Evidence map›Paper›PMID 23953737›Full record

ReviewDental materials : official publication of the Academy of Dental Materials2013

Strategies to prevent hydrolytic degradation of the hybrid layer-A review.

Leo Tjäderhane, Fabio D Nascimento, Lorenzo Breschi, Annalisa Mazzoni, Ivarne L S Tersariol, Saulo Geraldeli, Arzu Tezvergil-Mutluay, Marcela Carrilho, Ricardo M Carvalho, Franklin R Tay and 1 more

Open access · greenAbstract readReview
In one paragraph

Review in Dental materials : official publication of the Academy of Dental Materials, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers, 8 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
129citing papers in PubMed, 8 pooled it
26.8field-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

129 citing papers in PubMed, 8 syntheses or guidelines pooled it, 405 citations in OpenAlex.

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  15. Preparation and Structural Evolution of ZrBMaterials (Basel, Switzerland) · 2026
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69 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

11 authors at 8 institutions in 6 countries.

Leo TjäderhaneInstitute of Dentistry, University of Oulu/Oulu University Hospital, Oulu, Finland; Institute of Dentistry, University of Turku, Turku, Finland; The NordicInstitute of Dental Materials (NIOM), Oslo, Norway. Electronic address: leo.tjaderhane@oulu.fi.
Fabio D Nascimento
Lorenzo Breschi
Annalisa Mazzoni
Ivarne L S Tersariol
Saulo Geraldeli
Arzu Tezvergil-Mutluay
Marcela Carrilho
Ricardo M Carvalho
Franklin R Tay
David H Pashley
Augusta University · USUniversity of Trieste · ITUniversidade de Mogi das Cruzes · BRUniversity of British Columbia · CAUniversity of Florida · USUniversity of Oulu · FIUniversity of Turku · FIWestern University · CA

Funding

Reasons for poor durability of resin-dentin bondsR01DE015306 · NIDCR · MEDICAL COLLEGE OF GEORGIA (MCG) · PI PASHLEY, DAVID H · 2004 to 2013
$4.4M
NIDCR NIH HHS DE 015306NIDCR NIH HHS R01 DE015306
6 · The paper itself

Abstract

objectiveEndogenous dentin collagenolytic enzymes, matrix metalloproteinases (MMPs) and cysteine cathepsins, are responsible for the time-dependent hydrolysis of collagen matrix of hybrid layers. As collagen matrix integrity is essential for the preservation of long-term dentin bond strength, inhibition of endogenous dentin proteases is necessary for durable resin-bonded restorations.

methodsSeveral tentative approaches to prevent enzyme function have been proposed. Some of them have already demonstrated clinical efficacy, while others need to be researched further before clinical protocols can be proposed. This review will examine both the principles and outcomes of techniques to prevent collagen hydrolysis in dentin-resin interfaces.

resultsChlorhexidine, a general inhibitor of MMPs and cysteine cathepsins, is the most tested method. In general, these experiments have shown that enzyme inhibition is a promising approach to improve hybrid layer preservation and bond strength durability. Other enzyme inhibitors, e.g. enzyme-inhibiting monomers, may be considered promising alternatives that would allow more simple clinical application than chlorhexidine. Cross-linking collagen and/or dentin matrix-bound enzymes could render hybrid layer organic matrices resistant to degradation. Alternatively, complete removal of water from the hybrid layer with ethanol wet bonding or biomimetic remineralization should eliminate hydrolysis of both collagen and resin components. SIGNIFICANCE: Understanding the function of the enzymes responsible for the hydrolysis of hybrid layer collagen has prompted several innovative approaches to retain hybrid layer integrity and strong dentin bonding. The ultimate goal, prevention of collagen matrix degradation with clinically applicable techniques and commercially available materials may be achievable in several ways.

Indexed as

CathepsinsCollagenHydrolysisMatrix MetalloproteinasesMicroscopy, Electron, ScanningMicroscopy, Electron, TransmissionProtease InhibitorsCathepsinsCollagenMatrix MetalloproteinasesProtease InhibitorsChlorhexidineCysteine cathepsinsDegradationDentin bondingDurabilityEnzyme inhibitionEnzymesHybrid layerMatrix metalloproteinasesReview

Identifiers

PMID23953737
PMCPMC3899917
OpenAlexW2091132707

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.