Evidence map›Paper›PMID 12820886›Full record

ArticleBiochemistry2003

The three-dimensional structure of bovine calcium ion-bound osteocalcin using 1H NMR spectroscopy.

T L Dowd, J F Rosen, L Li, C M Gundberg

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 1 pooled it
1.7field-weighted citation impact, top 17% 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

33 citing papers in PubMed, 1 synthesis or guideline pooled it, 78 citations in OpenAlex.

  1. Pooled it
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  10. Growth Factor Engineering Strategies for Regenerative Medicine Applications.Frontiers in bioengineering and biotechnology · 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

4 authors at 3 institutions in 1 country.

T L DowdDepartment of Pediatrics, Montefiore Medical Center, Albert Einstein College of Medicine, Bronx, New York 10467, USA. dowd@aecom.yu.edu
J F Rosen
L Li
C M Gundberg
Montefiore Medical Center · USNational Institute of Environmental Health Sciences · USYale University · US

Funding

OSTEOCALCIN SYNTHESIS AND CATABOLISM IN VIVO AND IN VITRR01AR038460 · NIAMS · YALE UNIVERSITY · PI GUNDBERG, CAREN · 1986 to 2007
$2.5M
Effect of Pb2+ Toxicity at the Molecular LevelR01ES009032 · NIEHS · MONTEFIORE MEDICAL CENTER (BRONX, NY) · PI DOWD, TERRY LYNNE · 2005 to 2009
$1.0M
NOT STATEDR29ES009032 · NIEHS · MONTEFIORE MEDICAL CENTER (BRONX, NY) · PI DOWD, TERRY L · 1997 to 2001
$190k
ENVIRONMENTAL POLYCYCLICS: METABOLISM AND ACTIVATIONR01ES002030 · NIEHS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI LAVOIE, EDMOND J · 1985 to 1988
–
ENVIRONMENTAL POLYCYCLICS: METABOLISM AND ACTIVATIONR37ES002030 · NIEHS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI LAVOIE, EDMOND J · 1988 to 1997
–
NIAMS NIH HHS AR-38460NIAMS NIH HHS R01 AR038460NIEHS NIH HHS ES-02030NIEHS NIH HHS R01 ES009032NIEHS NIH HHS R29 ES009032
6 · The paper itself

Abstract

Structural information on osteocalcin or other noncollagenous bone proteins is very limited. We have solved the three-dimensional structure of calcium bound osteocalcin using (1)H 2D NMR techniques and proposed a mechanism for mineral binding. The protons in the 49 amino acid sequence were assigned using standard two-dimensional homonuclear NMR experiments. Distance constraints, dihedral angle constraints, hydrogen bonds, and (1)H and (13)C chemical shifts were all used to calculate a family of 13 structures. The tertiary structure of the protein consisted of an unstructured N terminus and a C-terminal loop (residues 16-49) formed by long-range hydrophobic interactions. Elements of secondary structure within residues 16-49 include type III turns (residues 20-25) and two alpha-helical regions (residues 27-35 and 41-44). The three Gla residues project from the same face of the helical turns and are surface exposed. The genetic algorithm-molecular dynamics simulation approach was used to place three calcium atoms on the NMR-derived structure. One calcium atom was coordinated by three side chain oxygen atoms, two from Asp30, and one from Gla24. The second calcium atom was coordinated to four oxygen atoms, two from the side chain in Gla 24, and two from the side chain of Gla 21. The third calcium atom was coordinated to two oxygen atoms of the side chain of Gla17. The best correlation of the distances between the uncoordinated Gla oxygen atoms is with the intercalcium distance of 9.43 A in hydroxyapatite. The structure may provide further insight into the function of osteocalcin.

Indexed as

AnimalsCalciumCattleMagnetic Resonance SpectroscopyOsteocalcinProtein BindingCalciumOsteocalcin

Identifiers

PMID12820886
PMCPMC4517610
OpenAlexW2006538880

What OpenQuestion holds

Textmetadata
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.