Metamorphic proteins mediate evolutionary transitions of structure
about
Experimental support for the evolution of symmetric protein architecture from a simple peptide motifWhy reinvent the wheel? Building new proteins based on ready-made partsMembrane deformation by neolectins with engineered glycolipid binding sitesA designed point mutant in Fis1 disrupts dimerization and mitochondrial fissionA vocabulary of ancient peptides at the origin of folded proteinsStructural gymnastics of multifunctional metamorphic proteins.Evolutionary bridges to new protein folds: design of C-terminal Cro protein chameleon sequences.Effects of point mutations on protein structure are nonexponentially distributed.A polymetamorphic protein.Functional β-propeller lectins by tandem duplications of repetitive units.New structural and functional contexts of the Dx[DN]xDG linear motif: insights into evolution of calcium-binding proteinsComputational design of a self-assembling symmetrical β-propeller protein.Subdomain interactions foster the design of two protein pairs with ∼80% sequence identity but different folds.Regulated unfolding of proteins in signalingOrigination of the Protein Fold Repertoire from Oily Pluripotent Peptides.Protein conformational switches: from nature to design.Emergence of symmetric protein architecture from a simple peptide motif: evolutionary models.Binding sugars: from natural lectins to synthetic receptors and engineered neolectins.Interpreting functional effects of coding variants: challenges in proteome-scale prediction, annotation and assessment.A NAD(P) reductase like protein is the salicylic acid receptor in the appendix of the Sauromatum guttatum inflorescence.The role of defensive ecological interactions in the evolution of conotoxins.De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints.Evolution of a protein folding nucleusTwo modes of protein sequence evolution and their compositional dependencies.Potential steps in the evolution of a fused trimeric all-β dUTPase involve a catalytically competent fused dimeric intermediate.Extant fold-switching proteins are widespread.Cooperative amino acid changes shift the response of the σ54-dependent regulator XylR from natural m-xylene towards xenobiotic 2,4-dinitrotoluene
P2860
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P2860
Metamorphic proteins mediate evolutionary transitions of structure
description
2010 nî lūn-bûn
@nan
2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Metamorphic proteins mediate evolutionary transitions of structure
@ast
Metamorphic proteins mediate evolutionary transitions of structure
@en
Metamorphic proteins mediate evolutionary transitions of structure
@nl
type
label
Metamorphic proteins mediate evolutionary transitions of structure
@ast
Metamorphic proteins mediate evolutionary transitions of structure
@en
Metamorphic proteins mediate evolutionary transitions of structure
@nl
prefLabel
Metamorphic proteins mediate evolutionary transitions of structure
@ast
Metamorphic proteins mediate evolutionary transitions of structure
@en
Metamorphic proteins mediate evolutionary transitions of structure
@nl
P2093
P2860
P356
P1476
Metamorphic proteins mediate evolutionary transitions of structure
@en
P2093
Dan S Tawfik
Itamar Yadid
Noam Kirshenbaum
P2860
P304
P356
10.1073/PNAS.0912616107
P407
P577
2010-04-20T00:00:00Z