Evidence map›Paper›PMID 20413295›Full record

ReviewCurrent opinion in structural biology2010

Analyzing protein structure and function using ancestral gene reconstruction.

Michael J Harms, Joseph W Thornton

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed
8.0field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

126 citing papers in PubMed, 209 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Substrate scope of ancestral versus modern family-1 glycosidases.Protein science : a publication of the Protein Society · 2026
    Article
  6. Article
  7. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Applications of ancestral sequence reconstruction for understanding the evolution of plant specialized metabolism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  18. Article
  19. Genome-Wide Identification and Expression Analysis of theCurrent issues in molecular biology · 2024
    Article
  20. Review

66 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Michael J HarmsHoward Hughes Medical Institute, Center for Ecology and Evolutionary Biology, University of Oregon, Eugene, OR 97403, USA. harms@uoregon.edu
Joseph W Thornton
Howard Hughes Medical Institute · USUniversity of Oregon · US

Funding

Experimental and structural evolution of hormone receptorsR01GM081592 · NIGMS · UNIVERSITY OF OREGON · PI THORNTON, JOSEPH W · 2007 to 2010
$1.3M
Molecular Mechanisms of the Evolution of Steroid Receptor-Ligand InteractionsF32GM090650 · NIGMS · UNIVERSITY OF OREGON · PI HARMS, MICHAEL JONATHAN · 2010 to 2012
$153k
Evolution of Steroid Receptor-Hormone InteractionsF32GM074398 · NIGMS · UNIVERSITY OF OREGON · PI BRIDGHAM, JAMIE T · 2005 to 2006
$99k
Howard Hughes Medical InstituteNIGMS NIH HHS 1F32GM989650NIGMS NIH HHS F32 GM074398NIGMS NIH HHS F32-GM074398NIGMS NIH HHS F32 GM090650NIGMS NIH HHS F32-GM090650NIGMS NIH HHS R01 GM081592NIGMS NIH HHS R01-GM081592
6 · The paper itself

Abstract

Protein families with functionally diverse members can illuminate the structural determinants of protein function and the process by which protein structure and function evolve. To identify the key amino acid changes that differentiate one family member from another, most studies have taken a horizontal approach, swapping candidate residues between present-day family members. This approach has often been stymied, however, by the fact that shifts in function often require multiple interacting mutations; chimeric proteins are often nonfunctional, either because one lineage has amassed mutations that are incompatible with key residues that conferred a new function on other lineages, or because it lacks mutations required to support those key residues. These difficulties can be overcome by using a vertical strategy, which reconstructs ancestral genes and uses them as the appropriate background in which to study the effects of historical mutations on functional diversification. In this review, we discuss the advantages of the vertical strategy and highlight several exemplary studies that have used ancestral gene reconstruction to reveal the molecular underpinnings of protein structure, function, and evolution.

Indexed as

Evolution, MolecularGreen Fluorescent ProteinsHumansOpsinsProteinsReceptors, SteroidGreen Fluorescent ProteinsOpsinsProteinsReceptors, Steroid

Identifiers

PMID20413295
PMCPMC2916957
OpenAlexW2027351435

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.