Cited by 218Glycosylation and Glycoproteins ResearchViral Infectious Diseases and Gene Expression in InsectsCarbohydrate Chemistry and Synthesis

Lectin-resistant CHO glycosylation mutants

Patnaik, Santosh Kumar, Stanley, Pamela·2006·Methods in Enzymology

Abstract

Chinese hamster ovary (CHO) mutant cells with a wide variety of alterations in the glycosylation of proteins and lipids have been isolated by selection for resistance to the cytotoxicity of plant lectins. These CHO mutants have been used to characterize glycosylation pathways, to identify genes that code for glycosylation activities, to elucidate functional roles of glycans that mediate biological processes, and for glycosylation engineering. In this chapter, we briefly describe the available panel of lectin-resistant CHO mutants and summarize their glycan alterations and the biochemical and genetic bases of mutation.

Integrity signals

Registry

Crossref · 10.1016/s0076-6879(06)16011-5

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • CHO cells are unable to produce some types of human glycosylation, such as α-2,6-sialylation and α-1,3/4-fucosylation.

    “Although CHO cells possess many advantages for glycoprotein productions, they are unable to produce some types of human glycosylation, such as α-2,6-sialylation and α-1,3/4-fucosylation (Patnaik and Stanley, 2006).”

    From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Patnaik and Stanley, 2006

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Patnaik, S. K., & Stanley, P.
Affiliations
Albert Einstein College of Medicine (US)
Venue
Methods in Enzymology
Publisher
Elsevier
Published
2006
Volume
416
Pages
159-182
ISSN
0076-6879 (ISSN-L)
OpenAlex
W2105081087
Cited by
218
References
1
Citations by year
2026: 5 · 2025: 7 · 2024: 14 · 2023: 6 · 2022: 11 · 2021: 10 · 2020: 10 · 2019: 10 · 2018: 12 · 2017: 20 · 2016: 9 · 2015: 9 · 2014: 19 · 2013: 12 · 2012: 18
FWCI
13.31
Type
book chapter
Language
en
Open access
closed
Locations
  • Methods in enzymology on CD-ROM/Methods in enzymology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • U.S. Public Health Service (R0136434)
  • National Cancer Institute
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
  • Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
Keywords
CHO cells, protein glycosylation, glycan function, glycosylation engineering, mutant selection
MeSH terms
Animals, Cell Line, Cricetulus, Glycosylation, Cricetinae, Mutation, Polysaccharides, CHO Cells, Lectins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review