ArticleJournal of Tongji Medical University = Tong ji yi ke da xue xue bao1998
Effect of fragment Asp1961-Glu1978 in fibronectin on the expression of triple-domain polypeptide in E. coli.
Article in Journal of Tongji Medical University = Tong ji yi ke da xue xue bao, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed, 0 citations in OpenAlex.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two plasmids were constructed and used to express two triple-domain recombinant polypeptide of human fibronectin (FN). The cDNAs in plasmids code for two polypeptides, CH62 (Pro1239-Ser1515 of FN linked with Ala1690-Val2049 through Met) and CH63 (CH62 without Ile1850-Glu1978). The expression level of CH62 in E. coli was very low, but that of CH63 was very high. The results suggests that Asp1961-Glu1978 in FN is a key sequence influencing the expression of triple-domain polypeptide in E. Coli. After being dissolved and renatured, CH63 can be purified by heparin-agarose affinity chromatography. Both of the cell-binding domains in the recombinant polypeptide were functional. The production of CH63 provides a fundamental basis for further study of recombinant products with better anti-metastasis function.
Indexed as
Identifiers
What 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.