Evidence map›Paper›PMID 31023093›Full record

ReviewCritical reviews in biochemistry and molecular biology2019

TPR-containing proteins control protein organization and homeostasis for the endoplasmic reticulum.

Jill B Graham, Nathan P Canniff, Daniel N Hebert

Abstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Article
  2. ScRNA-seq Data Reveal Gene Upregulation and Downregulation in Oxygen-Induced Retinopathy.Medical science monitor : international medical journal of experimental and clinical research · 2026
    Article
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  13. Review
  14. High expression ofTranslational cancer research · 2022
    Article
  15. Article
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  17. Article
  18. Article
  19. Article
  20. Dnj1 Promotes Virulence inFrontiers in microbiology · 2021
    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

3 authors.

Jill B Grahama Molecular Cellular Biology Program , University of Massachusetts , Amherst , MA , USA.
Nathan P Canniffa Molecular Cellular Biology Program , University of Massachusetts , Amherst , MA , USA.
Daniel N Heberta Molecular Cellular Biology Program , University of Massachusetts , Amherst , MA , USA.

Funding

Cellular protein maturation and degradationR01GM086874 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI RAUCH, JENNIFER NICOLE · 2009 to 2025
$4.5M
CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
NIGMS NIH HHS R01 GM086874NIGMS NIH HHS T32 GM008515
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is a complex, multifunctional organelle comprised of a continuous membrane and lumen that is organized into a number of functional regions. It plays various roles including protein translocation, folding, quality control, secretion, calcium signaling, and lipid biogenesis. Cellular protein homeostasis is maintained by a complicated chaperone network, and the largest functional family within this network consists of proteins containing tetratricopeptide repeats (TPRs). TPRs are well-studied structural motifs that mediate intermolecular protein-protein interactions, supporting interactions with a wide range of ligands or substrates. Seven TPR-containing proteins have thus far been shown to localize to the ER and control protein organization and homeostasis within this multifunctional organelle. Here, we discuss the roles of these proteins in controlling ER processes and organization. The crucial roles that TPR-containing proteins play in the ER are highlighted by diseases or defects associated with their mutation or disruption.

Indexed as

ProteostasisTetratricopeptide RepeatAnimalsCalciumEndoplasmic ReticulumHumansModels, MolecularMolecular ChaperonesProtein Interaction MapsProteinsProtein TransportCalciumMolecular ChaperonesProteinschaperonesEndoplasmic reticulumglycosylationprotein translocationTPR domains

Identifiers

PMID31023093
PMCPMC6816462

What OpenQuestion holds

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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.