Evidence map›Paper›PMID 26851678›Full record

ReviewMatrix biology : journal of the International Society for Matrix Biology

SPARC/osteonectin in mineralized tissue.

Emilie M Rosset, Amy D Bradshaw

Open access · greenAbstract readReview
In one paragraph

Review in Matrix biology : journal of the International Society for Matrix Biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
166citing papers in PubMed, 1 pooled it
18.0field-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

166 citing papers in PubMed, 1 synthesis or guideline pooled it, 308 citations in OpenAlex.

  1. Pooled it
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  19. Novel SNP Combination for Predictive Osteoporotic Diagnosis.International journal of molecular sciences · 2025
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106 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

2 authors at 2 institutions in 1 country.

Emilie M RossetDepartment of Oral Health Sciences, College of Dental Medicine, Medical University of South Carolina, Charleston, SC, United States.
Amy D BradshawDepartment of Oral Health Sciences, College of Dental Medicine, Medical University of South Carolina, Charleston, SC, United States; Department of Medicine, Division of Cardiology, Medical University of South Carolina, Charleston, SC, United States; Ralph H. Johnson Veterans Administration, VA Medical Center, Charleston, SC, United States.
Medical University of South Carolina · USRalph H. Johnson VA Medical Center · US

Funding

T-COHR: Training in Craniofacial and Oral Health ResearchT32DE017551 · NIDCR · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI YAO, HAI · 2006 to 2025
$10.3M
Pilot and Feasibility Project ProgramP30GM103331 · NIGMS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI KIRKWOOD, KEITH L · 2012 to 2016
$5.2M
Procollagen Binding Proteins in Age-Dependent LV RemodelingI01BX001385 · VA · RALPH H JOHNSON VA MEDICAL CENTER · PI BRADSHAW, AMY D · 2012 to 2015
–
BLRD VA I01 BX001385NIDCR NIH HHS T32 DE017551NIGMS NIH HHS P30 GM103331
6 · The paper itself

Abstract

Secreted protein acidic and rich in cysteine (SPARC/osteonectin/BM40) is one of the most abundant non-collagenous protein expressed in mineralized tissues. This review will focus on elucidating functional roles of SPARC in bone formation building upon results from non-mineralized cells and tissues, the phenotype of SPARC-null bones, and recent discoveries of human diseases with either dysregulated expression of SPARC or mutations in the gene encoding SPARC that give rise to bone pathologies. The capacity of SPARC to influence pathways involved in extracellular matrix assembly such as procollagen processing and collagen fibril formation as well as the capacity to influence osteoblast differentiation and osteoclast activity will be addressed. In addition, the potential for SPARC to regulate cross-linking of extracellular matrix proteins by members of the transglutaminase family of enzymes is explored. Elucidating defined biological functions of SPARC in terms of bone formation and turnover are critical. Further insight into specific cellular mechanisms involved in the formation and homeostasis of mineralized tissues will lead to a better understanding of disease progression.

Indexed as

Calcification, PhysiologicAnimalsBone and BonesCell DifferentiationExtracellular MatrixGene Expression RegulationHumansMutationOsteoblastsOsteoclastsOsteogenesis ImperfectaOsteonectinOsteoporosisTransglutaminasesOsteonectinSPARC protein, humanTransglutaminasesCollagenMatricellularMineralOsteoblastOsteoclast

Identifiers

PMID26851678
PMCPMC5327628
OpenAlexW2288411839

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.