Evidence map›Paper›PMID 27458983›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2016

Aspartate-Based CXCR4 Chemokine Receptor Binding of Cross-Bridged Tetraazamacrocyclic Copper(II) and Zinc(II) Complexes.

Randall D Maples, Amy N Cain, Benjamin P Burke, Jon D Silversides, Ryan E Mewis, Thomas D'huys, Dominique Schols, Douglas P Linder, Stephen J Archibald, Timothy J Hubin

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2016. 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
–field-weighted citation impact
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.

  1. Article
  2. Dalton transactions (Cambridge, England : 2003) · 2024
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2020
    Article
  9. Article
  10. Article
  11. Article
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

10 authors.

Randall D MaplesDepartment of Chemistry and Physics, Southwestern Oklahoma State University, Weatherford, OK, 73096, USA.
Amy N CainDepartment of Chemistry and Physics, Southwestern Oklahoma State University, Weatherford, OK, 73096, USA.
Benjamin P BurkeDepartment of Chemistry and Positron Emission Tomography Research Centre, University of Hull, Hull, HU6 7RX, UK.
Jon D SilversidesDepartment of Chemistry and Positron Emission Tomography Research Centre, University of Hull, Hull, HU6 7RX, UK.
Ryan E MewisDepartment of Chemistry and Positron Emission Tomography Research Centre, University of Hull, Hull, HU6 7RX, UK.
Thomas D'huysRega Institute for Medical Research, KU Leuven, 3000, Leuven, Belgium.
Dominique ScholsRega Institute for Medical Research, KU Leuven, 3000, Leuven, Belgium.
Douglas P LinderDepartment of Chemistry and Physics, Southwestern Oklahoma State University, Weatherford, OK, 73096, USA.
Stephen J ArchibaldDepartment of Chemistry and Positron Emission Tomography Research Centre, University of Hull, Hull, HU6 7RX, UK. S.J.Archibald@Hull.ac.uk.
Timothy J HubinDepartment of Chemistry and Physics, Southwestern Oklahoma State University, Weatherford, OK, 73096, USA. Tim.Hubin@swosu.edu.ORCID http://orcid.org/0000-0003-2277-1191

Funding

Proteomics CoreP20GM103447 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI Mark L Lang · 2012 to 2026
$60.2M
NIGMS NIH HHS P20 GM103447
6 · The paper itself

Abstract

The CXCR4 chemokine receptor is implicated in a number of diseases including HIV infection and cancer development and metastasis. Previous studies have demonstrated that configurationally restricted bis-tetraazamacrocyclic metal complexes are high-affinity CXCR4 antagonists. Here, we present the synthesis of Cu(2+) and Zn(2+) acetate complexes of six cross-bridged tetraazamacrocycles to mimic their coordination interaction with the aspartate side chains known to bind them to CXCR4. X-ray crystal structures for three new Cu(2+) acetate complexes and two new Zn(2+) acetate complexes demonstrate metal-ion-dependent differences in the mode of binding the acetate ligand concomitantly with the requisite cis-V-configured cross-bridged tetraazamacrocyle. Concurrent density functional theory molecular modelling studies produced an energetic rationale for the unexpected [Zn(OAc)(H2 O)](+) coordination motif present in all of the Zn(2+) cross-bridged tetraazamacrocycle crystal structures, which differs from the chelating acetate [Zn(OAc)](+) structures of known unbridged and side-bridged tetraazamacrocyclic Zn(2+) -containing CXCR4 antagonists.

Indexed as

Aspartic AcidChelating AgentsCoordination ComplexesCopperCrystallography, X-RayLigandsProtein BindingReceptors, CXCR4ZincAspartic AcidChelating AgentsCoordination ComplexesCopperLigandsReceptors, CXCR4Zincacetate bindingcopperCXCR4 chemokine receptortetraazamacrocycleszinc

Identifiers

PMID27458983
PMCPMC5224883

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.