Evidence map›Paper›PMID 21151648›Full record

ArticleJournal of biomedicine & biotechnology2010

The expression of soluble and active recombinant Haemophilus influenzae IgA1 protease in E. coli.

Shinong Long, Elaine Phan, Michel C Vellard

Open access · hybridAbstract read
In one paragraph

Article in Journal of biomedicine & biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 35% of its field
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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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

3 authors at 1 institution in 1 country.

Shinong LongDepartment of Cellular and Molecular Biology, BioMarin Pharmaceutical Inc., 105 Digital Drive, Novato, CA 94949, USA. slong@bmrn.com
Elaine Phan
Michel C Vellard
BioMarin (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Immunoglobulin A1 (IgA1) proteases from Haemophilus influenzae are extracellular proteases that specifically cleave the hinge region of human IgA1, the predominant class of immunoglobulin present on mucosal membranes. The IgA1 proteases may have the potential to cleave IgA1 complexes in the kidney and be a therapeutic agent for IgA1 nephropathy (IgAN), a disease characterized by deposition of the IgA1 antibody in the glomerulus. We have screened for the expression of recombinant H. influenzae IgA1 protease by combining various expression plasmids, IgA1 protease constructs, and E. coli strains under multiple conditions. Using the method we have developed, approximately 20-40 mg/L of soluble and active H. influenzae IgA1 protease can be produced from E. coli strain C41(DE3), a significant increase in yield compared to the yield upon expression in H. influenzae or other related bacteria.

Indexed as

BiotechnologyElectrophoresis, Polyacrylamide GelEnzyme ActivationEnzyme-Linked Immunosorbent AssayEscherichia coliHaemophilus influenzaeHumansInclusion BodiesRecombinant ProteinsSerine EndopeptidasesSolubilityIgA-specific serine endopeptidaseRecombinant ProteinsSerine Endopeptidases

Identifiers

PMID21151648
PMCPMC2995913
OpenAlexW2003044934

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.