Evidence map›Paper›PMID 21075854›Full record

ArticleThe Journal of biological chemistry2011

The polypeptide binding conformation of calreticulin facilitates its cell-surface expression under conditions of endoplasmic reticulum stress.

Elise Jeffery, Larry Robert Peters, Malini Raghavan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

32 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  4. Article
  5. Article
  6. The role of cellular proteostasis in antitumor immunity.The Journal of biological chemistry · 2022
    Review
  7. Article
  8. Review
  9. Article
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  11. Review
  12. Article
  13. Article
  14. The Novel Type 1 Fimbriae FimH Receptor Calreticulin Plays a Role inFrontiers in cellular and infection microbiology · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Regulation of calreticulin-major histocompatibility complex (MHC) class I interactions by ATP.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  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

3 authors at 1 institution in 1 country.

Elise JefferyDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
Larry Robert Peters
Malini Raghavan
University of Michigan–Ann Arbor · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
INTERACTIONS &MECHANISMS OF FUNCTION OF THE TAP COMPLEXR01AI044115 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MALINI RAGHAVAN · 1999 to 2026
$9.3M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
Calreticulin's functions in the adaptive immune responseR01AI066131 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAGHAVAN, MALINI · 2007 to 2010
$1.7M
NIAID NIH HHS AI066131NIAID NIH HHS R01 AI044115NIAID NIH HHS R01 AI066131NIGMS NIH HHS T32 GM007223NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

We define two classes of calreticulin mutants that retain glycan binding activity; those that display enhanced or reduced polypeptide-specific chaperone activity, due to conformational effects. Under normal conditions, neither set of mutants significantly impacts the ability of calreticulin to mediate assembly and trafficking of major histocompatibility complex class I molecules, which are calreticulin substrates. However, in cells treated with thapsigargin, which depletes endoplasmic reticulum calcium, major histocompatibility complex class I trafficking rates are accelerated coincident with calreticulin secretion, and detection of cell-surface calreticulin is dependent on its polypeptide binding conformations. Together, these findings identify a site on calreticulin that is an important determinant of the induction of its polypeptide binding conformation and demonstrate the relevance of the polypeptide binding conformations of calreticulin to endoplasmic reticulum stress-induced interactions.

Indexed as

Gene Expression RegulationStress, PhysiologicalUnfolded Protein ResponseAnimalsCalbindin 2CalciumCatalytic DomainCell LineEndoplasmic ReticulumEnzyme InhibitorsHistocompatibility Antigens Class IHumansMiceMolecular ChaperonesMutationPeptide MappingCalbindin 2CalciumEnzyme InhibitorsHistocompatibility Antigens Class IMolecular ChaperonesS100 Calcium Binding Protein GThapsigargin

Identifiers

PMID21075854
PMCPMC3024734
OpenAlexW2054214630

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.