Natural selection against protein aggregation on self-interacting and essential proteins in yeast, fly, and worm.
about
Aggregation propensity of the human proteomeA model of proteostatic energy cost and its use in analysis of proteome trends and sequence evolutionSelection on protein structure, interaction, and sequence.An evolutionary and structural characterization of mammalian protein complex organization.Protein aggregation profile of the bacterial cytosol.Evolution of protein binding modes in homooligomers.Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric statesImpact of translational error-induced and error-free misfolding on the rate of protein evolution.Insights into the evolutionary features of human neurodegenerative diseases.The influence of selection for protein stability on dN/dS estimationsEvolutionary capacitance and control of protein stability in protein-protein interaction networks.Nuclear bodies: random aggregates of sticky proteins or crucibles of macromolecular assembly?Proteome-wide prediction of self-interacting proteins based on multiple properties.Population size dependence of fitness effect distribution and substitution rate probed by biophysical model of protein thermostability.X chromosome reactivation perturbs intracellular self/not-self discrimination.Computational approaches to understanding protein aggregation in neurodegeneration.Prediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes.Evolutionary selection for protein aggregation.Three independent determinants of protein evolutionary rate.Predicting aggregation-prone sequences in proteins.Understanding and predicting protein misfolding and aggregation: Insights from proteomics.SPAR: a random forest-based predictor for self-interacting proteins with fine-grained domain information.Protein aggregation profile of the human kinomeHighly abundant proteins favor more stable 3D structures in yeast.Disorderness in Escherichia coli proteome: perception of folding fidelity and protein-protein interactions.Random protein sequences can form defined secondary structures and are well-tolerated in vivo.Discovering Putative Prion-Like Proteins in : A Computational and Experimental Analysis
P2860
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P2860
Natural selection against protein aggregation on self-interacting and essential proteins in yeast, fly, and worm.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh-hant
name
Natural selection against prot ...... teins in yeast, fly, and worm.
@en
Natural selection against prot ...... teins in yeast, fly, and worm.
@nl
type
label
Natural selection against prot ...... teins in yeast, fly, and worm.
@en
Natural selection against prot ...... teins in yeast, fly, and worm.
@nl
prefLabel
Natural selection against prot ...... teins in yeast, fly, and worm.
@en
Natural selection against prot ...... teins in yeast, fly, and worm.
@nl
P2860
P356
P1476
Natural selection against prot ...... teins in yeast, fly, and worm.
@en
P2093
Yiwen Chen
P2860
P304
P356
10.1093/MOLBEV/MSN122
P577
2008-05-23T00:00:00Z