Evidence map›Paper›PMID 25245280›Full record

ArticleOncotarget2014

Amphipathic tail-anchoring peptide is a promising therapeutic agent for prostate cancer treatment.

Gejing De, Jae-Kyun Ko, Tao Tan, Hua Zhu, Haichang Li, Jianjie Ma

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2014. 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
1.3field-weighted citation impact, top 22% 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, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Targeting Tumors Using Peptides.Molecules (Basel, Switzerland) · 2020
    Review
  5. Review
  6. Article
  7. Article
  8. Peptides as drug delivery vehicles across biological barriers.Journal of pharmaceutical investigation · 2018
    Article
  9. Tumor penetrating peptides for improved drug delivery.Advanced drug delivery reviews · 2017
    Review
  10. Review
  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

6 authors at 3 institutions in 1 country.

Gejing DeDepartment of Surgery, Davis Heart and Lung Research Institute, The Ohio State University Wexner Medical Center, Columbus, OH, USA.
Jae-Kyun KoDepartment of Physiology and Biophysics, Rutgers University-Robert Wood Johnson Medical School, Piscataway, NJ, USA. Mutagenex Inc., 1 Jill Court, Hillsborough, NJ, USA.
Tao TanTRIM-edicine, Inc, Columbus, OH, USA.
Hua ZhuDepartment of Surgery, Davis Heart and Lung Research Institute, The Ohio State University Wexner Medical Center, Columbus, OH, USA.
Haichang LiDepartment of Surgery, Davis Heart and Lung Research Institute, The Ohio State University Wexner Medical Center, Columbus, OH, USA.
Jianjie MaDepartment of Surgery, Davis Heart and Lung Research Institute, The Ohio State University Wexner Medical Center, Columbus, OH, USA. Department of Physiology and Biophysics, Rutgers University-Robert Wood Johnson Medical School, Piscataway, NJ, USA. TRIM-edicine, Inc, Columbus, OH, USA.
The Ohio State University Wexner Medical Center · USRutgers, The State University of New Jersey · USTRIM edicine (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amphipathic tail-anchoring peptide (ATAP) derived from the human anti-apoptotic protein Bfl-1 is a potent inducer of apoptosis by targeting mitochondria permeability transition. By linking ATAP to an internalizing RGD peptide (iRGD), selective targeting for ATAP to tumor cell was achieved. Confocal fluorescence microscopy showed that ATAP-iRGD could penetrate into cancer cells and distribute along the mitochondria network. ATAP-iRGD triggered mitochondria-dependent cell death through release of cytochrome c. In an effort to promote ATAP-iRGD physiochemical properties to approach clinic application, amino acid substitution and chemical modification were made with ATAP-iRGD to improve its bioactivity. One of these modified peptides, ATAP-iRGD-M8, was with improved stability and aqueous solubility without compromising in vitro cytotoxicity in cultured cancer cells. In vivo xenograft studies with multiple prostate cancer cell lines showed that intravenous administration of ATAP-iRGD-M8 suppressed tumor growth. Toxicological studies revealed that repetitive intravenous administration of ATAP-iRGD-M8 did not produce significant toxicity in the SV129 mice. Our data suggest that ATAP-iRGD-M8 is a promising agent with high selectivity and limited systemic toxicity for prostate cancer treatment.

Indexed as

AnimalsAntineoplastic AgentsHumansMaleMiceMice, NudeMicroscopy, ConfocalMinor Histocompatibility AntigensMolecular Targeted TherapyOligopeptidesPeptidesProstatic NeoplasmsProto-Oncogene Proteins c-bcl-2Xenograft Model Antitumor AssaysAntineoplastic AgentsBCL2-related protein A1Minor Histocompatibility AntigensN-end cysteine peptide tumor-homing peptideOligopeptidesPeptidesProto-Oncogene Proteins c-bcl-2

Identifiers

PMID25245280
PMCPMC4202157
OpenAlexW1838335582

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.