Evidence map›Paper›PMID 29890074›Full record

ArticleBiochemistry2018

Biophysical Examination of the Calcium-Modulated Nickel-Binding Properties of Human Calprotectin Reveals Conformational Change in the EF-Hand Domains and His

Toshiki G Nakashige, Sarah E J Bowman, Emily M Zygiel, Catherine L Drennan, Elizabeth M Nolan

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  4. Spectroscopic and computational investigations of Cobalt(II) binding to the innate immune protein human calprotectin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
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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

5 authors at 2 institutions in 1 country.

Toshiki G Nakashige
Emily M Zygiel
Catherine L DrennanORCID 0000-0001-5486-2755
Elizabeth M NolanORCID 0000-0002-6153-8803
Massachusetts Institute of Technology · USHoward Hughes Medical Institute · US

Funding

TOXICOLOGY CORE UNITP30ES002109 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI FOX, JAMES G · 1985 to 2020
$25.6M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Complex Metallocluster Structure and AssemblyR01GM069857 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI DRENNAN, CATHERINE L · 2004 to 2017
$3.1M
Metallobiochemistry of innate immunity and bacterial physiologyR01GM126376 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI NOLAN, ELIZABETH M, OGLESBY, AMANDA GAIL · 2017 to 2024
$2.4M
Bioinorganic Explorations of Host-Defense ProteinsR01GM118695 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI NOLAN, ELIZABETH M · 2017 to 2025
$2.3M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Structural investigation of Helicobacter pylori transcription regulator NikRF32GM099257 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BOWMAN, SARAH ELIZABETH JOHNSON · 2011 to 2011
$46k
Howard Hughes Medical InstituteNCRR NIH HHS S10 RR029205NIEHS NIH HHS P30 ES002109NIGMS NIH HHS F32 GM099257NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM069857NIGMS NIH HHS R01 GM118695NIGMS NIH HHS R01 GM126376
6 · The paper itself

Abstract

Calprotectin (CP, S100A8/S100A9 oligomer, MRP-8/MRP-14 oligomer) is a host-defense protein that sequesters nutrient transition metals from microbes. Each S100A8/S100A9 heterodimer contains four EF-hand domains and two transition-metal-binding sites. We investigate the effect of Ca(II) ions on the structure and Ni(II)-binding properties of human CP. By employing energy dispersive X-ray (EDX) spectroscopy, we evaluate the metal content of Ni(II)-bound CP-Ser [oligomer of S100A8(C42S) and S100A9(C3S)] crystals obtained in the absence and presence of Ca(II). We present a 2.1 Å resolution crystal structure of Ni(II)-bound CP-Ser and compare this structure to a reported Ni(II)- and Ca(II)-bound CP-Ser structure [Nakashige, T. G., et al. (2017) J. Am. Chem. Soc. 139, 8828-8836]. This analysis reveals conformational changes associated with coordination of Ca(II) to the EF-hands of S100A9 and that Ca(II) binding affects the coordination number and geometry of the Ni(II) ion bound to the His

Indexed as

Binding SitesCalciumCalgranulin ACalgranulin BCrystallography, X-RayEF Hand MotifsHumansModels, MolecularNickelProtein BindingProtein ConformationCalciumCalgranulin ACalgranulin BNickel

Identifiers

PMID29890074
PMCPMC6050108
OpenAlexW2808625382

What OpenQuestion holds

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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.