Evidence map›Paper›PMID 19261539›Full record

ReviewCurrent opinion in chemical biology2009

Advances in generating functional diversity for directed protein evolution.

Amol V Shivange, Jan Marienhagen, Hemanshu Mundhada, Alexander Schenk, Ulrich Schwaneberg

Abstract readReview
PubMed Publisher
In one paragraph

Review in Current opinion in chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

41 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Metabolic growth-coupling strategies forMetabolic engineering communications · 2025
    Article
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  11. Review
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  15. Review
  16. Article
  17. Advances in the directed evolution of proteins.Current opinion in chemical biology · 2014
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Amol V ShivangeRWTH Aachen University, Germany.
Jan Marienhagen
Hemanshu Mundhada
Alexander Schenk
Ulrich Schwaneberg

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite advances in screening technologies, only a very small fraction of theoretical protein sequence can be sampled in directed evolution experiments. At the current state of random mutagenesis technologies mutation frequencies have often been adjusted to values that cause a limited number of amino acid changes (often one to four amino acid changes per protein). For harvesting the power of directed evolution algorithms it is therefore important that generated mutant libraries are rich in diversity and enriched in active population. Insufficient knowledge about protein traits, mutational robustness of protein folds and technological limitations in diversity generating methods are main challenges for managing the complexity of protein sequence space. This review covers computational and experimental advances for high quality mutant library generation that have been achieved in the past two years.

Indexed as

Gene LibraryComputational BiologyDirected Molecular EvolutionMutant ProteinsProtein EngineeringMutant Proteins

Identifiers

What OpenQuestion holds

Textmetadata
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.