Evidence map›Paper›PMID 22953757›Full record

ArticleThe journal of physical chemistry. B2012

High-resolution structural insights into bone: a solid-state NMR relaxation study utilizing paramagnetic doping.

Kamal H Mroue, Neil MacKinnon, Jiadi Xu, Peizhi Zhu, Erin McNerny, David H Kohn, Michael D Morris, Ayyalusamy Ramamoorthy

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 55 citations in OpenAlex.

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  7. Design Parameters of Tissue-Engineering Scaffolds at the Atomic Scale.Angewandte Chemie (International ed. in English) · 2019
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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

8 authors at 1 institution in 1 country.

Kamal H MroueBiophysics, The University of Michigan, Ann Arbor, Michigan 48109-1055, USA.
Neil MacKinnon
Jiadi Xu
Peizhi Zhu
Erin McNerny
David H Kohn
Michael D Morris
Ayyalusamy Ramamoorthy
University of Michigan–Ann Arbor · US

Funding

Cellular Biotechnology Training Program (CBTP)T32GM008353 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHWENDEMAN, ANNA · 1991 to 2021
$9.3M
Dynamic Spectroscopic Imaging in Bone BiomechanicsR01AR052010 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MORRIS, MICHAEL DAVID · 2005 to 2015
$3.7M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
Chemical Structure Effects on Bone Response to Mechanical LoadR01AR056657 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MORRIS, MICHAEL DAVID · 2010 to 2014
$1.6M
Purchase of a 500 MHz Solid State NMR SpectrometerS10RR023597 · NCRR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2007 to 2007
$500k
NCRR NIH HHS RR023597NCRR NIH HHS S10 RR023597NIAMS NIH HHS AR052010NIAMS NIH HHS AR056657NIAMS NIH HHS R01 AR052010NIAMS NIH HHS R01 AR056657NIGMS NIH HHS T32 GM008353NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

The hierarchical heterogeneous architecture of bone imposes significant challenges to structural and dynamic studies conducted by traditional biophysical techniques. High-resolution solid-state nuclear magnetic resonance (SSNMR) spectroscopy is capable of providing detailed atomic-level structural insights into such traditionally challenging materials. However, the relatively long data-collection time necessary to achieve a reliable signal-to-noise ratio (S/N) remains a major limitation for the widespread application of SSNMR on bone and related biomaterials. In this study, we attempt to overcome this limitation by employing the paramagnetic relaxation properties of copper(II) ions to shorten the (1)H intrinsic spin-lattice (T(1)) relaxation times measured in natural-abundance (13)C cross-polarization (CP) magic-angle-spinning (MAS) NMR experiments on bone tissues for the purpose of accelerating the data acquisition time in SSNMR. To this end, high-resolution solid-state (13)C CPMAS experiments were conducted on type I collagen (bovine tendon), bovine cortical bone, and demineralized bovine cortical bone, each in powdered form, to measure the (1)H T(1) values in the absence and in the presence of 30 mM Cu(II)(NH(4))(2)EDTA. Our results show that the (1)H T(1) values were successfully reduced by a factor of 2.2, 2.9, and 3.2 for bovine cortical bone, type I collagen, and demineralized bone, respectively, without reducing the spectral resolution and thus enabling faster data acquisition. In addition, paramagnetic quenching of particular (13)C NMR resonances on exposure to Cu(2+) ions in the absence of mineral was also observed, potentially suggesting the relative proximity of three main amino acids in the protein backbone (glycine, proline, and alanine) to the bone mineral surface.

Indexed as

Amino AcidsAnimalsBone and BonesCattleCollagen Type ICopperMagnetic Resonance SpectroscopyMolecular StructureOrganometallic CompoundsReference StandardsAmino AcidsCollagen Type ICopperOrganometallic Compounds

Identifiers

PMID22953757
PMCPMC3460063
OpenAlexW1998346337

What OpenQuestion holds

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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.