Evidence map›Paper›PMID 32875613›Full record

ReviewDevelopmental dynamics : an official publication of the American Association of Anatomists2021

The quest for substrates and binding partners: A critical barrier for understanding the role of ADAMTS proteases in musculoskeletal development and disease.

Brandon Satz-Jacobowitz, Dirk Hubmacher

Open access · greenAbstract readReview
In one paragraph

Review in Developmental dynamics : an official publication of the American Association of Anatomists, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 14% 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

9 citing papers in PubMed, 1 synthesis or guideline pooled it, 19 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. O-fucosylation of thrombospondin type 1 repeats is essential for ECM remodeling and signaling during bone development.Matrix biology : journal of the International Society for Matrix Biology · 2022
    Article
  6. Metalloproteases in gonad formation and ovulation.General and comparative endocrinology · 2021
    Review
  7. Review
  8. Alternative splicing of the metalloprotease ADAMTS17 spacer regulates secretion and modulates autoproteolytic activity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  9. Regulation of ADAMTS Proteases.Frontiers in molecular biosciences · 2021
    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.

Brandon Satz-JacobowitzOrthopedic Research Laboratories, Leni & Peter W. May Department of Orthopedics, Icahn School of Medicine at Mount Sinai, New York, New York, USA.
Dirk HubmacherOrthopedic Research Laboratories, Leni & Peter W. May Department of Orthopedics, Icahn School of Medicine at Mount Sinai, New York, New York, USA.ORCID 0000-0003-1569-9451
Icahn School of Medicine at Mount Sinai · US

Funding

Regulation of Skeletal Growth by Soft Tissue Extracellular MatrixR01AR070748 · NIAMS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI HUBMACHER, DIRK · 2017 to 2021
$1.9M
Ines Mandl Research FoundationLeni & Peter W. May Department for OrthopaedicsNIAMS NIH HHS R01 AR070748
6 · The paper itself

Abstract

Secreted ADAMTS metalloproteases are involved in the sculpting, remodeling, and erosion of connective tissues throughout the body, including in the musculoskeletal system. ADAMTS proteases contribute to musculoskeletal development, pathological tissue destruction, and are mutated in congenital musculoskeletal disorders. Examples include versican cleavage by ADAMTS9 which is required for interdigital web regression during limb development, ADAMTS5-mediated aggrecan degradation in osteoarthritis resulting in joint erosion, and mutations in ADAMTS10 or ADAMTS17 that cause Weill-Marchesani syndrome, a short stature syndrome with bone, joint, muscle, cardiac, and eye involvement. Since the function of ADAMTS proteases and proteases in general is primarily defined by the molecular consequences of proteolysis of their respective substrates, it is paramount to identify all physiological substrates for each individual ADAMTS protease. Here, we review the current knowledge of ADAMTS proteases and their involvement in musculoskeletal development and disease, focusing on some of their known physiological substrates and the consequences of substrate cleavage. We further emphasize the critical need for the identification and validation of novel ADAMTS substrates and binding partners by describing the principles of mass spectrometry-based approaches and by emphasizing strategies that need to be considered for validating the physiological relevance for ADAMTS-mediated proteolysis of novel putative substrates.

Indexed as

Musculoskeletal DevelopmentADAMTS ProteinsAnimalsHumansMusculoskeletal DiseasesADAMTS ProteinsADAMTS-like proteinsconnective tissuedegradomicsextracellular matrixN-terminomicsprotease

Identifiers

PMID32875613
PMCPMC7902295
OpenAlexW3082513189

What OpenQuestion holds

Textmetadata
LicenceTDM
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.