Evidence map›Paper›PMID 34580715›Full record

ReviewJournal of biochemistry2022

Physiological importance of NGLY1, as revealed by rodent model analyses.

Haruhiko Fujihira, Makoto Asahina, Tadashi Suzuki

Erratum issuedOpen access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Journal of biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

8 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Haruhiko FujihiraGlycometabolic Biochemistry Laboratory, RIKEN Cluster for Pioneering Research, RIKEN, Saitama, 3510198, Japan.
Makoto AsahinaT-CiRA Discovery, Takeda Pharmaceutical Company Ltd, Kanagawa, 2518555, Japan.
Tadashi SuzukiGlycometabolic Biochemistry Laboratory, RIKEN Cluster for Pioneering Research, RIKEN, Saitama, 3510198, Japan.
Takeda (Japan) · JPJuntendo University · JP

Funding

Grants-in-Aid for Scientific Research 18H03990Japan Agency for Medical Research and Development-Core Research for Evolutional Science and Technology JP21gm1410003Kyoto UniversityRIKEN Pioneering Research Project
6 · The paper itself

Abstract

Cytosolic peptide:N-glycanase (NGLY1) is an enzyme that cleaves N-glycans from glycoproteins that has been retrotranslocated from the endoplasmic reticulum (ER) lumen into the cytosol. It is known that NGLY1 is involved in the degradation of cytosolic glycans (non-lysosomal glycan degradation) as well as ER-associated degradation, a quality control system for newly synthesized glycoproteins. The discovery of NGLY1 deficiency, which is caused by mutations in the human NGLY1 gene and results in multisystemic symptoms, has attracted interest in the physiological functions of NGLY1 in mammals. Studies using various animal models led to the identification of possible factors that contribute to the pathogenesis of NGLY1 deficiency. In this review, we summarize phenotypic consequences that have been reported for various Ngly1-deficient rodent models and discuss future perspectives to provide more insights into the physiological functions of NGLY1.

Indexed as

Endoplasmic Reticulum-Associated DegradationRodentiaAnimalsCytosolGlycoproteinsPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseGlycoproteinsPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseENGASEFBS2NGLY1NGLY1 deficiencyrodent model

Identifiers

PMID34580715
OpenAlexW3203288134

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.