Evidence map›Paper›PMID 32580944›Full record

ArticleThe Journal of biological chemistry2020

Negatively charged amino acids in the stalk region of membrane proteins reduce ectodomain shedding.

Ryo Iwagishi, Rika Tanaka, Munenosuke Seto, Tomoyo Takagi, Naoko Norioka, Tomoe Ueyama, Teruhisa Kawamura, Junichi Takagi, Yoshihiro Ogawa, Kyoko Shirakabe

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Functional Differences Between SIRPα Splice Isoforms.Genes to cells : devoted to molecular & cellular mechanisms · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Ryo IwagishiDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Kusatsu, Japan.
Rika TanakaDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Kusatsu, Japan.
Munenosuke SetoDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Kusatsu, Japan.
Tomoyo TakagiDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Kusatsu, Japan.
Naoko NoriokaLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Osaka, Japan.
Tomoe UeyamaDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Kusatsu, Japan.
Teruhisa KawamuraDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Kusatsu, Japan.
Junichi TakagiLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Osaka, Japan.
Yoshihiro OgawaDepartment of Molecular and Cellular Metabolism, Graduate School of Medical and Dental Sciences, Tokyo Medical and Dental University, Tokyo, Japan.ORCID 0000-0002-0834-2836
Kyoko ShirakabeDepartment of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Kusatsu, Japan kshira@fc.ritsumei.ac.jp.ORCID 0000-0002-7080-582X
Ritsumeikan University · JPProtein Research Foundation · JPTokyo Medical and Dental University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ectodomain shedding is a post-translational modification mechanism by which the entire extracellular domain of membrane proteins is liberated through juxtamembrane processing. Because shedding rapidly and irreversibly alters the characteristics of cells, this process is properly regulated. However, the molecular mechanisms governing the propensity of membrane proteins to shedding are largely unknown. Here, we present evidence that negatively charged amino acids within the stalk region, an unstructured juxtamembrane region at which shedding occurs, contribute to shedding susceptibility. We show that two

Indexed as

Activated-Leukocyte Cell Adhesion MoleculeADAM17 ProteinAnimalsCell MembraneMiceProtein DomainsRAW 264.7 CellsReceptor, ErbB-4Activated-Leukocyte Cell Adhesion MoleculeADAM17 ProteinAdam17 protein, mouseErbb4 protein, mouseReceptor, ErbB-4activated leukocyte cell adhesion molecule (ALCAM)ADAMalternative splicingectodomain sheddingErb-B2 receptor tyrosine kinase 4 (ERBB4)immunoglobulin-like domainmembrane proteinmetalloproteaseposttranslational modificationstalk region

Identifiers

PMID32580944
PMCPMC7458810
OpenAlexW3037017503

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.