Evidence map›Paper›PMID 33263189›Full record

ArticleFEBS letters2021

Identification of two subtilisin-like serine proteases engaged in the degradation of recombinant proteins in Nicotiana benthamiana.

Alejandro A Puchol Tarazona, Daniel Maresch, Annette Grill, Janet Bakalarz, Juan A Torres Acosta, Alexandra Castilho, Herta Steinkellner, Lukas Mach

Open access · hybridAbstract read
In one paragraph

Article in FEBS letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Green Biologics: Harnessing the Power of Plants to Produce Pharmaceuticals.International journal of molecular sciences · 2023
    Review
  9. Article
  10. Plant-based biopharmaceutical engineering.Nature reviews bioengineering · 2023
    Review
  11. Article
  12. Review
  13. Transient proteolysis reduction ofFrontiers in plant science · 2022
    Article
  14. Article
  15. 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

8 authors at 1 institution in 1 country.

Alejandro A Puchol TarazonaDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Daniel MareschDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
Annette GrillDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Janet BakalarzDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Juan A Torres AcostaDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Alexandra CastilhoDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Herta SteinkellnerDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Lukas MachDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.ORCID 0000-0001-9013-5408
BOKU University · AT

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

The tobacco variant Nicotiana benthamiana has recently emerged as a versatile host for the manufacturing of protein therapeutics, but the fidelity of many recombinant proteins generated in this system is compromised by inadvertent proteolysis. Previous studies have revealed that the anti-HIV-1 antibodies 2F5 and PG9 as well as the protease inhibitor α

Indexed as

Agrobacterium tumefaciensalpha 1-AntitrypsinAmino Acid Chloromethyl KetonesAntibodies, MonoclonalGene ExpressionHIV AntibodiesIsoenzymesNicotianaPhenylmethylsulfonyl FluoridePlant ProteinsPlants, Genetically ModifiedProtease InhibitorsProteolysisRecombinant ProteinsSubtilisinsalpha 1-AntitrypsinAmino Acid Chloromethyl KetonesAntibodies, Monoclonalbenzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketoneHIV AntibodiesIsoenzymesN-acetyl-tyrosyl-valyl-alanyl-aspartyl chloromethyl ketonePhenylmethylsulfonyl FluoridePlant ProteinsProtease InhibitorsRecombinant ProteinsSubtilisinsbiopharmaceuticalmolecular farmingmonoclonal antibodyNicotiana benthamianarecombinant protein expressionserine protease

Identifiers

PMID33263189
PMCPMC8221030
OpenAlexW3107585175

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.