Evidence map›Paper›PMID 7816058›Full record

ReviewMolecular and cellular biochemistry1994

Calreticulin: not just another calcium-binding protein.

P D Nash, M Opas, M Michalak

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular and cellular biochemistry, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 134 citations in OpenAlex.

  1. Article
  2. Luminal transport through intact endoplasmic reticulum limits the magnitude of localized CaProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. Article
  5. Dissecting physical structure of calreticulin, an intrinsically disordered CaJournal of biomolecular structure & dynamics · 2018
    Article
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  16. Article
  17. The role of saliva in tick feeding.Frontiers in bioscience (Landmark edition) · 2009
    Review
  18. Article
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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 2 institutions in 1 country.

P D NashDepartment of Biochemistry, University of Alberta, Edmonton, Canada.
M Opas
M Michalak
University of Alberta · CAUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this paper we review some of the rapidly expanding information about calreticulin, a Ca(2+)-binding/storage protein of the endoplasmic reticulum. The emphasis is placed on the structure and function of calreticulin. We believe that calreticulin is a multifunctional Ca(2+)-binding protein and that distinct functional properties of the protein may be localized to each of the three structural domains of calreticulin. Most evidence indicates that calreticulin is a resident endoplasmic reticulum protein. However, it can also be found outside of the endoplasmic reticulum compartment, i.e. in the nuclear envelope, in the nucleus, in the cytotoxic granules in T-lymphocytes and in acrosomal vesicles of sperm cells. The evidence reviewed here clearly suggests that calreticulin has other functions in addition to its role as a Ca2+ storage protein in the endoplasmic reticulum.

Indexed as

Amino Acid SequenceAnimalsAutoantigensBiological TransportCalcium-Binding ProteinsCalreticulinEndoplasmic ReticulumHumansMolecular Sequence DataProtein Structure, TertiaryRibonucleoproteinsSequence Homology, Amino AcidStructure-Activity RelationshipAutoantigensCalcium-Binding ProteinsCalreticulinRibonucleoproteins

Identifiers

PMID7816058
OpenAlexW1967328876

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.