ArticleNew Mexico journal of science2021
Efficient Protocol for Expression and Purification of DUSP5.
Article in New Mexico journal of science, 2021. 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
3 authors at 1 institution in 1 country.
Funding
Abstract
Dual Specificity Phosphatase 5 (DUSP5) is a human protein that targets specific kinases and dephosphorylates phosphoserine/threonine and phosphotyrosine residues. DUSP5 is found to be involved in cardiovascular diseases and many cancer pathways, including skin and breast cancer. For this reason, availability of an efficient protocol of expression and purification of DUSP proteins can play a crucial role in their studies towards better understanding of the disease process and development of better therapeutic approaches. For example, purification of DUSP5 could be used for the in vitro assays of the inhibitors of DUSP5 identified from the in-silico studies. This report provides the full procedure for protein purification thereby allowing the collection of desired amounts of DUSP5 using Glutathione S-transferase (GST) tag. The described method shows an efficient way to solubilize and purify DUSP5 for further protein studies.
Indexed as
Identifiers
36594902PMC9799713W4313489275What 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.