Evidence map›Paper›PMID 26546677›Full record

ArticleThe Journal of biological chemistry2016

Cytokine Activation by Antibody Fragments Targeted to Cytokine-Receptor Signaling Complexes.

Srilalitha Kuruganti, Shane Miersch, Ashlesha Deshpande, Jeffrey A Speir, Bethany D Harris, Jill M Schriewer, R Mark L Buller, Sachdev S Sidhu, Mark R Walter

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.1field-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

6 citing papers in PubMed, 10 citations in OpenAlex.

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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

9 authors at 4 institutions in 2 countries.

Srilalitha KurugantiFrom the Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294.
Shane MierschBanting and Best Department of Medical Science, Donnelly Centre, University of Toronto, Toronto, Ontario M5G 1L6, Canada.
Ashlesha DeshpandeFrom the Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294.
Jeffrey A SpeirNational Resource for Automated Molecular Microscopy, Department of Integrative Structural and, Computational Biology, The Scripps Research Institute, La Jolla, California 92037, and.
Bethany D HarrisFrom the Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294.
Jill M SchriewerDepartment of Microbiology and Immunology, Saint Louis University Health Sciences Center, St. Louis, Missouri 63104.
R Mark L BullerDepartment of Microbiology and Immunology, Saint Louis University Health Sciences Center, St. Louis, Missouri 63104.
Sachdev S SidhuBanting and Best Department of Medical Science, Donnelly Centre, University of Toronto, Toronto, Ontario M5G 1L6, Canada.
Mark R WalterFrom the Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, walter@uab.edu.
University of Alabama at Birmingham · USSaint Louis University · USUniversity of Toronto · CAScripps Research Institute · US

Funding

XRAY CRYSTALLOGRAPHYP30CA013148 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI Robert S Welner · 1985 to 2026
$165.9M
TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
Prevention of Primary HCMV Infection by Vaccinating against HCMV-Encoded IL-10R01AI049342 · NIAID · UNIVERSITY OF CALIFORNIA DAVIS · PI BARRY, PETER A, WALTER, MARK R · 2002 to 2017
$6.9M
Vaccine-mediated Targeting of Viral IL10 to Control HCMV Shedding and ReinfectionR01AI097629 · NIAID · UNIVERSITY OF CALIFORNIA AT DAVIS · PI BARRY, PETER A, WALTER, MARK R · 2012 to 2016
$3.1M
NCI NIH HHS P30 CA013148NIAID NIH HHS R01 AI049342NIAID NIH HHS R01AI049342NIAID NIH HHS R01 AI097629NIAID NIH HHS R01AI097629NIGMS NIH HHS P41 GM103310
6 · The paper itself

Abstract

Exogenous cytokine therapy can induce systemic toxicity, which might be prevented by activating endogenously produced cytokines in local cell niches. Here we developed antibody-based activators of cytokine signaling (AcCS), which recognize cytokines only when they are bound to their cell surface receptors. AcCS were developed for type I interferons (IFNs), which induce cellular activities by binding to cell surface receptors IFNAR1 and IFNAR2. As a potential alternative to exogenous IFN therapy, AcCS were shown to potentiate the biological activities of natural IFNs by ∼100-fold. Biochemical and structural characterization demonstrates that the AcCS stabilize the IFN-IFNAR2 binary complex by recognizing an IFN-induced conformational change in IFNAR2. Using IFN mutants that disrupt IFNAR1 binding, AcCS were able to enhance IFN antiviral potency without activating antiproliferative responses. This suggests AcCS can be used to manipulate cytokine signaling for basic science and possibly for therapeutic applications.

Indexed as

Signal TransductionAntiviral AgentsBinding SitesCell Line, TumorCell ProliferationCytokinesGene Expression ProfilingGene Expression RegulationHumansImmunoglobulin FragmentsInterferon-alphaKineticsMutationPhosphorylationProtein ConformationReceptor, Interferon alpha-betaAntiviral AgentsCytokinesImmunoglobulin FragmentsInterferon-alphaReceptor, Interferon alpha-betaReceptors, CytokineSTAT1 Transcription Factorcell signalingconformational changecytokineinterferonphage displayprotein structurereceptor

Identifiers

PMID26546677
PMCPMC4697184
OpenAlexW2124280909

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.