Evidence map›Paper›PMID 26756335›Full record

ArticlePloS one2016

A Novel Triazolopyridine-Based Spleen Tyrosine Kinase Inhibitor That Arrests Joint Inflammation.

Gregory D Ferguson, Mercedes Delgado, Veronique Plantevin-Krenitsky, Kristen Jensen-Pergakes, R J Bates, Sanaa Torres, Maria Celeridad, Heather Brown, Kelven Burnett, Lisa Nadolny and 17 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

0 citing papers in PubMed, 11 citations in OpenAlex.

No citing paper in PubMed yet.

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

27 authors at 2 institutions in 2 countries.

Gregory D FergusonDepartment of Inflammation Research, Celgene Corporation, San Diego, California, United States of America.
Mercedes DelgadoDepartment of Chemistry, Celgene Corporation, San Diego, California, United States of America.
Veronique Plantevin-KrenitskyDepartment of Chemistry, Celgene Corporation, San Diego, California, United States of America.
Kristen Jensen-PergakesDepartment of Tumor Cell Biology, Pfizer Corporation, San Diego, California, United States of America.
R J BatesDepartment of Inflammation Research, Celgene Corporation, San Diego, California, United States of America.
Sanaa TorresDepartment of Inflammation Research, Celgene Corporation, San Diego, California, United States of America.
Maria CeleridadDepartment of Inflammation Research, Celgene Corporation, San Diego, California, United States of America.
Heather BrownDepartment of Pharmacology, Celgene Corporation, San Diego, California, United States of America.
Kelven BurnettDepartment of Pharmacology, Celgene Corporation, San Diego, California, United States of America.
Lisa NadolnyDepartment of Chemistry, Celgene Corporation, San Diego, California, United States of America.
Lida TehraniDepartment of Chemistry, Celgene Corporation, San Diego, California, United States of America.
Garrick PackardDepartment of Chemistry, Celgene Corporation, San Diego, California, United States of America.
Barbra PagariganDepartment of Biochemistry, Celgene Corporation, San Diego, California, United States of America.
Jason HaelewynDepartment of Biochemistry, Celgene Corporation, San Diego, California, United States of America.
Trish NguyenDepartment of Biochemistry, Celgene Corporation, San Diego, California, United States of America.
Li XuDepartment of Inflammation Research, Celgene Corporation, San Diego, California, United States of America.
Yang TangDepartment of Pharmacology, Celgene Corporation, San Diego, California, United States of America.
Matthew HickmanDepartment of Biochemistry, Celgene Corporation, San Diego, California, United States of America.
Frans BaculiDepartment of Biochemistry, Celgene Corporation, San Diego, California, United States of America.
Steven PierceDepartment of Biochemistry, Celgene Corporation, San Diego, California, United States of America.
Keiji MiyazawaDepartment of Corporate Planning and Strategy, Kissei Pharmaceutical Company, Matsumoto City, Nagano, Japan.
Pilgrim JacksonDepartment of Biochemistry, Celgene Corporation, San Diego, California, United States of America.
Philip ChamberlainDepartment of Biochemistry, Celgene Corporation, San Diego, California, United States of America.
Laurie LeBrunDepartment of Biochemistry, Celgene Corporation, San Diego, California, United States of America.
Weilin XieDepartment of Inflammation Research, Celgene Corporation, San Diego, California, United States of America.
Brydon BennettDepartment of Inflammation Research, Celgene Corporation, San Diego, California, United States of America.
Kate BleaseDepartment of Pharmacology, Celgene Corporation, San Diego, California, United States of America.
Kissei Pharmaceutical (Japan) · JPPfizer (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autoantibodies and the immunoreceptors to which they bind can contribute to the pathogenesis of autoimmune diseases such as rheumatoid arthritis (RA). Spleen Tyrosine Kinase (Syk) is a non-receptor tyrosine kinase with a central role in immunoreceptor (FcR) signaling and immune cell functionality. Syk kinase inhibitors have activity in antibody-dependent immune cell activation assays, in preclinical models of arthritis, and have progressed into clinical trials for RA and other autoimmune diseases. Here we describe the characterization of a novel triazolopyridine-based Syk kinase inhibitor, CC-509. This compound is a potent inhibitor of purified Syk enzyme, FcR-dependent and FcR-independent signaling in primary immune cells, and basophil activation in human whole blood. CC-509 is moderately selective across the kinome and against other non-kinase enzymes or receptors. Importantly, CC-509 was optimized away from and has modest activity against cellular KDR and Jak2, kinases that when inhibited in a preclinical and clinical setting may promote hypertension and neutropenia, respectively. In addition, CC-509 is orally bioavailable and displays dose-dependent efficacy in two rodent models of immune-inflammatory disease. In passive cutaneous anaphylaxis (PCA), CC-509 significantly inhibited skin edema. Moreover, CC-509 significantly reduced paw swelling and the tissue levels of pro-inflammatory cytokines RANTES and MIP-1α in the collagen-induced arthritis (CIA) model. In summary, CC-509 is a potent, moderately selective, and efficacious inhibitor of Syk that has a differentiated profile when compared to other Syk compounds that have progressed into the clinic for RA.

Indexed as

AnimalsArthritis, ExperimentalBasophilsCell LineCollagenCrystallography, X-RayDose-Response Relationship, DrugEdemaEosinophilsFemaleHEK293 CellsHumansHypertensionIndazolesInflammationInhibitory Concentration 50CC-509CollagenIndazolesIntracellular Signaling Peptides and ProteinsJAK2 protein, humanJanus Kinase 2Protein-Tyrosine KinasesPyridinesReceptors, FcSyk KinaseSYK protein, humanSyk protein, ratTriazolesVascular Endothelial Growth Factor Receptor-2

Identifiers

PMID26756335
PMCPMC4710522
OpenAlexW2238091472

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.