Evidence map›Paper›PMID 30554144›Full record

ArticleThe Journal of biological chemistry2019

A serine in the first transmembrane domain of the human E3 ubiquitin ligase MARCH9 is critical for down-regulation of its protein substrates.

Cyrus Tan, Eamon F X Byrne, Casey Ah-Cann, Melissa J Call, Matthew E Call

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

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

12 citing papers in PubMed, 13 citations in OpenAlex.

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  12. How to Inactivate Human Ubiquitin E3 Ligases by Mutation.Frontiers in cell and developmental biology · 2020
    Review
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

5 authors at 2 institutions in 2 countries.

Cyrus TanFrom the Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, 3052 Parkville, Victoria, Australia.
Eamon F X Byrnethe Department of Bioengineering, Stanford University, Stanford, California 94305, and.ORCID 0000-0001-7513-5944
Casey Ah-Cannthe Department of Medical Biology, University of Melbourne, 3052 Parkville, Victoria, Australia.
Melissa J CallFrom the Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, 3052 Parkville, Victoria, Australia, call@wehi.edu.au.ORCID 0000-0001-7684-5841
Matthew E CallFrom the Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, 3052 Parkville, Victoria, Australia, call@wehi.edu.au.ORCID 0000-0001-5846-6469
The University of Melbourne · AUStanford University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The

Indexed as

Down-RegulationGene Expression Regulation, EnzymologicCD4 AntigensHEK293 CellsHLA-A2 AntigenHumansMembrane ProteinsProtein DomainsProtein Structure, SecondarySerineUbiquitin-Protein LigasesCD4 AntigensHLA-A2 AntigenMARCHF9 protein, humanMembrane ProteinsSerineUbiquitin-Protein LigasesE3 ligaseimmunologymajor histocompatibility complex (MHC)membrane-associated RING-CH (MARCH)membrane proteinnuclear magnetic resonance (NMR)receptor endocytosisT-celltransmembrane domainubiquitin ligase

Identifiers

PMID30554144
PMCPMC6378983
OpenAlexW2905571351

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.