Evidence map›Paper›PMID 7807549›Full record

ArticleJournal of molecular evolution1994

On hypervariability at the reactive center of proteolytic enzymes and their inhibitors.

T Ohta

Abstract read
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In one paragraph

Article in Journal of molecular evolution, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–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

6 citing papers in PubMed.

  1. Article
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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

1 author.

T OhtaNational Institute of Genetics, Mishima, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The pattern of synonymous and nonsynonymous substitutions at the reactive center of proteases (kallikrein) and their inhibitors (alpha 1-antitrypsin and serpin) was examined. In the case of alpha 1-antitrypsin, the proportion of different nonsynonymous sites exceeds that of different synonymous sites at the reactive center for sequence pairs of recent duplication. The result indicates that the positive selection has operated after duplication to increase functional diversity. In the cases of kallikrein, serpin, and remote sequence pairs of alpha 1-antitrypsin, the proportion of different synonymous sites at the reactive center exceeds that of different synonymous sites at the remaining region. The result indicates that gene conversion followed by natural selection is working. On the whole, it is concluded that hypervariability of amino acids at the reactive center is generated by an interaction among natural selection, random genetic drift, point mutation, and gene conversion. Gene duplication may provide potential for them to interact.

Indexed as

alpha 1-AntitrypsinAnimalsBinding SitesBiological EvolutionCattleGene ConversionGenetic VariationGuinea PigsHumansKallikreinsMiceMultigene FamilyPapioPeptide HydrolasesPoint MutationProtease Inhibitorsalpha 1-AntitrypsinKallikreinsPeptide HydrolasesProtease InhibitorsSerpins

Identifiers

PMID7807549

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.