Evidence map›Paper›PMID 29439465›Full record

ArticleInternational journal of molecular sciences2018

Impact of Arginine to Cysteine Mutations in Collagen II on Protein Secretion and Cell Survival.

Salin A Chakkalakal, Juliane Heilig, Ulrich Baumann, Mats Paulsson, Frank Zaucke

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2018. 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
1.6field-weighted citation impact, top 15% 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, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Genetic Disorders of the Extracellular Matrix.Anatomical record (Hoboken, N.J. : 2007) · 2020
    Review
  11. Extracellular Matrix in Development and Disease.International journal of molecular sciences · 2019
    Article
  12. 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.

Salin A ChakkalakalCenter for Research in FOP and Related Disorders, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. salin.chakkalakal@gmail.com.ORCID 0000-0002-9014-0896
Juliane HeiligCenter for Biochemistry, Medical Faculty, University of Cologne, 50931 Cologne, Germany. juliane.heilig@uni-koeln.de.
Ulrich BaumannInstitute of Biochemistry, University of Cologne, 50931 Cologne, Germany. ubaumann@uni-koeln.de.
Mats PaulssonCenter for Biochemistry, Medical Faculty, University of Cologne, 50931 Cologne, Germany. mats.paulsson@uni-koeln.de.
Frank ZauckeCenter for Biochemistry, Medical Faculty, University of Cologne, 50931 Cologne, Germany. frank.zaucke@friedrichsheim.de.ORCID 0000-0002-7680-9354
University of Cologne · DEUniversity of Pennsylvania · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inherited point mutations in collagen II in humans affecting mainly cartilage are broadly classified as chondrodysplasias. Most mutations occur in the glycine (Gly) of the Gly-X-Y repeats leading to destabilization of the triple helix. Arginine to cysteine substitutions that occur at either the X or Y position within the Gly-X-Y cause different phenotypes like Stickler syndrome and congenital spondyloepiphyseal dysplasia (SEDC). We investigated the consequences of arginine to cysteine substitutions (X or Y position within the Gly-X-Y) towards the N and C terminus of the triple helix. Protein expression and its secretion trafficking were analyzed. Substitutions R75C, R134C and R704C did not alter the thermal stability with respect to wild type; R740C and R789C proteins displayed significantly reduced melting temperatures (T

Indexed as

Amino Acid SubstitutionUnfolded Protein ResponseCell Line, TumorCell SurvivalCollagen Type IIHEK293 CellsHumansOsteochondrodysplasiasProtein DenaturationProtein DomainsProtein StabilityProtein TransportCollagen Type IIchondrodysplasiacollagen IImutationtriple helixunfolded protein response

Identifiers

PMID29439465
PMCPMC5855763
OpenAlexW2793283600

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.