Evidence map›Paper›PMID 25359769›Full record

ArticleThe Journal of biological chemistry2014

A unified mechanism for aminopeptidase N-based tumor cell motility and tumor-homing therapy.

Chang Liu, Yang Yang, Lang Chen, Yi-Lun Lin, Fang Li

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. 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
1.8field-weighted citation impact, top 14% 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, 40 citations in OpenAlex.

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  13. GlycineAdvanced functional materials · 2017
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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 1 institution in 1 country.

Chang LiuFrom the Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota 55455.
Yang YangFrom the Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota 55455.
Lang ChenFrom the Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota 55455.
Yi-Lun LinFrom the Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota 55455.
Fang LiFrom the Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota 55455 lifang@umn.edu.
University of Minnesota Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tumor cell surface aminopeptidase N (APN or CD13) has two puzzling functions unrelated to its enzymatic activity: mediating tumor cell motility and serving as a receptor for tumor-homing peptides (peptides that bring anti-cancer drugs to tumor cells). To investigate APN-based tumor-homing therapy, we determined the crystal structure of APN complexed with a tumor-homing peptide containing a representative Asn-Gly-Arg (NGR) motif. The tumor-homing peptide binds to the APN enzymatic active site, but it resists APN degradation due to a distorted scissile peptide bond. To explore APN-based tumor cell motility, we examined the interactions between APN and extracellular matrix (ECM) proteins. APN binds to, but does not degrade, NGR motifs in ECM proteins that share similar conformations with the NGR motif in the APN-bound tumor-homing peptide. Therefore, APN-based tumor cell motility and tumor-homing therapy rely on a unified mechanism in which both functions are driven by the specific and stable interactions between APN and the NGR motifs in ECM proteins and tumor-homing peptides. This study further implicates APN as an integrin-like molecule that functions broadly in cell motility and adhesion by interacting with its signature NGR motifs in the extracellular environment.

Indexed as

Cell MovementAmino Acid MotifsAmino Acid SequenceAnimalsAntineoplastic AgentsBiological TransportCD13 AntigensCell AdhesionCell Line, TumorCrystallography, X-RayExtracellular Matrix ProteinsHumansModels, MolecularOligopeptidesProtein ConformationSwineAntineoplastic AgentsCD13 AntigensExtracellular Matrix ProteinsNGR peptideOligopeptidesCancer BiologyCancer TherapyCell MotilityCrystallographyExtracellular Matrix ProteinTumor MarkerTumor Metastases

Identifiers

PMID25359769
PMCPMC4263860
OpenAlexW2123114567

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.