Evidence map›Paper›PMID 8654359›Full record

ArticleThe EMBO journal1996

AChR phosphorylation and aggregation induced by an agrin fragment that lacks the binding domain for alpha-dystroglycan.

T Meier, M Gesemann, V Cavalli, M A Ruegg, B G Wallace

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1996. 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
3.3field-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

10 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Article
  3. LRP4 is critical for neuromuscular junction maintenance.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  4. Article
  5. Article
  6. alpha-Dystroglycan functions in acetylcholine receptor aggregation but is not a coreceptor for agrin-MuSK signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Article
  7. Neural agrin induces ectopic postsynaptic specializations in innervated muscle fibers.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1997
    Article
  8. Article
  9. Review
  10. Aggregation of sodium channels induced by a postnatally upregulated isoform of agrin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1996
    Article
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 1 institution in 1 country.

T MeierDepartment of Physiology, University of Colorado Health Sciences Center, Denver, CO 80262, USA.
M Gesemann
V Cavalli
M A Ruegg
B G Wallace
University of Colorado Health · US

Funding

MECHANISMS OF SYNAPSE FORMATIONR01NS029673 · NINDS · UNIVERSITY OF COLORADO DENVER · PI WALLACE, BRUCE G · 1991 to 1999
–
NINDS NIH HHS NS29673
6 · The paper itself

Abstract

Agrin induces both phosphorylation and aggregation of nicotinic acetylcholine receptors (AChRs) when added to myotubes in culture, apparently by binding to a specific receptor on the myotube surface. One such agrin receptor is alpha-dystroglycan, although binding to alpha-dystroglycan appears not to mediate AChR aggregation. To determine whether agrin-induced AChR phosphorylation is mediated by alpha-dystroglycan or by a different agrin receptor, fragments of recombinant agrin that differ in affinity for alpha-dystroglycan were examined for their ability to induce AChR phosphorylation and aggregation in mouse C2 myotubes. The carboxy-terminal 95 kDa agrin fragment agrin-c95(A0B0), which binds to alpha-dystroglycan with high affinity, failed to induce AChR phosphorylation and aggregation. In contrast, agrin-c95(A4B8) which binds less strongly to alpha-dystroglycan, induced both phosphorylation and aggregation, as did a small 21 kDa fragment of agrin, agrin-c21(B8), that completely lacks the binding domain for alpha-dystroglycan. We conclude that agrin-induced AChR phosphorylation and aggregation are triggered by an agrin receptor that is distinct from alpha-dystroglycan.

Indexed as

AgrinAnimalsCells, CulturedChickensCytoskeletal ProteinsDystroglycansMacromolecular SubstancesMembrane GlycoproteinsMiceMuscle, SkeletalPhosphorylationPhosphotyrosineProtein BindingReceptor AggregationReceptors, NicotinicAgrinCytoskeletal ProteinsDystroglycansMacromolecular SubstancesMembrane GlycoproteinsPhosphotyrosineReceptors, Nicotinic

Identifiers

PMID8654359
PMCPMC450197
OpenAlexW155383426

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.