Evidence map›Paper›PMID 22461020›Full record

ReviewSeminars in immunopathology2012

Roles for major histocompatibility complex glycosylation in immune function.

Sean O Ryan, Brian A Cobb

Open access · greenAbstract readReview
In one paragraph

Review in Seminars in immunopathology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

49 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Review
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  5. Article
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  7. Galectin-9 binding to HLA-DR in dendritic cells controls immune synapse formation and T cell proliferation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Review
  10. Frontiers in immunology · 2025
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Immunometabolism (Cobham, Surrey) · 2023
    Review
  18. Review
  19. Review
  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

2 authors at 2 institutions in 1 country.

Sean O RyanDepartment of Pathology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Brian A Cobb
Case Western Reserve University · USUniversity School · US

Funding

Antigenic Carbohydrate Structure, Function, and SpecificityR01GM082916 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI COBB, BRIAN A · 2009 to 2016
$1.9M
T cell Dependent Immune Responses to Carbohydrate AntigensDP2OD004225 · OD · CASE WESTERN RESERVE UNIVERSITY · PI COBB, BRIAN A · 2008 to 2008
$1.9M
NIGMS NIH HHS GM082916NIGMS NIH HHS R01 GM082916NIH HHS DP2 OD004225NIH HHS OD004225
6 · The paper itself

Abstract

The major histocompatibility complex (MHC) glycoprotein family, also referred to as human leukocyte antigens, present endogenous and exogenous antigens to T lymphocytes for recognition and response. These molecules play a central role in enabling the immune system to distinguish self from non-self, which is the basis for protective immunity against pathogenic infections and disease while at the same time representing a serious obstacle for tissue transplantation. All known MHC family members, like the majority of secreted, cell surface, and other immune-related molecules, carry asparagine (N)-linked glycans. The immune system has evolved increasing complexity in higher-order organisms along with a more complex pattern of protein glycosylation, a relationship that may contribute to immune function beyond the early protein quality control events in the endoplasmic reticulum that are commonly known. The broad MHC family maintains peptide sequence motifs for glycosylation at sites that are highly conserved across evolution, suggesting importance, yet functional roles for these glycans remain largely elusive. In this review, we will summarize what is known about MHC glycosylation and provide new insight for additional functional roles for this glycoprotein modification in mediating immune responses.

Indexed as

Antigen PresentationAmino Acid SequenceBinding SitesGlycosylationHLA AntigensHumansMajor Histocompatibility ComplexPolysaccharidesProtein Structure, SecondaryProtein Structure, TertiarySequence AlignmentT-LymphocytesHLA AntigensPolysaccharides

Identifiers

PMID22461020
PMCPMC3884644
OpenAlexW2013075345

What OpenQuestion holds

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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.