Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
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Analyzing effects of naturally occurring missense mutationsStructural and physico-chemical effects of disease and non-disease nsSNPs on proteinsMolecular mechanisms of disease-causing missense mutationsChronic Beryllium Disease: revealing the role of beryllium ion and small peptides binding to HLA-DP2Cancer missense mutations alter binding properties of proteins and their interaction networksCombining structural modeling with ensemble machine learning to accurately predict protein fold stability and binding affinity effects upon mutationRational design of small-molecule stabilizers of spermine synthase dimer by virtual screening and free energy-based approachIn silico and in vitro investigations of the mutability of disease-causing missense mutation sites in spermine synthaseDomain-mediated protein interaction prediction: From genome to network.Modulating protein-protein interactions with small molecules: the importance of binding hotspots.An X-linked channelopathy with cardiomegaly due to a CLIC2 mutation enhancing ryanodine receptor channel activity.siRNA knockdown of ribosomal protein gene RPL19 abrogates the aggressive phenotype of human prostate cancer.Determining effects of non-synonymous SNPs on protein-protein interactions using supervised and semi-supervised learning.Computational analysis of missense mutations causing Snyder-Robinson syndromeOncogenic potential is related to activating effect of cancer single and double somatic mutations in receptor tyrosine kinasesEnhancing human spermine synthase activity by engineered mutationsOn the role of electrostatics in protein-protein interactions.Predicting the Impact of Missense Mutations on Protein-Protein Binding Affinity.On the energy components governing molecular recognition in the framework of continuum approachesPredicting folding free energy changes upon single point mutationsStructural assessment of the effects of amino acid substitutions on protein stability and protein protein interaction.Convert your favorite protein modeling program into a mutation predictor: "MODICT"SAAMBE: Webserver to Predict the Charge of Binding Free Energy Caused by Amino Acids Mutations.A survey of proteins encoded by non-synonymous single nucleotide polymorphisms reveals a significant fraction with altered stability and activity.Docking-based modeling of protein-protein interfaces for extensive structural and functional characterization of missense mutations.Exploring Protein-Protein Interactions as Drug Targets for Anti-cancer Therapy with In Silico Workflows.Integration of structural dynamics and molecular evolution via protein interaction networks: a new era in genomic medicine.Annotating Mutational Effects on Proteins and Protein Interactions: Designing Novel and Revisiting Existing Protocols.Purification of Ovine Respiratory Complex I Results in a Highly Active and Stable Preparation.Computational investigation of cancer-associated molecular mechanism in Aurora A (S155R) mutation.On human disease-causing amino acid variants: statistical study of sequence and structural patterns.Revealing the Effects of Missense Mutations Causing Snyder-Robinson Syndrome on the Stability and Dimerization of Spermine Synthase.The Contribution of Missense Mutations in Core and Rim Residues of Protein-Protein Interfaces to Human Disease.Screening of nucleotide variations in genomic sequences encoding charged protein regions in the human genome.Decoding disease-causing mechanisms of missense mutations from supramolecular structures.Prediction of phenotypes of missense mutations in human proteins from biological assemblies.A rational free energy-based approach to understanding and targeting disease-causing missense mutationsA Y328C missense mutation in spermine synthase causes a mild form of Snyder-Robinson syndrome.Molecular docking and molecular dynamics study on the effect of ERCC1 deleterious polymorphisms in ERCC1-XPF heterodimer.Investigation of binding phenomenon of NSP3 and p130Cas mutants and their effect on cell signalling.
P2860
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P2860
Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
description
2009 nî lūn-bûn
@nan
2009 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մարտին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
@ast
Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
@en
Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
@nl
type
label
Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
@ast
Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
@en
Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
@nl
prefLabel
Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
@ast
Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
@en
Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
@nl
P2093
P2860
P3181
P1433
P1476
Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
@en
P2093
Anna Panchenko
Emil Alexov
Shaolei Teng
Thomas Madej
P2860
P304
P3181
P356
10.1016/J.BPJ.2008.12.3904
P407
P577
2009-03-18T00:00:00Z