In silico and in vitro investigations of the mutability of disease-causing missense mutation sites in spermine synthase
about
DelPhi: a comprehensive suite for DelPhi software and associated resourcesAnalyzing effects of naturally occurring missense mutationsStructural and physico-chemical effects of disease and non-disease nsSNPs on proteinsMolecular mechanisms of disease-causing missense mutationsRational design of small-molecule stabilizers of spermine synthase dimer by virtual screening and free energy-based approachAn X-linked channelopathy with cardiomegaly due to a CLIC2 mutation enhancing ryanodine receptor channel activity.Integrating in silico prediction methods, molecular docking, and molecular dynamics simulation to predict the impact of ALK missense mutations in structural perspectiveOncogenic potential is related to activating effect of cancer single and double somatic mutations in receptor tyrosine kinasesProtein Nano-Object Integrator (ProNOI) for generating atomic style objects for molecular modeling.Enhancing human spermine synthase activity by engineered mutationsRecognition of methylated peptides by Drosophila melanogaster polycomb chromodomainPredicting folding free energy changes upon single point mutationsMutations in the KDM5C ARID Domain and Their Plausible Association with Syndromic Claes-Jensen-Type Disease.SAAMBE: Webserver to Predict the Charge of Binding Free Energy Caused by Amino Acids Mutations.Rational design of a novel propeptide for improving active production of Streptomyces griseus trypsin in Pichia pastoris.Using DelPhi capabilities to mimic protein's conformational reorganization with amino acid specific dielectric constants.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.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.Investigation of binding phenomenon of NSP3 and p130Cas mutants and their effect on cell signalling.Biophysical Aspect of Huntingtin Protein During polyQ: An In Silico Insight.Structure-function studies on non-synonymous SNPs of chemokine receptor gene implicated in cardiovascular disease: a computational approach.Comparative computational assessment of the pathogenicity of mutations in the Aspartoacylase enzyme.Improvement of catalytic efficiency and thermostability of recombinant Streptomyces griseus trypsin by introducing artificial peptide.Advances in Human Biology: Combining Genetics and Molecular Biophysics to Pave the Way for Personalized Diagnostics and Medicine
P2860
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P2860
In silico and in vitro investigations of the mutability of disease-causing missense mutation sites in spermine synthase
description
2011 nî lūn-bûn
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2011 թուականին հրատարակուած գիտական յօդուած
@hyw
2011 թվականին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
In silico and in vitro investi ...... ion sites in spermine synthase
@ast
In silico and in vitro investi ...... ion sites in spermine synthase
@en
In silico and in vitro investi ...... ion sites in spermine synthase
@nl
type
label
In silico and in vitro investi ...... ion sites in spermine synthase
@ast
In silico and in vitro investi ...... ion sites in spermine synthase
@en
In silico and in vitro investi ...... ion sites in spermine synthase
@nl
prefLabel
In silico and in vitro investi ...... ion sites in spermine synthase
@ast
In silico and in vitro investi ...... ion sites in spermine synthase
@en
In silico and in vitro investi ...... ion sites in spermine synthase
@nl
P2093
P2860
P3181
P1433
P1476
In silico and in vitro investi ...... ion sites in spermine synthase
@en
P2093
Charles Schwartz
Emil Alexov
Joy Norris
P2860
P304
P3181
P356
10.1371/JOURNAL.PONE.0020373
P407
P577
2011-01-01T00:00:00Z