Literature DB >> 1851019

Structure and expression of a rat agrin.

F Rupp1, D G Payan, C Magill-Solc, D M Cowan, R H Scheller.   

Abstract

Agrin is a component of the basal lamina that causes the aggregation of acetylcholine receptors on cultured muscle fibers. An agrin cDNA clone isolated from electromotor neurons of a marine ray was used to characterize the corresponding cDNAs from a rat embryonic spinal cord library. Analysis of a set of clones predicts a 1940 amino acid protein containing 141 cysteine residues. The predicted protein has nine domains homologous to protease inhibitors, a region similar to domain III of laminin, and four epidermal growth factor repeats. The agrin gene is expressed in rat embryonic nervous system and muscle. The rat agrin protein is concentrated at synapses, where it may play a role in development and regeneration.

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Year:  1991        PMID: 1851019     DOI: 10.1016/0896-6273(91)90177-2

Source DB:  PubMed          Journal:  Neuron        ISSN: 0896-6273            Impact factor:   17.173


  52 in total

1.  Neural agrin controls acetylcholine receptor stability in skeletal muscle fibers.

Authors:  G Bezakova; I Rabben; I Sefland; G Fumagalli; T Lømo
Journal:  Proc Natl Acad Sci U S A       Date:  2001-08-07       Impact factor: 11.205

Review 2.  The role of agrin in synaptic development, plasticity and signaling in the central nervous system.

Authors:  Mathew P Daniels
Journal:  Neurochem Int       Date:  2012-03-05       Impact factor: 3.921

3.  Agrin is a major heparan sulfate proteoglycan accumulating in Alzheimer's disease brain.

Authors:  M M Verbeek; I Otte-Höller; J van den Born; L P van den Heuvel; G David; P Wesseling; R M de Waal
Journal:  Am J Pathol       Date:  1999-12       Impact factor: 4.307

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

Authors:  T Meier; M Gesemann; V Cavalli; M A Ruegg; B G Wallace
Journal:  EMBO J       Date:  1996-06-03       Impact factor: 11.598

5.  Induction of filopodia-like protrusions by transmembrane agrin: role of agrin glycosaminoglycan chains and Rho-family GTPases.

Authors:  Lin Lin; Seumas McCroskery; Jaime M Ross; Yvonne Chak; Birgit Neuhuber; Mathew P Daniels
Journal:  Exp Cell Res       Date:  2010-05-13       Impact factor: 3.905

6.  The SEA module: a new extracellular domain associated with O-glycosylation.

Authors:  P Bork; L Patthy
Journal:  Protein Sci       Date:  1995-07       Impact factor: 6.725

Review 7.  The role of laminins in basement membrane function.

Authors:  M Aumailley; N Smyth
Journal:  J Anat       Date:  1998-07       Impact factor: 2.610

8.  Agrin induced morphological and structural changes in growth cones of cultured hippocampal neurons.

Authors:  R A Bergstrom; R C Sinjoanu; A Ferreira
Journal:  Neuroscience       Date:  2007-08-14       Impact factor: 3.590

9.  Specific agrin isoforms induce cAMP response element binding protein phosphorylation in hippocampal neurons.

Authors:  R R Ji; C M Böse; C Lesuisse; D Qiu; J C Huang; Q Zhang; F Rupp
Journal:  J Neurosci       Date:  1998-12-01       Impact factor: 6.167

Review 10.  Mechanotransduction: touch and feel at the molecular level as modeled in Caenorhabditis elegans.

Authors:  Laura Bianchi
Journal:  Mol Neurobiol       Date:  2007-09-27       Impact factor: 5.590

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