Identifying mutation specific cancer pathways using a structurally resolved protein interaction network.Large scale analysis of protein stability in OMIM disease related human protein variantsThree-Dimensional Model of Human Nicotinamide Nucleotide Transhydrogenase (NNT) and Sequence-Structure Analysis of its Disease-Causing Variations.Structural dynamics flexibility informs function and evolution at a proteome scale.Determining effects of non-synonymous SNPs on protein-protein interactions using supervised and semi-supervised learning.In-frame seven amino-acid duplication in AIP arose over the last 3000 years, disrupts protein interaction and stability and is associated with gigantismSuSPect: enhanced prediction of single amino acid variant (SAV) phenotype using network featuresIntegrating structure to protein-protein interaction networks that drive metastasis to brain and lung in breast cancer.Detection and analysis of disease-associated single nucleotide polymorphism influencing post-translational modification.Binding interface change and cryptic variation in the evolution of protein-protein interactions.Structure-Based Analysis Reveals Cancer Missense Mutations Target Protein Interaction InterfacesAlpha Helices Are More Robust to Mutations than Beta StrandsElucidating common structural features of human pathogenic variations using large-scale atomic-resolution protein networksAnnotating DNA variants is the next major goal for human genetics.Protein-protein interaction networks studies and importance of 3D structure knowledge.Identification of Sequence Variants within Experimentally Validated Protein Interaction Sites Provides New Insights into Molecular Mechanisms of Disease Development.Docking-based modeling of protein-protein interfaces for extensive structural and functional characterization of missense mutations.Integration of structural dynamics and molecular evolution via protein interaction networks: a new era in genomic medicine.Protein-Protein Interface and Disease: Perspective from Biomolecular Networks.GenProBiS: web server for mapping of sequence variants to protein binding sites.Deciphering Supramolecular Structures with Protein-Protein Interaction Network ModelingThe Contribution of Missense Mutations in Core and Rim Residues of Protein-Protein Interfaces to Human Disease.Molecular Principles of Gene Fusion Mediated Rewiring of Protein Interaction Networks in CancerPrediction of phenotypes of missense mutations in human proteins from biological assemblies.VarMod: modelling the functional effects of non-synonymous variants.Drug-Like Protein-Protein Interaction Modulators: Challenges and Opportunities for Drug Discovery and Chemical Biology.
P2860
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P2860
Protein-protein interaction sites are hot spots for disease-associated nonsynonymous SNPs.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh-hant
name
Protein-protein interaction si ...... associated nonsynonymous SNPs.
@en
Protein-protein interaction si ...... associated nonsynonymous SNPs.
@nl
type
label
Protein-protein interaction si ...... associated nonsynonymous SNPs.
@en
Protein-protein interaction si ...... associated nonsynonymous SNPs.
@nl
prefLabel
Protein-protein interaction si ...... associated nonsynonymous SNPs.
@en
Protein-protein interaction si ...... associated nonsynonymous SNPs.
@nl
P2860
P356
P1433
P1476
Protein-protein interaction sites are hot spots for disease-associated nonsynonymous SNPs
@en
P2093
Alessia David
Rozami Razali
P2860
P304
P356
10.1002/HUMU.21656
P577
2011-12-27T00:00:00Z