Evidence map›Paper›PMID 10377434›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Conformational variants of class II MHC/peptide complexes induced by N- and C-terminal extensions of minimal peptide epitopes.

O Rötzschke, K Falk, J Mack, J M Lau, G Jung, J L Strominger

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Synthetic High-density Lipoprotein Nanodiscs for Personalized Immunotherapy Against Gliomas.Clinical cancer research : an official journal of the American Association for Cancer Research · 2020
    Article
  2. Article
  3. Immunogenic peptide discovery in cancer genomes.Current opinion in genetics & development · 2015
    Review
  4. Article
  5. Structural Insights Into HLA-DM Mediated MHC II Peptide Exchange.Current topics in biochemical research · 2011
    Article
  6. Review
  7. Article
  8. A pH-sensitive histidine residue as control element for ligand release from HLA-DR molecules.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  9. Paradoxical intrathymic positive selection in mice with only a covalently presented agonist peptide.Proceedings of the National Academy of Sciences of the United States of America · 2001
    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

6 authors.

O RötzschkeDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
K Falk
J Mack
J M Lau
G Jung
J L Strominger

Funding

CHEMISTRY AND BIOLOGY OF LYMPHOCYTESR35CA047554 · NCI · HARVARD UNIVERSITY · PI STROMINGER, JACK L · 1988 to 2001
$4.7M
MHC-BOUND SELF-PEPTIDES IN AUTOIMMUNE DISEASEN01AI045198 · NIAID · HARVARD UNIVERSITY · PI STROMINGER, JACK L · 1994 to 1998
–
NCI NIH HHS 5R35-CA47554NIAID NIH HHS N01-AI-45198
6 · The paper itself

Abstract

Class II MHC molecules are known to exist in conformational variants. "Floppy" and "compact" forms of murine MHC molecules, for example, are discriminated by their migration behavior on SDS/PAGE and represent empty and ligand-loaded forms. Here we show that formation of distinctly faster-migrating ligand complexes (F-forms) rather than the normal compact (C-) forms of HLA-DR1 or -DR4 results from extensions of minimal peptide epitopes (such as HA306-318 or IC106-120) by approximately 10 amino acids at either the N or the C terminus. Two similar but distinct F-forms (FI and FII) were detected, depending on the site of the extension. Both F-forms were characterized by increased surface hydrophobicity and reduced SDS-stability. Native gel separations and size exclusion chromatography indicated that the F-forms had increased hydrodynamic radii compared with the C-form and an apparent size similar to that of empty MHC molecules. The regions on the ligand overhangs responsible for the effect began at a distance of approximately 5 amino acids on either side of the epitopes, comprised 4-8 amino acids (i.e., a total overhang of 9-14), and did not have a particular sequence preference. The possible functional significance of these forms is discussed.

Indexed as

Antigen PresentationProtein ConformationEpitopesHLA-D AntigensHumansLigandsPeptidesStructure-Activity RelationshipEpitopesHLA-D AntigensLigandsPeptides

Identifiers

PMID10377434
PMCPMC22105

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.