Evidence map›Paper›PMID 31222623›Full record

ReviewBiological trace element research2019

From Selenium Absorption to Selenoprotein Degradation.

Herena Y Ha, Naghum Alfulaij, Marla J Berry, Lucia A Seale

Open access · greenAbstract readReview
In one paragraph

Review in Biological trace element research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed, 1 pooled it
8.0field-weighted citation impact, top 2% 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

54 citing papers in PubMed, 1 synthesis or guideline pooled it, 121 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Redox Modulation of Erythropoiesis by Selenoproteins.Biological trace element research · 2026
    Review
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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.

Herena Y HaDepartment of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii at Manoa, 651 Ilalo Street, Honolulu, HI, 96813, USA.
Naghum AlfulaijDepartment of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii at Manoa, 651 Ilalo Street, Honolulu, HI, 96813, USA.
Marla J BerryDepartment of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii at Manoa, 651 Ilalo Street, Honolulu, HI, 96813, USA.
Lucia A SealeDepartment of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii at Manoa, 651 Ilalo Street, Honolulu, HI, 96813, USA. lseale@hawaii.edu.ORCID http://orcid.org/0000-0002-0686-7516
University of Hawaiʻi at Mānoa · US

Funding

The Role of gp120 on Cardiovascular Disease in People Living with HIVU54MD007601 · NIMHD · UNIVERSITY OF HAWAII AT MANOA · PI Benjamin C. Fogelgren · 2017 to 2026
$59.5M
RESEARCH DESIGN, BIOSTATISTICS AND RESEARCH ETHICS COREG12MD007601 · NIMHD · UNIVERSITY OF HAWAII AT MANOA · PI BERRY, MARLA J · 2012 to 2016
$13.0M
MECHANISM OF SELENOPROTEIN SYNTHESIS IN EUKARYOTESR01DK047320 · NIDDK · UNIVERSITY OF HAWAII AT MANOA · PI BERRY, MARLA J · 1994 to 2020
$5.8M
NIDDK NIH HHS R01 DK047320NIDDK NIH HHS R01DK47320NIMHD NIH HHS G12 MD007601NIMHD NIH HHS U54 MD007601NIMHD NIH HHS U54MD007601 - subproject 5544Office of Dietary Supplements R01DK47320-S1
6 · The paper itself

Abstract

Selenium is an essential dietary micronutrient. Ingested selenium is absorbed by the intestines and transported to the liver where it is mostly metabolized to selenocysteine (Sec). Sec is then incorporated into selenoproteins, including selenoprotein P (SELENOP), which is secreted into plasma and serves as a source of selenium to other tissues of the body. Herein, we provide an overview of the biology of selenium from its absorption and distribution to selenoprotein uptake and degradation, with a particular focus on the latter. Molecular mechanisms of selenoprotein degradation include the lysosome-mediated pathway for SELENOP and endoplasmic reticulum-mediated degradation of selenoproteins via ubiquitin-activated proteasomal pathways. Ubiquitin-activated pathways targeting full-length selenoproteins include the peroxisome proliferator-activated receptor gamma-dependent pathway and substrate-dependent ubiquitination. An alternate mechanism is utilized for truncated selenoproteins, in which cullin-RING E3 ubiquitin ligase 2 targets the defective proteins for ubiquitin-proteasomal degradation. Selenoproteins, particularly SELENOP, may have their Sec residues reutilized for new selenoprotein synthesis via Sec decomposition. This review will explore these aspects in selenium biology, providing insights to knowledge gaps that remain to be uncovered.

Indexed as

ProteolysisAnimalsHumansIntestinal MucosaLiverProteasome Endopeptidase ComplexSeleniumSelenoprotein PProteasome Endopeptidase ComplexSeleniumSELENOP protein, humanSelenoprotein PDegradationSeleniumSelenocysteineSelenoproteinUbiquitination

Identifiers

PMID31222623
PMCPMC6801053
OpenAlexW2953331693

What OpenQuestion holds

Textmetadata
LicenceTDM
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.