Evidence map›Paper›PMID 35364718›Full record

ReviewMolecular biology reports2022

N-glycosylation, a leading role in viral infection and immunity development.

Vijay Kant Pandey, Rajani Sharma, Gopal Kumar Prajapati, Tapan Kumar Mohanta, Awdhesh Kumar Mishra

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular biology reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

29 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Quantitative Modeling of IgG N-Glycosylation Profiles from Population Data.International journal of molecular sciences · 2025
    Article
  7. Article
  8. Review
  9. Biochemistry and biophysics reports · 2025
    Article
  10. Article
  11. The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025
    Review
  12. Article
  13. A Closer Look at Dystonia with the Glycosylation.Cellular and molecular neurobiology · 2025
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review
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

5 authors at 3 institutions in 3 countries.

Vijay Kant PandeyDepartment of Agriculture, Netaji Subhas University, Jamshedpur, Jharkhand, India.
Rajani SharmaDepartment of Biotechnology, Amity University Jharkhand, Niwaranpur, Ranchi, 834002, India. rsharma@rnc.amity.edu.ORCID http://orcid.org/0000-0002-3474-4433
Gopal Kumar PrajapatiPromea Therapeutics Pvt. Ltd, Hyderabad, India.
Tapan Kumar MohantaMedicinal Sciences Research Center, University of Nizwa, 616, Nizwa, Oman.
Awdhesh Kumar MishraDepartment of Biotechnology, Yeungnam University, Gyeongsan, Gyeongbuk, 38541, South Korea. awadhesh.biotech07@gmail.com.
Amity University · AEUniversity of Nizwa · OMYeungnam University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-linked protein glycosylation is an essential co-and posttranslational protein modification that occurs in all three domains of life; the assembly of N-glycans follows a complex sequence of events spanning the (Endoplasmic Reticulum) ER and the Golgi apparatus. It has a significant impact on both physicochemical properties and biological functions. It plays a significant role in protein folding and quality control, glycoprotein interaction, signal transduction, viral attachment, and immune response to infection. Glycoengineering of protein employed for improving protein properties and plays a vital role in the production of recombinant glycoproteins and struggles to humanize recombinant therapeutic proteins. It considers an alternative platform for biopharmaceuticals production. Many immune proteins and antibodies are glycosylated. Pathogen's glycoproteins play vital roles during the infection cycle and their expression of specific oligosaccharides via the N-glycosylation pathway to evade detection by the host immune system. This review focuses on the aspects of N-glycosylation processing, glycoengineering approaches, their role in viral attachment, and immune responses to infection.

Indexed as

Golgi ApparatusVirus DiseasesEndoplasmic ReticulumGlycoproteinsGlycosylationHumansPolysaccharidesRecombinant ProteinsGlycoproteinsPolysaccharidesRecombinant ProteinsGlycoengineeringImmune responseN-glycanPosttranslational modificationsViral infection

Identifiers

PMID35364718
PMCPMC8974804
OpenAlexW4225533659

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.