Evidence map›Paper›PMID 25960419›Full record

ReviewMatrix biology : journal of the International Society for Matrix Biology2015

Latent TGF-β-binding proteins.

Ian B Robertson, Masahito Horiguchi, Lior Zilberberg, Branka Dabovic, Krassimira Hadjiolova, Daniel B Rifkin

Open access · hybridAbstract readReview
In one paragraph

Review in Matrix biology : journal of the International Society for Matrix Biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 299 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
299citing papers in PubMed, 2 pooled it
24.0field-weighted citation impact, top 1% 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

299 citing papers in PubMed, 2 syntheses or guidelines pooled it, 439 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Review
  4. Article
  5. Article
  6. Regulators of ECM structure enable functional adaptation to tensile loading in tendon explants.Matrix biology : journal of the International Society for Matrix Biology · 2026
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  15. [Integrating Bioinformatics and Machine Learning Algorithms to Screen Inflammatory Biomarkers for Atrial Fibrillation and Experimental Validation].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2026
    Article
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239 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Ian B RobertsonThe Department of Cell Biology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA.
Masahito HoriguchiThe Department of Cell Biology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA.
Lior ZilberbergThe Department of Cell Biology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA.
Branka DabovicThe Department of Cell Biology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA.
Krassimira HadjiolovaThe Department of Cell Biology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA.
Daniel B RifkinThe Department of Cell Biology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA. Electronic address: daniel.rifkin@nyumc.org.
New York University · US

Funding

PROJECT 4: Exploration of Therapeutic Strategies in MarP01AR049698 · NIAMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI RAMIREZ, FRANCESCO B · 2004 to 2014
$13.9M
Regulation of TGF-Beta Activity in the Lung by LTBP-4R01CA034282 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI RIFKIN, DANIEL B · 1985 to 2016
$5.8M
NCI NIH HHS R01 CA034282NIAMS NIH HHS P01 AR049698NIAMS NIH HHS P01 AR49698
6 · The paper itself

Abstract

The LTBPs (or latent transforming growth factor β binding proteins) are important components of the extracellular matrix (ECM) that interact with fibrillin microfibrils and have a number of different roles in microfibril biology. There are four LTBPs isoforms in the human genome (LTBP-1, -2, -3, and -4), all of which appear to associate with fibrillin and the biology of each isoform is reviewed here. The LTBPs were first identified as forming latent complexes with TGFβ by covalently binding the TGFβ propeptide (LAP) via disulfide bonds in the endoplasmic reticulum. LAP in turn is cleaved from the mature TGFβ precursor in the trans-golgi network but LAP and TGFβ remain strongly bound through non-covalent interactions. LAP, TGFβ, and LTBP together form the large latent complex (LLC). LTBPs were originally thought to primarily play a role in maintaining TGFβ latency and targeting the latent growth factor to the extracellular matrix (ECM), but it has also been shown that LTBP-1 participates in TGFβ activation by integrins and may also regulate activation by proteases and other factors. LTBP-3 appears to have a role in skeletal formation including tooth development. As well as having important functions in TGFβ regulation, TGFβ-independent activities have recently been identified for LTBP-2 and LTBP-4 in stabilizing microfibril bundles and regulating elastic fiber assembly.

Indexed as

AnimalsExtracellular MatrixFibrillinsHumansLatent TGF-beta Binding ProteinsMicrofilament ProteinsProtein IsoformsSignal TransductionTransforming Growth Factor betaFibrillinsLatent TGF-beta Binding ProteinsMicrofilament ProteinsProtein IsoformsTransforming Growth Factor betaExtracellular matrixLatency associated proteinLatent TGFβ binding proteinsTGFβ activation

Identifiers

PMID25960419
PMCPMC4844006
OpenAlexW228843169

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.