Evidence map›Paper›PMID 21454605›Full record

ArticleThe Journal of biological chemistry2011

A multi-domain fragment of Nogo-A protein is a potent inhibitor of cortical axon regeneration via Nogo receptor 1.

Eric A Huebner, Byung G Kim, Philip J Duffy, Rebecca H Brown, Stephen M Strittmatter

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

42 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
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  6. Inositol Polyphosphate-5-Phosphatase K (The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
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  14. Review
  15. Diltiazem Promotes Regenerative Axon Growth.Molecular neurobiology · 2019
    Article
  16. Plexina2 and CRMP2 Signaling Complex Is Activated by Nogo-A-Liganded Ngr1 to Restrict Corticospinal Axon Sprouting after Trauma.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  17. Article
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  20. Review
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

5 authors at 2 institutions in 2 countries.

Eric A HuebnerDepartment of Neurology and Program in Cellular Neuroscience, Neurodegeneration, and Repair, Yale University School of Medicine, New Haven, Connecticut 06536, USA.
Byung G Kim
Philip J Duffy
Rebecca H Brown
Stephen M Strittmatter
Yale University · USAjou University · KR

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007205 · NIGMS · YALE UNIVERSITY · PI KAZMIERCZAK, BARBARA I · 1985 to 2019
$42.9M
MOLECULAR DETERMINANTS OF AXONAL REGENERATIONR01NS039962 · NINDS · YALE UNIVERSITY · PI STRITTMATTER, STEPHEN M · 2000 to 2010
$3.9M
Nogo Receptor in Axonal RegenerationR01NS042304 · NINDS · YALE UNIVERSITY · PI STRITTMATTER, STEPHEN M · 2001 to 2010
$3.3M
Axonal Growth Cone Signal TransductionR37NS033020 · NINDS · YALE UNIVERSITY · PI STRITTMATTER, STEPHEN M · 2005 to 2011
$2.9M
NEURONAL GROWTH CONE SIGNAL TRANSDUCTION MECHANISMSR01NS033020 · NINDS · YALE UNIVERSITY · PI STRITTMATTER, STEPHEN M · 1993 to 2004
$2.0M
NIGMS NIH HHS MSTP TG T32GM07205NIGMS NIH HHS T32 GM007205NINDS NIH HHS R01 NS033020NINDS NIH HHS R01 NS039962NINDS NIH HHS R01 NS042304NINDS NIH HHS R01NS33020NINDS NIH HHS R01NS39962NINDS NIH HHS R01NS42304NINDS NIH HHS R37 NS033020
6 · The paper itself

Abstract

Nogo-A limits axon regeneration and functional recovery after central nervous system injury in adult mammals. Three regions of Nogo-A (Nogo-A-24, Nogo-66, and Nogo-C39) interact with the neuronal Nogo-66 receptor 1 (NgR1). Nogo-66 also interacts with a structurally unrelated cell surface receptor, paired immunoglobulin-like receptor (PirB). We show here that the other two NgR1-interacting domains, Nogo-A-24 and Nogo-C39, also bind to PirB with high affinity. A purified 22-kDa protein containing all three NgR1- and PirB-interacting domains (Nogo-22) is a substantially more potent growth cone-collapsing molecule than Nogo-66 for chick dorsal root ganglion neurons and mature cortical neurons. Moreover, Nogo-22 inhibits axon regeneration of mature cortical neurons in vitro more potently than does Nogo-66. Although all three NgR1-interacting domains of Nogo-A also interact with PirB, expression of PirB in mature cortical cultures is nearly undetectable. Consistent with a relatively minor role for PirB in mature cortical neurons, Nogo-22 inhibition of axon regeneration is abolished by genetic deletion of NgR1. Thus, NgR1 is the predominant receptor for Nogo-22 in regenerating cortical neurons.

Indexed as

AnimalsAxonsCells, CulturedCerebral CortexChickensChlorocebus aethiopsGanglia, SpinalGPI-Linked ProteinsHumansMiceMyelin ProteinsNogo ProteinsNogo Receptor 1Protein Structure, TertiaryReceptors, Cell SurfaceReceptors, ImmunologicGPI-Linked ProteinsMyelin ProteinsNogo ProteinsNogo Receptor 1Pirb protein, mouseReceptors, Cell SurfaceReceptors, ImmunologicRTN4 protein, humanRtn4 protein, mouseRTN4R protein, human

Identifiers

PMID21454605
PMCPMC3093876
OpenAlexW2087527232

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.