Evidence map›Paper›PMID 29029544›Full record

ReviewOncotarget2017

Melflufen - a peptidase-potentiated alkylating agent in clinical trials.

Malin Wickström, Peter Nygren, Rolf Larsson, Johan Harmenberg, Jakob Lindberg, Per Sjöberg, Markus Jerling, Fredrik Lehmann, Paul Richardson, Kenneth Anderson and 2 more

Open access · diamondAbstract readReview
In one paragraph

Review in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.2field-weighted citation impact, top 10% 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

43 citing papers in PubMed, 83 citations in OpenAlex.

  1. Trial
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  6. Melflufen and Dexamethasone in Heavily Pretreated Relapsed and Refractory Multiple Myeloma.Journal of clinical oncology : official journal of the American Society of Clinical Oncology · 2021
    Trial
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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

12 authors at 5 institutions in 2 countries.

Malin WickströmDepartment of Medical Sciences, Division of Clinical Pharmacology, Uppsala University, Uppsala SE, Sweden.
Peter NygrenDepartment of Medical Sciences, Division of Clinical Pharmacology, Uppsala University, Uppsala SE, Sweden.
Rolf LarssonDepartment of Medical Sciences, Division of Clinical Pharmacology, Uppsala University, Uppsala SE, Sweden.
Johan HarmenbergOncopeptides AB, Västra Trädgårdsgatan 15, Stockholm, Sweden.
Jakob LindbergOncopeptides AB, Västra Trädgårdsgatan 15, Stockholm, Sweden.
Per SjöbergOncopeptides AB, Västra Trädgårdsgatan 15, Stockholm, Sweden.
Markus JerlingOncopeptides AB, Västra Trädgårdsgatan 15, Stockholm, Sweden.
Fredrik LehmannRecipharm OT Chemistry AB, Sweden.
Paul RichardsonDepartment of Medical Oncology, The LeBow Institute for Myeloma Therapeutics and Jerome Lipper Myeloma Center, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts.
Kenneth AndersonDepartment of Medical Oncology, The LeBow Institute for Myeloma Therapeutics and Jerome Lipper Myeloma Center, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts.
Dharminder ChauhanDepartment of Medical Oncology, The LeBow Institute for Myeloma Therapeutics and Jerome Lipper Myeloma Center, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts.
Joachim GullboDepartment of Medical Sciences, Division of Clinical Pharmacology, Uppsala University, Uppsala SE, Sweden.
Oncopeptides (Sweden) · SEDana-Farber Cancer Institute · USUppsala University · SEKarolinska Institutet · SERecipharm (Sweden) · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminopeptidases like aminopeptidase N (APN, also known as CD13) play an important role not only in normal cellular functioning but also in the development of cancer, including processes like tumor cell invasion, differentiation, proliferation, apoptosis, motility, and angiogenesis. An increased expression of APN has been described in several types of human malignancies, especially those characterized by fast-growing and aggressive phenotypes, suggesting APN as a potential therapeutic target. Melphalan flufenamide ethyl ester (melflufen, previously denoted J1) is a peptidase-potentiated alkylating agent. Melflufen readily penetrates membranes and an equilibrium is rapidly achieved, followed by enzymatic cleavage in aminopeptidase positive cells, which results in trapping of less lipophilic metabolites. This targeting effect results in very high intracellular concentrations of its metabolite melphalan and subsequent apoptotic cell death. This results in a potency increase (melflufen

Indexed as

aminopeptidasecancermelflufentargeted chemotherapy

Identifiers

PMID29029544
PMCPMC5630444
OpenAlexW2624372404

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.