ArticleNature biotechnology2003
Sialylated endogenous glycoconjugates in plant cells.
Article in Nature biotechnology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
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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.
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Who cites it
12 citing papers in PubMed, 86 citations in OpenAlex.
- Glyco-Engineering of Plant-Based Expression Systems.Advances in biochemical engineering/biotechnology · 2021Article
- Structural basis for the delivery of activated sialic acid into Golgi for sialyation.Nature structural & molecular biology · 2019Article
- Article
- Sialic acid utilization.Advances in nutrition (Bethesda, Md.) · 2012Review
- Engineering mammalian mucin-type O-glycosylation in plants.The Journal of biological chemistry · 2012Article
- Green algae Chlamydomonas reinhardtii possess endogenous sialylated N-glycans.FEBS open bio · 2011Article
- Metabolic glycoengineering: sialic acid and beyond.Glycobiology · 2009Review
- Construction of a functional CMP-sialic acid biosynthesis pathway in Arabidopsis.Plant physiology · 2008Article
- A human anti-Pseudomonas aeruginosa serotype O6ad immunoglobulin G1 expressed in transgenic tobacco is capable of recruiting immune system effector function in vitro.Antimicrobial agents and chemotherapy · 2007Article
- Article
- A genetic and structural analysis of the N-glycosylation capabilities.Plant molecular biology · 2004Article
- Plants as bioreactors: Recent developments and emerging opportunities.Biotechnology advancesReview
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bioengineered plants are emerging as promising systems for the production of therapeutically valuable proteins. It has been commonly accepted that plants do not perform mammalian-like post-translational modifications, particularly sialylation of glycoconjugates, and no evidence has previously been reported to suggest that they have such capabilities. Here we report the presence of sialylated glycoconjugates in suspension-cultured cells of Arabidopsis thaliana and suggest that a genetic and enzymatic basis for sialylation exists in plants.
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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.