Evidence map›Paper›PMID 25927841›Full record

ReviewJournal of translational medicine2015

Proteomic database mining opens up avenues utilizing extracellular protein phosphorylation for novel therapeutic applications.

Garif Yalak, Bjorn R Olsen

Open access · goldAbstract readReview
In one paragraph

Review in Journal of translational medicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
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  5. Article
  6. Around the collagen triple helix: an introduction to studying associated genetic and acquired diseases.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. The phosphorylation of serineMatrix biology : journal of the International Society for Matrix Biology · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Garif YalakDepartment of Developmental Biology, Harvard Medical School/Harvard School of Dental Medicine, 188 Longwood Avenue, Boston, MA, 02115, USA. garif_yalak@hms.harvard.edu.
Bjorn R OlsenDepartment of Developmental Biology, Harvard Medical School/Harvard School of Dental Medicine, 188 Longwood Avenue, Boston, MA, 02115, USA. bjorn_olsen@hms.harvard.edu.
Harvard University · US

Funding

STRUCTURE OF TYPE I AND TYPE II PROCOLLAGENSR01AR036819 · NIAMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI OLSEN, BJORN REINO · 1986 to 2016
$8.7M
NIAMS NIH HHS R01 AR036819
6 · The paper itself

Abstract

Recent advances in extracellular signaling suggest that extracellular protein phosphorylation is a regulatory mechanism outside the cell. The list of reported active extracellular protein kinases and phosphatases is growing, and phosphorylation of an increasing number of extracellular matrix molecules and extracellular domains of trans-membrane proteins is being documented. Here, we use public proteomic databases, collagens - the major components of the extracellular matrix, extracellular signaling molecules and proteolytic enzymes as examples to assess what the roles of extracellular protein phosphorylation may be in health and disease. We propose that novel tools be developed to help assess the role of extracellular protein phosphorylation and translate the findings for biomedical applications. Furthermore, we suggest that the phosphorylation state of extracellular matrix components as well as the presence of extracellular kinases be taken into account when designing translational medical applications.

Indexed as

Databases, ProteinData MiningProteomicsAmino Acid SequenceExtracellular SpaceHumansMolecular Sequence DataPhosphorylationProteinsProteins

Identifiers

PMID25927841
PMCPMC4427915
OpenAlexW2128261167

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.