Evidence map›Paper›PMID 24841172›Full record

ArticleJournal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research2014

PEGylation improves the pharmacokinetic properties and ability of interferon gamma to inhibit growth of a human tumor xenograft in athymic mice.

Christine M Fam, Stephen P Eisenberg, Sharon J Carlson, Elizabeth A Chlipala, George N Cox, Mary S Rosendahl

Open access · greenAbstract read
In one paragraph

Article in Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

10 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Fibronectin-targeted FUD and PEGylated FUD peptides for fibrotic diseases.Journal of controlled release : official journal of the Controlled Release Society · 2023
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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

6 authors at 2 institutions in 1 country.

Christine M Fam1 Bolder BioTechnology, Inc. , Boulder, Colorado.
Stephen P Eisenberg
Sharon J Carlson
Elizabeth A Chlipala
George N Cox
Mary S Rosendahl
Bolder Biotechnology, Inc. · USLongmont United Hospital · US

Funding

Long Acting IFN-gamma for Treating ImmunodeficienciesR44AI060043 · NIAID · BOLDER BIOTECHNOLOGY, INC. · PI COX, GEORGE NORBERT · 2007 to 2008
$762k
Long-Acting IFN-gamma for Treating Ovarian CancerR43CA108001 · NCI · BOLDER BIOTECHNOLOGY, INC. · PI COX, GEORGE NORBERT · 2005 to 2005
$122k
Long-Acting IFN-gamma for Treating ImmunodeficienciesR43AI060043 · NIAID · BOLDER BIOTECHNOLOGY, INC. · PI ROSENDAHL, MARY S. · 2005 to 2005
$99k
NCI NIH HHS R43CA108001NIAID NIH HHS R43AI060043NIAID NIH HHS R44AI060043
6 · The paper itself

Abstract

Interferon gamma (IFN-γ) is a 28 kDa homodimeric cytokine that exhibits potent immunomodulatory, anti-proliferative, and antiviral properties. The protein is used to treat chronic granulomatous disease and malignant osteopetrosis, and it is under investigation as a treatment for a variety of cancer, fungal and viral diseases. IFN-γ has a short circulating half life in vivo, which necessitates frequent administration to patients. An unusual feature of IFN-γ is that the protein contains no native cysteines. To create a longer-acting and potentially more effective form of the protein, we introduced a cysteine residue into the IFN-γ coding sequence at amino acid position 103, which is located in a surface-exposed, non-helical region of the protein. The added cysteine residue served as the site for targeted modification of the protein with a cysteine-reactive polyethylene glycol (PEG) reagent. The recombinant protein was expressed in bacteria, purified and modified with 10, 20, and 40 kDa maleimide PEGs. The purified, PEGylated proteins had in vitro bioactivities comparable to IFN-γ, as measured using an in vitro cell growth inhibition assay. The PEGylated proteins displayed 20- to 32-fold longer half lives than IFN-γ in rats, and they were significantly more effective than IFN-γ at inhibiting growth of a human tumor xenograft in athymic mice.

Indexed as

AnimalsCell Line, TumorCysteineFemaleGrowth InhibitorsHumansImmunomodulationInterferon-gammaMaleMiceMice, NudeMutationPolyethylene GlycolsProtein BindingProtein ConformationProtein EngineeringCysteineGrowth InhibitorsInterferon-gammaPolyethylene Glycols

Identifiers

PMID24841172
PMCPMC4186768
OpenAlexW2335479685

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.