David M. McCandlish
Genetics · 2016–2018
A researcher in the Science corpus: 3 papers; trusts 10 researchers and is trusted by 3 researchers here, as inferred from the citation graph.
Subfields
- Genetics — 37 citations into it; #4,380 of 6,854 by trust here, #4,743 by citations
- Molecular Biology — 31 citations into it; #12,263 of 17,773 by trust here, #13,891 by citations
- Sociology and Political Science — 13 citations into it
- Computational Biology & Bioinformatics — 7 citations into it
- Public Health, Environmental and Occupational Health — 5 citations into it
Whom David M. McCandlish trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
- Jakub Otwinowski
- Daniel M. Weinreich
- H. Jacquier
- Richard A. Goldstein
- Mark A. DePristo
- Nicholas C. Wu
- Matteo Figliuzzi
- Sergey Kryazhimskiy
- C. Scott Wylie
- N. H. Barton
Who trusts David M. McCandlish overall
Papers from David M. McCandlish's perspective
Ordered by how strongly the researchers David M. McCandlish trusts endorse each paper. Same corpus, a different order for every researcher.
- Darwinian Evolution Can Follow Only Very Few Mutational Paths to Fitter Proteins
- Towards a general theory of adaptive walks on rugged landscapes.
- Missense meanderings in sequence space: a biophysical view of protein evolution
- Robustness–epistasis link shapes the fitness landscape of a randomly drifting protein
- Inferring fitness landscapes by regression produces biased estimates of epistasis
- A biophysical protein folding model accounts for most mutational fitness effects in viruses
- Epistasis as the primary factor in molecular evolution
- Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations.
- Capturing the mutational landscape of the beta-lactamase TEM-1
- Mutational effects on stability are largely conserved during protein evolution
Their papers
- Epistasis and the Dynamics of Reversion in Molecular Evolution (2016) — 50 citations
- Inferring the shape of global epistasis (2018) — 249 citations
- Selection for Protein Stability Enriches for Epistatic Interactions (2018) — 9 citations