Evidence map›Paper›PMID 31947880›Full record

ReviewBiomolecules2020

From Translation to Protein Degradation as Mechanisms for Regulating Biological Functions: A Review on the SLRP Family in Skeletal Tissues.

Jérémie Zappia, Marc Joiret, Christelle Sanchez, Cécile Lambert, Liesbet Geris, Marc Muller, Yves Henrotin

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2020. 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
1.3field-weighted citation impact, top 17% 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, 19 citations in OpenAlex.

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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

7 authors at 1 institution in 1 country.

Jérémie ZappiaBone and Cartilage Research Unit, Arthropôle Liège, Center for Interdisciplinary research on Medicines (CIRM) Liège, Liège University, Institute of Pathology, CHU Sart-Tilman, 4000 Liège, Belgium.
Marc JoiretBiomechanics Research Unit, B34 GIGA-R, In Silico Medicine, Liège University, CHU Sart-Tilman, 4000 Liège, Belgium.
Christelle SanchezBone and Cartilage Research Unit, Arthropôle Liège, Center for Interdisciplinary research on Medicines (CIRM) Liège, Liège University, Institute of Pathology, CHU Sart-Tilman, 4000 Liège, Belgium.
Cécile LambertBone and Cartilage Research Unit, Arthropôle Liège, Center for Interdisciplinary research on Medicines (CIRM) Liège, Liège University, Institute of Pathology, CHU Sart-Tilman, 4000 Liège, Belgium.
Liesbet GerisBiomechanics Research Unit, B34 GIGA-R, In Silico Medicine, Liège University, CHU Sart-Tilman, 4000 Liège, Belgium.
Marc MullerLaboratory for Organogenesis and Regeneration (LOR), GIGA-Research, Liège University, Avenue de l'Hôpital, B-4000 Liège, Belgium.
Yves HenrotinBone and Cartilage Research Unit, Arthropôle Liège, Center for Interdisciplinary research on Medicines (CIRM) Liège, Liège University, Institute of Pathology, CHU Sart-Tilman, 4000 Liège, Belgium.
University of Liège · BE

Funding

Fonds De La Recherche Scientifique - FNRS 30480119
6 · The paper itself

Abstract

The extracellular matrix can trigger cellular responses through its composition and structure. Major extracellular matrix components are the proteoglycans, which are composed of a core protein associated with glycosaminoglycans, among which the small leucine-rich proteoglycans (SLRPs) are the largest family. This review highlights how the codon usage pattern can be used to modulate cellular response and discusses the biological impact of post-translational events on SLRPs, including the substitution of glycosaminoglycan moieties, glycosylation, and degradation. These modifications are listed, and their impacts on the biological activities and structural properties of SLRPs are described. We narrowed the topic to skeletal tissues undergoing dynamic remodeling.

Indexed as

AnimalsCodon UsageExtracellular MatrixExtracellular Matrix ProteinsGlycosaminoglycansHumansLeucineMuscle, SkeletalProtein Processing, Post-TranslationalProteoglycansProteolysisSmall Leucine-Rich ProteoglycansExtracellular Matrix ProteinsGlycosaminoglycansLeucineProteoglycansSmall Leucine-Rich Proteoglycanscatabolismcodon usageglycosaminoglycanglycosylationpost-translational eventsmall leucine-rich proteoglycans

Identifiers

PMID31947880
PMCPMC7023458
OpenAlexW2998095523

What Socratic 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 Socratic graph.