Evidence map›Paper›PMID 30900513›Full record

ArticlemAbs

Functional mimetic of the G-protein coupled receptor CXCR4 on a soluble antibody scaffold.

Adem C Koksal, Meghan E Pennini, Marcello Marelli, Xiaodong Xiao, William F Dall'Acqua

Open access · goldAbstract read
In one paragraph

Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Review
  3. 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

5 authors at 1 institution in 1 country.

Adem C Koksala Department of Antibody Discovery and Protein Engineering , AstraZeneca , Gaithersburg , MD , USA.
Meghan E Penninib Microbial Sciences , MedImmune, AstraZeneca , Gaithersburg , MD , USA.
Marcello Marellia Department of Antibody Discovery and Protein Engineering , AstraZeneca , Gaithersburg , MD , USA.
Xiaodong Xiaoa Department of Antibody Discovery and Protein Engineering , AstraZeneca , Gaithersburg , MD , USA.
William F Dall'Acquaa Department of Antibody Discovery and Protein Engineering , AstraZeneca , Gaithersburg , MD , USA.
AstraZeneca (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G-protein coupled receptors (GPCRs) constitute major drug targets due to their involvement in critical biological functions and pathophysiological disorders. The leading challenge in their structural and functional characterization has been the need for a lipid environment to accommodate their hydrophobic cores. Here, we report an antibody scaffold mimetic (ASM) platform where we have recapitulated the extracellular functional domains of the GPCR, C-X-C chemokine receptor 4 (CXCR4) on a soluble antibody framework. The engineered ASM molecule can accommodate the N-terminal loop and all three extracellular loops of CXCR4. These extracellular features are important players in ligand recruitment and interaction for allostery and signal transduction. Our study shows that ASM

Indexed as

AntibodiesBiomimeticsChemokine CXCL12HEK293 CellsHIV Envelope Protein gp120HumansLigandsProtein BindingProtein ConformationProtein EngineeringReceptors, CXCR4Receptors, G-Protein-CoupledSignal TransductionAntibodiesChemokine CXCL12HIV Envelope Protein gp120LigandsReceptors, CXCR4Receptors, G-Protein-CoupledC-X-C chemokine receptor 4 (CXCR4)extracellular loop (ECL)gp120G-protein coupled receptor (GPCR)mimeticmodelingSDF-1αsoluble scaffoldtransmembrane proteins

Identifiers

PMID30900513
PMCPMC6601569
OpenAlexW2923361707

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.