Evidence map›Paper›PMID 11150334›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2001

An evolutionarily conserved transmembrane protein that is a novel downstream target of neurotrophin and ephrin receptors.

H Kong, J Boulter, J L Weber, C Lai, M V Chao

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

68 citing papers in PubMed, 169 citations in OpenAlex.

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  15. In vivo functions of p75Trends in pharmacological sciences · 2021
    Review
  16. Article
  17. Article
  18. Article
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  20. Article

8 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

H KongMolecular Neurobiology Program, Skirball Institute for Biomolecular Medicine, New York University School of Medicine, New York, New York, USA.
J Boulter
J L Weber
C Lai
M V Chao
New York University · USScripps Research Institute · USUniversity of California, Los Angeles · US

Funding

The Role of Striosome Neurons in Mediating Opiod RewardP50DA005010 · NIDA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FANSELOW, MICHAEL S · 1987 to 2021
$30.7M
TITLE REGULATION OF NEURONAL MITOSISP01HD023315 · NICHD · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI DREYFUS, CHERYL F · 1987 to 2013
$17.5M
MOLECULAR BIOLOGY OF THE NERVE GROWTH FACTOR RECEPTORR01NS021072 · NINDS · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI CHAO, MOSES VICTOR · 1985 to 2015
$5.8M
Molecular Analysis of Neurotrophin ActionR56NS021072 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI CHAO, MOSES VICTOR · 2011 to 2017
$882k
MECHANISMS OF NGF-MEDIATED CELL DEATHF32NS010489 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI KONG, HAEYOUNG · 1997 to 2000
$39k
NICHD NIH HHS HD 23315NICHD NIH HHS P01 HD023315NIDA NIH HHS P50 DA005010NINDS NIH HHS F32 NS010489NINDS NIH HHS NS 10489NINDS NIH HHS NS 21072NINDS NIH HHS R01 NS021072NINDS NIH HHS R56 NS021072
6 · The paper itself

Abstract

Appropriate development of nervous system connectivity involves a variety of processes, including neuronal life-and-death decisions, differentiation, axon guidance and migration, and synaptogenesis. Although these activities likely require specialized signaling events, few substrates unique to these neurotrophic functions have been identified. Here we describe the cloning of ankyrin repeat-rich membrane spanning (ARMS), which encodes a novel downstream target of neurotrophin and ephrin receptor tyrosine kinases, Trk and Eph, respectively. The amino acid sequence of ARMS is highly conserved from nematode to human, suggesting an evolutionarily conserved role for this protein. The ARMS protein consists of 1715 amino acids containing four putative transmembrane domains, multiple ankyrin repeats, a sterile alpha motif domain, and a potential PDZ-binding motif. In the rat, ARMS is specifically expressed in the developing nervous system and in highly plastic areas of the adult brain, regions enriched in Trks and Eph receptors. ARMS can physically associate with TrkA and p75 neurotrophin receptors. Moreover, endogenous ARMS protein is tyrosine phosphorylated after neurotrophin treatment of pheochromocytoma 12 cells and primary hippocampal neurons or ephrin B treatment of NG108-15 cells, demonstrating that ARMS is a downstream target for both neurotrophin and ephrin receptors.

Indexed as

PhosphoproteinsAmino Acid MotifsAnimalsAnkyrin RepeatCell LineCentral Nervous SystemCloning, MolecularConserved SequenceHumansMembrane ProteinsMolecular Sequence DataNerve Growth FactorsOrgan SpecificityPC12 CellsPhosphorylationRatsKidins220 protein, ratMembrane ProteinsNerve Growth FactorsPhosphoproteinsReceptor, EphA1Receptor, Nerve Growth FactorReceptor Protein-Tyrosine KinasesReceptors, Nerve Growth FactorReceptor, trkAReceptor, trkBRNA, Messenger

Identifiers

PMID11150334
PMCPMC6762419
OpenAlexW1871356778

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.