Evidence map›Paper›PMID 24609034›Full record

ReviewDisease models & mechanisms2014

Glycoprotein folding and quality-control mechanisms in protein-folding diseases.

Sean P Ferris, Vamsi K Kodali, Randal J Kaufman

Open access · goldAbstract readReview
In one paragraph

Review in Disease models & mechanisms, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

46 citing papers in PubMed, 89 citations in OpenAlex.

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  7. Deciphering the determinants of recombinant protein expression across the human secretome.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  20. Collagen's enigmatic, highly conservedProceedings of the National Academy of Sciences of the United States of America · 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 at 2 institutions in 1 country.

Sean P FerrisDepartment of Biological Chemistry and Medical Scientist Training Program, University of Michigan, Ann Arbor, MI 48109, USA.
Vamsi K Kodali
Randal J Kaufman
Sanford Burnham Prebys Medical Discovery Institute · USUniversity of Michigan–Ann Arbor · US

Funding

TRANSGENIC MODELS FOR THE STUDY OF FACTOR V FUNCTIONP01HL057346 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KAUFMAN, RANDAL J. · 1997 to 2013
$19.9M
PREDOCTORAL TRAINING IN GENETICST32GM007544 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MORAN, JOHN V. · 1985 to 2022
$11.3M
Regulation of Factor VIII SecretionR01HL052173 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KAUFMAN, RANDAL J. · 1995 to 2014
$6.5M
Role of the Unfolded Protein Response in Beta CellR37DK042394 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KAUFMAN, RANDAL J. · 2007 to 2016
$4.9M
Regulation of ER stress-induced cell deathR01DK088227 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KAUFMAN, RANDAL J. · 2010 to 2014
$3.1M
Unfolded Protein Response in Glucose HomeostasisR01DK042394 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KAUFMAN, RANDAL J. · 2003 to 2006
$1.2M
NHLBI NIH HHS HL052173NHLBI NIH HHS HL057346NHLBI NIH HHS P01 HL057346NHLBI NIH HHS R01 HL052173NIDDK NIH HHS DK042394NIDDK NIH HHS DK088227NIDDK NIH HHS R01 DK042394NIDDK NIH HHS R01 DK088227NIDDK NIH HHS R37 DK042394NIGMS NIH HHS T32 GM007544
6 · The paper itself

Abstract

Biosynthesis of proteins--from translation to folding to export--encompasses a complex set of events that are exquisitely regulated and scrutinized to ensure the functional quality of the end products. Cells have evolved to capitalize on multiple post-translational modifications in addition to primary structure to indicate the folding status of nascent polypeptides to the chaperones and other proteins that assist in their folding and export. These modifications can also, in the case of irreversibly misfolded candidates, signal the need for dislocation and degradation. The current Review focuses on the glycoprotein quality-control (GQC) system that utilizes protein N-glycosylation and N-glycan trimming to direct nascent glycopolypeptides through the folding, export and dislocation pathways in the endoplasmic reticulum (ER). A diverse set of pathological conditions rooted in defective as well as over-vigilant ER quality-control systems have been identified, underlining its importance in human health and disease. We describe the GQC pathways and highlight disease and animal models that have been instrumental in clarifying our current understanding of these processes.

Indexed as

Protein FoldingAnimalsEndoplasmic ReticulumGlycoproteinsGlycosylationHumansProteolysisProteostasis DeficienciesGlycoproteinsER-associated degradationER exportER quality controlGlycoprotein foldingN-glycosylation

Identifiers

PMID24609034
PMCPMC3944493
OpenAlexW2136171593

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.