Evidence map›Paper›PMID 21837552›Full record

ReviewCellular & molecular biology letters2011

ERp57/GRP58: a protein with multiple functions.

Carlo Turano, Elisa Gaucci, Caterina Grillo, Silvia Chichiarelli

Open access · hybridAbstract readReview
In one paragraph

Review in Cellular & molecular biology letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

66 citing papers in PubMed, 132 citations in OpenAlex.

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  15. 1700029I15Rik orchestrates the biosynthesis of acrosomal membrane proteins required for sperm-egg interaction.Proceedings of the National Academy of Sciences of the United States of America · 2023
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6 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Carlo TuranoIstituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Sapienza, Università di Roma, Roma, Italy. carlo.turano@uniroma1.it
Elisa Gaucci
Caterina Grillo
Silvia Chichiarelli
Istituto Pasteur · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein ERp57/GRP58 is a stress-responsive protein and a component of the protein disulfide isomerase family. Its functions in the endoplasmic reticulum are well known, concerning mainly the proper folding and quality control of glycoproteins, and participation in the assembly of the major histocompatibility complex class 1. However, ERp57 is present in many other subcellular locations, where it is involved in a variety of functions, primarily suggested by its participation in complexes with other proteins and even with DNA. While in some instances these roles need to be confirmed by further studies, a great number of observations support the participation of ERp57 in signal transduction from the cell surface, in regulatory processes taking place in the nucleus, and in multimeric protein complexes involved in DNA repair.

Indexed as

Gene Expression RegulationAdaptation, BiologicalAnimalsCalcitriolCell NucleusDNADNA RepairEndoplasmic ReticulumHistocompatibility Antigens Class IHumansMiceMolecular ChaperonesProtein BindingProtein Disulfide-IsomerasesProtein Structure, TertiaryRatsCalcitriolDNAHistocompatibility Antigens Class IMolecular ChaperonesPDIA3 protein, humanPdia3 protein, mouseProtein Disulfide-IsomerasesSTAT3 Transcription Factor

Identifiers

PMID21837552
PMCPMC6275603
OpenAlexW2002987613

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.