Evidence map›Paper›PMID 38003717›Full record

ArticleInternational journal of molecular sciences2023

Phytaspase Is Capable of Detaching the Endoplasmic Reticulum Retrieval Signal from Tobacco Calreticulin-3.

Anastasia D Teplova, Artemii A Pigidanov, Marina V Serebryakova, Sergei A Golyshev, Raisa A Galiullina, Nina V Chichkova, Andrey B Vartapetian

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 35% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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

7 authors at 1 institution in 1 country.

Anastasia D TeplovaFaculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 119991, Russia.
Artemii A PigidanovFaculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 119991, Russia.
Marina V SerebryakovaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119991, Russia.
Sergei A GolyshevBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119991, Russia.
Raisa A GaliullinaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119991, Russia.
Nina V ChichkovaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119991, Russia.
Andrey B VartapetianBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow 119991, Russia.ORCID 0000-0003-2296-0929
Lomonosov Moscow State University · RU

Funding

Russian Science Foundation 19-14-00010Russian Science Foundation 22-14-00071
6 · The paper itself

Abstract

Soluble chaperones residing in the endoplasmic reticulum (ER) play vitally important roles in folding and quality control of newly synthesized proteins that transiently pass through the ER en route to their final destinations. These soluble residents of the ER are themselves endowed with an ER retrieval signal that enables the cell to bring the escaped residents back from the Golgi. Here, by using purified proteins, we showed that

Indexed as

CalreticulinNicotianaEndoplasmic ReticulumPeptide HydrolasesPlant ProteinsSubtilisinsCalreticulinPeptide HydrolasesPlant Proteinssubtilase, plantSubtilisinscalreticulin-3endoplasmic reticulumphytaspaseplant cellprotein traffickingproteolytic processingretrieval signal

Identifiers

PMID38003717
PMCPMC10671509
OpenAlexW4388824748

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.