Evidence map›Paper›PMID 26177309›Full record

ReviewBiochemistry2015

Decoding the Matrix: Instructive Roles of Proteoglycan Receptors.

Thomas Neill, Liliana Schaefer, Renato V Iozzo

Open access · greenAbstract readReview
In one paragraph

Review in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed, 1 pooled it
7.2field-weighted citation impact, top 2% 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

84 citing papers in PubMed, 1 synthesis or guideline pooled it, 125 citations in OpenAlex.

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24 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

3 authors at 3 institutions in 2 countries.

Thomas Neill†Department of Pathology, Anatomy and Cell Biology and Cancer Cell Biology and Signaling Program, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, United States.
Liliana Schaefer‡Department of Pharmacology, Goethe University, 60590 Frankfurt, Germany.
Renato V Iozzo†Department of Pathology, Anatomy and Cell Biology and Cancer Cell Biology and Signaling Program, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, United States.
Goethe University Frankfurt · DESidney Kimmel Cancer Center · USThomas Jefferson University · US

Funding

NEOPLASTIC MODULATION OF PROTEOGLYCAN METABOLISMR01CA039481 · NCI · UNIVERSITY OF PENNSYLVANIA · PI IOZZO, RENATO V. · 1985 to 2020
$7.1M
The Biology of Perlecan in Cancer and AngiogenesisR01CA047282 · NCI · THOMAS JEFFERSON UNIVERSITY · PI IOZZO, RENATO V. · 1990 to 2019
$5.7M
Progranulin signaling in bladder cancerR01CA164462 · NCI · THOMAS JEFFERSON UNIVERSITY · PI IOZZO, RENATO V., MORRIONE, ANDREA · 2012 to 2016
$1.6M
Natural EGFR Antagonists and CancerR01CA120975 · NCI · THOMAS JEFFERSON UNIVERSITY · PI IOZZO, RENATO V. · 2007 to 2010
$942k
NCI NIH HHS R01 CA039481NCI NIH HHS R01 CA047282NCI NIH HHS R01 CA120975NCI NIH HHS R01 CA164462NCI NIH HHS R01 CA39481NCI NIH HHS R01 CA47282
6 · The paper itself

Abstract

The extracellular matrix is a dynamic repository harboring instructive cues that embody substantial regulatory dominance over many evolutionarily conserved intracellular activities, including proliferation, apoptosis, migration, motility, and autophagy. The matrix also coordinates and parses hierarchical information, such as angiogenesis, tumorigenesis, and immunological responses, typically providing the critical determinants driving each outcome. We provide the first comprehensive review focused on proteoglycan receptors, that is, signaling transmembrane proteins that use secreted proteoglycans as ligands, in addition to their natural ligands. The majority of these receptors belong to an exclusive subset of receptor tyrosine kinases and assorted cell surface receptors that specifically bind, transduce, and modulate fundamental cellular processes following interactions with proteoglycans. The class of small leucine-rich proteoglycans is the most studied so far and constitutes the best understood example of proteoglycan-receptor interactions. Decorin and biglycan evoke autophagy and immunological responses that deter, suppress, or exacerbate pathological conditions such as tumorigenesis, angiogenesis, and chronic inflammatory disease. Basement membrane-associated heparan sulfate proteoglycans (perlecan, agrin, and collagen XVIII) represent a unique cohort and provide proteolytically cleaved bioactive fragments for modulating cellular behavior. The receptors that bind the genuinely multifactorial and multivalent proteoglycans represent a nexus in understanding basic biological pathways and open new avenues for therapeutic and pharmacological intervention.

Indexed as

Extracellular MatrixExtracellular Matrix ProteinsProteoglycansReceptors, Cell SurfaceAnimalsAutophagyCell Transformation, NeoplasticHumansInflammationNeovascularization, PathologicSignal TransductionExtracellular Matrix ProteinsProteoglycansReceptors, Cell Surface

Identifiers

PMID26177309
PMCPMC4859759
OpenAlexW2418536297

What OpenQuestion holds

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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.