ArticleMolecular diversity1996
Tolerance of different proteins for amino acid diversity.
Article in Molecular diversity, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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.
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Who cites it
7 citing papers in PubMed.
- Mining and Statistical Modeling of Natural and Variant Class IIa Bacteriocins Elucidate Activity and Selectivity Profiles across Species.Applied and environmental microbiology · 2020Article
- On the conservative nature of intragenic recombination.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Controlling the enantioselectivity of enzymes by directed evolution: practical and theoretical ramifications.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Compensatory mutations cause excess of antagonistic epistasis in RNA secondary structure folding.BMC evolutionary biology · 2003Article
- Mutations in human DNA polymerase eta motif II alter bypass of DNA lesions.The EMBO journal · 2001Article
- Scoring functions for computational algorithms applicable to the design of spiked oligonucleotides.Nucleic acids research · 1998Article
- Functional and nonfunctional mutations distinguished by random recombination of homologous genes.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Random mutagenesis of genes followed by positive genetic selection in bacteria requires that the variant molecules confer biological activity, and is thus the most demanding approach for generating new functionally active molecules. Furthermore, one can learn much about the protein in question by comparing the population of selected molecules to the library from which they were selected. Described here is a mathematical method designed to guide such comparisons. We use as examples the results of randomization-selection studies of four different proteins. There exists, in general, a positive correlation between the number of amino acid substitutions in a critical region of a protein and the likelihood of inactivation of that protein; a correlation long suspected, but developed here in detail. At this time, we are comparing regions in different proteins and our conclusions must be limited. However, the method presented can serve as a guideline for anticipating the yield of new active mutants in genetic complementation assays based on the extent of randomization.
Indexed as
Identifiers
9238641What OpenQuestion holds
Registered trials
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.