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1 urally more aberrant than those lacking only alpha-syntrophin.
2 e and transgenic mice expressing full-length alpha-syntrophin.
3 e sarcolemma by binding to the PDZ domain of alpha-syntrophin.
4                                              Alpha-syntrophin, a protein containing one PDZ domain an
5 ith targeted disruption of the gene encoding alpha-syntrophin (alpha-Syn(-/-)) that lack the perivasc
6 in brain and skeletal muscle of mice lacking alpha-syntrophin (alpha-Syn(-/-)).
7                                              alpha-syntrophin (alpha-syn) and alpha-dystrobrevin (alp
8 ith targeted disruption of the gene encoding alpha-syntrophin (alpha-Syn) that demonstrate diminished
9                                              alpha-Syntrophin (alpha-syn), a scaffold protein, links
10 r DPC proteins, including beta-dystroglycan, alpha-syntrophin and alpha-dystrobrevin in mdx muscle.
11                        We conclude that both alpha-syntrophin and beta2-syntrophin play distinct role
12 of nNOS by the dystrophin-associated protein alpha-syntrophin and may have implications for the devel
13 rough a PDZ domain-mediated interaction with alpha-syntrophin and suggest an important role for the D
14                    The COOH-terminal half of alpha-syntrophin binds to dystrophin and related protein
15                                The Delta PDZ alpha-syntrophin displaced endogenous alpha- and beta 1-
16 trophin's rod domain and the adaptor protein alpha-syntrophin for sarcolemmal targeting.
17                                        Thus, alpha-syntrophin has an important role in synapse format
18 vestigated the function of the PDZ domain of alpha-syntrophin in vivo by generating transgenic mouse
19                                              alpha-Syntrophin is a scaffolding adapter protein expres
20 trophin were masked by compensation from the alpha-syntrophin isoform, we crossed these mice with our
21 orrect the aberrant AChR distribution of the alpha-syntrophin knock-out mice.
22 led to associate with the DGC in brains from alpha-syntrophin knockout mice.
23                   Transgenic mice expressing alpha-syntrophin lacking portions of the first pleckstri
24 ng full-length alpha-syntrophin or a mutated alpha-syntrophin lacking the PDZ domain (Delta PDZ).
25  and in transgenic mice expressing a mutated alpha-syntrophin lacking the PDZ domain (DeltaPDZ), both
26 in, but no rescue was observed in muscles of alpha-syntrophin mutants that also lacked beta1-syntroph
27 artial NMJ rescue was seen in the muscles of alpha-syntrophin mutants that expressed beta1-syntrophin
28                              The full-length alpha-syntrophin, not the Delta PDZ form, reestablished
29 ire PDZ domain (DeltaPDZ) were bred onto the alpha-syntrophin null background.
30 this hypothesis, we performed experiments in alpha-syntrophin null mice and in transgenic mice expres
31 y impaired in the contracting muscles of the alpha-syntrophin null mice and transgenic DeltaPDZ mice
32                            We have generated alpha-syntrophin null mice by targeted gene disruption t
33 sed these mice with our previously described alpha-syntrophin null mice to produce mice lacking both
34 J architecture that were observed in mdx and alpha-syntrophin null muscles.
35 l mutants, dystrophin-deficient mdx mice and alpha-syntrophin null mutants showed reductions in the c
36 oth transgenic mouse lines were bred with an alpha-syntrophin-null mouse which lacks sarcolemmal nNOS
37 ransgenic mouse lines expressing full-length alpha-syntrophin or a mutated alpha-syntrophin lacking t
38 on of muscle sodium channels, which bind the alpha-syntrophin PDZ domain in vitro, were not altered.
39                             Mice lacking the alpha-syntrophin PDZ domain or either half of the PH1 do
40 epends on the presence of a dystrophin-bound alpha-syntrophin PDZ domain.
41 to a PH domain were found to be conserved in alpha-syntrophins' PH1 domains and absent in PH2 domains
42 emonstrated that Kir4.1 can bind directly to alpha-syntrophin, requiring the presence of the last thr
43        In addition, stable overexpression of alpha-syntrophin significantly increased alpha1D-AR prot
44                                              Alpha-syntrophin specifically recognized the C terminus
45 ng, because mice deficient in dystrophin and alpha-syntrophin, which localizes neuronal nitric oxide
46 so seen in mice lacking the scaffold protein alpha-syntrophin, which manifest reduced astrocyte water
47                          We demonstrate that alpha-Syntrophin, which resides in nuclei of myocytes, f
48  We conclude that the PH1 and PDZ domains of alpha-syntrophin work in concert to facilitate the local