Evidence map›Paper›PMID 32057111›Full record

ReviewJournal of cellular physiology2020

Pichia pastoris: A highly successful expression system for optimal synthesis of heterologous proteins.

Mohsen Karbalaei, Seyed A Rezaee, Hadi Farsiani

Abstract readReview
In one paragraph

Review in Journal of cellular physiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 277 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
277citing papers in PubMed, 2 pooled it
–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

277 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Pooled it
  2. Pooled it
  3. Trial
  4. Trial
  5. Development and characterization of a Cre/Synthetic and systems biotechnology · 2027
    Article
  6. Article
  7. Systematic optimization ofEngineering microbiology · 2026
    Review
  8. Reassessment of IRES Element Activity inInternational journal of molecular sciences · 2026
    Article
  9. Article
  10. Review
  11. Metabolic engineering ofApplied and environmental microbiology · 2026
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

217 more citing papers are in PubMed but not listed here.

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.

Mohsen KarbalaeiDepartment of Microbiology and Virology, School of Medicine, Jiroft University of Medical Sciences, Jiroft, Iran.ORCID 0000-0001-9899-2885
Seyed A RezaeeSchool of Medicine, Mashhad University of Medical Sciences, Inflammation and Inflammatory Diseases Research Centre, Mashhad, Iran.ORCID 0000-0001-6814-5992
Hadi FarsianiMashhad University of Medical Sciences, Antimicrobial Resistance Research Center, Mashhad, Iran.ORCID 0000-0002-4738-0245

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of the most important branches of genetic engineering is the expression of recombinant proteins using biological expression systems. Nowadays, different expression systems are used for the production of recombinant proteins including bacteria, yeasts, molds, mammals, plants, and insects. Yeast expression systems such as Saccharomyces cerevisiae (S. cerevisiae) and Pichia pastoris (P. pastoris) are more popular. P. pastoris expression system is one of the most popular and standard tools for the production of recombinant protein in molecular biology. Overall, the benefits of protein production by P. pastoris system include appropriate folding (in the endoplasmic reticulum) and secretion (by Kex2 as signal peptidase) of recombinant proteins to the external environment of the cell. Moreover, in the P. pastoris expression system due to its limited production of endogenous secretory proteins, the purification of recombinant protein is easy. It is also considered a unique host for the expression of subunit vaccines which could significantly affect the growing market of medical biotechnology. Although P. pastoris expression systems are impressive and easy to use with well-defined process protocols, some degree of process optimization is required to achieve maximum production of the target proteins. Methanol and sorbitol concentration, Mut forms, temperature and incubation time have to be adjusted to obtain optimal conditions, which might vary among different strains and externally expressed protein. Eventually, optimal conditions for the production of a recombinant protein in P. pastoris expression system differ according to the target protein.

Indexed as

ProteomicsFungal ProteinsProprotein ConvertasesProtein BiosynthesisRecombinant ProteinsSaccharomyces cerevisiae ProteinsSaccharomycetalesFungal ProteinsKEX2 protein, S cerevisiaeProprotein ConvertasesRecombinant ProteinsSaccharomyces cerevisiae Proteinsexpression systemoptimizationPichia pastorisrecombinant proteinssubunit vaccines

Identifiers

PMID32057111
PMCPMC7228273

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.