(Q47982690)

7 February 2018

title

Statistical properties of neutral evolution. (English)

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7 February 2018

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1

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7 February 2018

Michele Vendruscolo

series ordinal

4

object named as

Michele Vendruscolo

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7 February 2018

Markus Porto

2

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7 February 2018

H Eduardo Roman

series ordinal

3

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7 February 2018

publication date

1 January 2003

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7 February 2018

Journal of Molecular Evolution

published in

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7 February 2018

volume

57 Suppl 1

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7 February 2018

page(s)

S103-19

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7 February 2018

https://scigraph.springernature.com/pub.10.1007/s00239-003-0013-4

exact match

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cites work

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Adaptive protein evolution in Drosophila

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Evolution-like selection of fast-folding model proteins

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Neutral evolution of model proteins: diffusion in sequence space and overdispersion

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Mapping the protein universe

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Neutral networks in protein space: a computational study based on knowledge-based potentials of mean force

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Lineage effects and the index of dispersion of molecular evolution

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Non-functional conserved residues in globins and their possible role as a folding nucleus

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Fitting Discrete Probability Distributions to Evolutionary Events

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Non-Darwinian Evolution

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Optimal protein-folding codes from spin-glass theory

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Rates of DNA sequence evolution differ between taxonomic groups

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How to derive a protein folding potential? A new approach to an old problem

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Slightly Deleterious Mutant Substitutions in Evolution

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An examination of the constancy of the rate of molecular evolution

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Protein structures sustain evolutionary drift

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A statistical mechanical method to optimize energy functions for protein folding

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Enlarged representative set of protein structures

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A Method to Identify Protein Sequences That Fold into a Known Three-Dimensional Structure

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How are model protein structures distributed in sequence space?

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Evolutionary Rate at the Molecular Level

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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Preponderance of synonymous changes as evidence for the neutral theory of molecular evolution

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How to guarantee optimal stability for most representative structures in the Protein Data Bank.

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The foldability landscape of model proteins

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12 December 2020

10.1007/S00239-003-0013-4

Identifiers

DOI

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7 February 2018

release_tu2acdqwlbbchcywwim53f5wiy

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PubMed ID

15008407

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7 February 2018