Evidence map›Paper›PMID 27589372›Full record

ArticleBiomaterials2016

Studies of chain substitution caused sub-fibril level differences in stiffness and ultrastructure of wildtype and oim/oim collagen fibers using multifrequency-AFM and molecular modeling.

Tao Li, Shu-Wei Chang, Naiara Rodriguez-Florez, Markus J Buehler, Sandra Shefelbine, Ming Dao, Kaiyang Zeng

Open access · bronzeAbstract read
In one paragraph

Article in Biomaterials, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

12 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  10. Multiscale characterization of pathological bone tissue.Microscopy research and technique · 2022
    Article
  11. Intrafibrillar mineralization deficiency and osteogenesis imperfecta mouse bone fragility.Journal of the mechanical behavior of biomedical materials · 2021
    Article
  12. 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

7 authors at 5 institutions in 4 countries.

Tao LiDepartment of Mechanical Engineering, National University of Singapore, Singapore.
Shu-Wei ChangDepartment of Civil Engineering, National Taiwan University, Taipei 10617, Taiwan; Department of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA.
Naiara Rodriguez-FlorezDepartment of Bioengineering, Imperial College London, London SW7 2AZ, UK.
Markus J BuehlerDepartment of Civil and Environmental Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA.
Sandra ShefelbineDepartment of Mechanical and Industrial Engineering, Northeastern University, Boston, MA, USA. Electronic address: s.shefelbine@neu.edu.
Ming DaoDepartment of Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA. Electronic address: mingdao@mit.edu.
Kaiyang ZengDepartment of Mechanical Engineering, National University of Singapore, Singapore. Electronic address: mpezk@nus.edu.sg.
Massachusetts Institute of Technology · USNational University of Singapore · SGImperial College London · GBNational Taipei University of Technology · TWNortheastern University · US

Funding

Models to Predict Protein Biomaterial PerformanceU01EB014976 · NIBIB · TUFTS UNIVERSITY MEDFORD · PI BUEHLER, MARKUS J., KAPLAN, DAVID L. · 2012 to 2020
$5.2M
Cross-scale interactions between mineral and collagen for tendon-bone attachmentU01EB016422 · NIBIB · WASHINGTON UNIVERSITY · PI GENIN, GUY M, THOMOPOULOS, STAVROS · 2013 to 2017
$2.4M
NIBIB NIH HHS U01 EB014976NIBIB NIH HHS U01 EB016422
6 · The paper itself

Abstract

Molecular alteration in type I collagen, i.e., substituting the α2 chain with α1 chain in tropocollagen molecule, can cause osteogenesis imperfecta (OI), a brittle bone disease, which can be represented by a mouse model (oim/oim). In this work, we use dual-frequency Atomic Force Microscopy (AFM) and incorporated with molecular modeling to quantify the ultrastructure and stiffness of the individual native collagen fibers from wildtype (+/+) and oim/oim diseased mice humeri. Our work presents direct experimental evidences that the +/+ fibers have highly organized and compact ultrastructure and corresponding ordered stiffness distribution. In contrast, oim/oim fibers have ordered but loosely packed ultrastructure with uncorrelated stiffness distribution, as well as local defects. The molecular model also demonstrates the structural and molecular packing differences between +/+ and oim/oim collagens. The molecular mutation significantly altered sub-fibril structure and mechanical property of collagen fibers. This study can give the new insight for the mechanisms and treatment of the brittle bone disease.

Indexed as

Models, MolecularMolecular Dynamics SimulationAmino AcidsAmino Acid SubstitutionCollagen Type IElastic ModulusMicroscopy, Atomic ForceProtein ConformationProtein DomainsStress, MechanicalStructure-Activity RelationshipAmino AcidsCollagen Type IBoneCollagenDual-frequency AFMOimStiffness

Identifiers

PMID27589372
PMCPMC5040355
OpenAlexW2509008394

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.