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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 02 Oct 2014.

Receptor-associated protein of the synapse

43-kDa, Rapsyn, RAPSN
This gene encodes a member of a family of proteins that are receptor associated proteins of the synapse. The encoded protein contains a conserved cAMP-dependent protein kinase phosphorylation site, and plays a critical role in clustering and anchoring nicotinic acetylcholine receptors at synaptic sites by linking the receptors to the underlying postsynaptic cytoskeleton, possibly by direct association with actin or spectrin. Mutations in this gene may play a role in postsynaptic congenital myasthenic syndromes. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Apr 2011] (from NCBI)
Top mentioned proteins: ACID, HAD, CAN, fibrillin-1, CD45
Papers on 43-kDa
Serological and antigenic profiles of clinical isolates of Paracoccidioides spp. from Central Western Brazil.
Hahn et al., Cuiabá, Brazil. In Mycoses, Aug 2014
The results observed for reactions of radial immunodiffusion against the commonly used exoantigens containing a 43-kDa glycoprotein (gp43) suggest that this fungus exhibits major antigenic variability by geographic region.
How common is childhood myasthenia? The UK incidence and prevalence of autoimmune and congenital myasthenia.
Jayawant et al., Oxford, United Kingdom. In Arch Dis Child, Jun 2014
CHRNE, RAPSN and DOK7 were the most commonly identified mutations.
Targeted high-throughput sequencing identifies a TARDBP mutation as a cause of early-onset FTD without motor neuron disease.
Adamczyk et al., Tübingen, Germany. In Neurobiol Aging, May 2014
For example, although the 43-kDa transactive response DNA binding protein is the major pathologic hallmark linking ALS and FTD, mutations in the gene encoding 43-kDa transactive response DNA binding protein (TARDBP) have been appreciated only as a cause of ALS-phenotypes, but not yet of pure FTD.
Sequential distribution of pTDP-43 pathology in behavioral variant frontotemporal dementia (bvFTD).
Trojanowski et al., Philadelphia, United States. In Acta Neuropathol, Mar 2014
We examined regional distribution patterns of phosphorylated 43-kDa TAR DNA-binding protein (pTDP-43) intraneuronal inclusions in frontotemporal lobar degeneration (FTLD).
Acceleration of TDP43 and FUS/TLS protein expressions in the preconditioned hippocampus following repeated transient ischemia.
Abe et al., Okayama, Japan. In J Neurosci Res, Jan 2014
The 43-kDa transactivation response DNA binding protein (TDP43), fused in sarcoma/translocated in liposarcoma (FUS/TLS), heat shock protein 70 (HSP70), and β-amyloid (Aβ) are induced and involved in cerebral ischemia, amyotrophic lateral sclerosis (ALS), and Alzheimer's disease (AD), but their relationships in ischemic tolerance have never been examined, although they could be involved in endogenous neuroprotection under ischemic preconditioning.
Amyotrophic lateral sclerosis--a model of corticofugal axonal spread.
Del Tredici et al., Ulm, Germany. In Nat Rev Neurol, Dec 2013
The pathological process underlying amyotrophic lateral sclerosis (ALS) is associated with the formation of cytoplasmic inclusions consisting mainly of phosphorylated 43-kDa transactive response DNA-binding protein (pTDP-43), which plays an essential part in the pathogenesis of ALS.
[An autopsy case of amyotrophic lateral sclerosis with prominent muscle cramps, fasciculation, and high titer of anti-voltage gated potassium channel (VGKC) complex antibody].
Yamazaki et al., Niigata, Japan. In Rinsho Shinkeigaku, Dec 2013
Characteristic cellular features, including Bunina bodies in the remaining lower motor neurons and phosphorylated TAR DNA-binding protein 43-kDa (pTDP-43)-immunopositive inclusions in both upper and lower motor neuron systems, were evident.
Biochemical characterization of a phospholipase A2 from Photobacterium damselae subsp. piscicida.
Liu et al., Chi-lung, Taiwan. In Z Naturforsch C, Nov 2013
A single 43-kDa band was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
[Myositis-specific autoantibodies].
Fujimoto, Kanazawa, Japan. In Brain Nerve, Apr 2013
Moreover, a recent study suggested the presence of autoantibodies to a 43-kDa muscle protein in patients with inclusion body myositis.
[Congenital myasthenic syndromes: difficulties in the diagnosis, course and prognosis, and therapy--The French National Congenital Myasthenic Syndrome Network experience].
Membres du réseau national Syndromes Myasthéniques Congénitaux et al., Paris, France. In Rev Neurol (paris), Feb 2013
The long-term prognosis of CMS was studied in a series of 79 patients recruited with the following gene mutations: CHRNA; CHRNE; DOK7; COLQ; RAPSN; AGRN; and MUSK.
The contractile system as a negative regulator of the connexin 43 hemichannel.
Bultynck et al., Leuven, Belgium. In Biol Cell, 2012
The molecular mechanisms underlying the regulation of gap junction (GJ) channels based on the 43-kDa connexin isoform (Cx43) have been studied extensively.
Poxvirus cell entry: how many proteins does it take?
Moss, Bethesda, United States. In Viruses, 2012
Regardless of the pathway or whether the MV or EV mediates infection, fusion is dependent on 11 to 12 non-glycosylated, transmembrane proteins ranging in size from 4- to 43-kDa that are associated in a complex.
Prenatal diagnosis and genetic analysis of fetal akinesia deformation sequence and multiple pterygium syndrome associated with neuromuscular junction disorders: a review.
Chen, Taipei, Taiwan. In Taiwan J Obstet Gynecol, 2012
Genetic analysis of mutations in the neuromuscular junction genes such as CHRNA1, CHRND, CHRNG, CNTN1, DOK7, RAPSN, and SYNE1 may unveil the pathogenetic cause of fetal akinesia deformation sequence and multiple pterygium syndrome, and the information acquired is helpful for genetic counseling and clinical management.
Rapsyn mediates subsynaptic anchoring of PKA type I and stabilisation of acetylcholine receptor in vivo.
Rudolf et al., Eggenstein-Leopoldshafen, Germany. In J Cell Sci, 2012
Molecular modelling, immunoprecipitation and bimolecular fluorescence complementation approaches identify an alpha-helical stretch of rapsyn to be crucial for binding to the dimerisation and docking domain of PKA type I.
Glutamatergic neurons induce expression of functional glutamatergic synapses in primary myotubes.
Buffelli et al., Verona, Italy. In Plos One, 2011
typical anchoring proteins of central excitatory synapses coimmunoprecipitate and colocalize with rapsyn
Diagnosis of congenital myasthenic syndrome with mutation of the RAPSN gene after general anaesthesia.
Baroncini et al., Bologna, Italy. In Eur J Anaesthesiol, 2011
a mutation of the RAPSN gene may have a role in development of congenital myasthenic syndrome after general anaesthesia [case report]
Investigation for RAPSN and DOK-7 mutations in a cohort of seronegative myasthenia gravis patients.
Skeie et al., Bergen, Norway. In Muscle Nerve, 2011
Investigation of mutations in RAPSN determines that patients with congenital myasthenic syndrome can be misdiagnosed with seronegative myasthenia gravis.
Acetylcholine receptor organization in membrane domains in muscle cells: evidence for rapsyn-independent and rapsyn-dependent mechanisms.
Hovius et al., Lausanne, Switzerland. In J Biol Chem, 2011
nAChR mobility in plasma membranes of myoblast cells during their differentiation to myotubes in the presence and absence of rapsyn
A novel protein that participates in nonself discrimination of malignant cells by homologous complement.
Seya et al., Ōsaka, Japan. In Nat Med, 1997
Only malignant cells and cell lines exposed to Fas or X-irradiation stimuli produced this protein, designated M161Ag, which was an unglycosylated 43-kDa protein.
Partial purification and characterization of mRNAs encoding glycollate oxidase and catalase.
Kindl et al., Marburg an der Lahn, Germany. In Planta, 1986
Characterizing the products of in-vitro translation directed by the mRNA prepared, we observed a 43-kDa species of glycollate oxidase and a 56-kDa species of apo-catalase.
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