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1 cetylcholine receptor complex as well as the dystrophin glycoprotein complex.
2 cles, indicating compromised assembly of the dystrophin glycoprotein complex.
3 can (alpha-DG), an integral component of the dystrophin glycoprotein complex.
4 le diseases that arise due to defects in the dystrophin glycoprotein complex.
5 ibers and, along with DMD, forms part of the dystrophin-glycoprotein complex.
6 roglycan (alpha-DG), an integral part of the dystrophin-glycoprotein complex.
7 aining for laminin-2 and for proteins of the dystrophin-glycoprotein complex.
8 ith the hope of finding novel members of the dystrophin-glycoprotein complex.
9 integrally associated with sarcospan in the dystrophin-glycoprotein complex.
10 the sarcolemma, where it associates with the dystrophin-glycoprotein complex.
11 asma membrane), where it associates with the dystrophin-glycoprotein complex.
12 s an integral component of the smooth muscle dystrophin-glycoprotein complex.
13 (nNOS) is anchored to the sarcolemma via the dystrophin-glycoprotein complex.
14 hy gene, resulted in the purification of the dystrophin-glycoprotein complex.
15 of electrophoretically separated and blotted dystrophin-glycoprotein complex.
16 her capacity than was observed with purified dystrophin-glycoprotein complex.
17 rification readily dissociates nNOS from the dystrophin-glycoprotein complex.
18 ed by genetic and biochemical defects of the dystrophin-glycoprotein complex.
19 Sspn encodes a protein in the dystrophin-glycoprotein complex.
20 x-binding protein and a key component of the dystrophin-glycoprotein complex.
21 ld protein, links signaling molecules to the dystrophin-glycoprotein complex.
22 s directly or indirectly associated with the dystrophin-glycoprotein complex.
23 KRP coexists with dystroglycan in the native dystrophin-glycoprotein complex.
24 of dystroglycan from within the sarcolemmal dystrophin-glycoprotein complex.
25 ion, and unaltered levels of proteins in the dystrophin-glycoprotein complex.
26 dystroglycan, an important component of the dystrophin-glycoprotein complex.
27 expression and successful restoration of the dystrophin-glycoprotein complex.
28 e dystrophin gene that result in loss of the dystrophin-glycoprotein complex, a laminin receptor that
29 uses recruitment of Src family kinase to the dystrophin glycoprotein complex, activating Rac1 and ind
30 xtracellular matrix binding component of the dystrophin-glycoprotein complex, alpha-dystroglycan (alp
31 the dysferlin-deficient mice have an intact dystrophin glycoprotein complex and normal levels of cav
32 al lamina using two distinct mechanisms: the dystrophin glycoprotein complex and the alpha 7 beta 1 i
34 cialized membrane micro-domains in which the dystrophin-glycoprotein complex and cellular signaling m
35 ed on the sarcolemma, where it assembled the dystrophin-glycoprotein complex and completely prevented
36 itive myofibers, with biochemically restored dystrophin-glycoprotein complex and improved contractile
37 odystrophin expression restored the critical dystrophin-glycoprotein complex and improved sarcolemma
38 us, nNOS is not an integral component of the dystrophin-glycoprotein complex and is not simply anothe
40 by Large(myd) muscles, which have an intact dystrophin-glycoprotein complex and lack only the lamini
41 l muscle of patients with disruptions in the dystrophin-glycoprotein complex and patients with a clin
46 dystroglycan in disease models involving the dystrophin-glycoprotein complex, and sarcolemmal FKRP im
47 eric actin and the sarcolemma, assembles the dystrophin-glycoprotein complex, and significantly slows
48 chanism that involves the disassembly of the dystrophin-glycoprotein complex, and Yap- and ERK-mediat
49 ic dysbindin-1 reductions independent of the dystrophin glycoprotein complex are frequent in schizoph
50 s a set of membrane-associated proteins (the dystrophin-glycoprotein complex) as well as gamma-actin
51 can C-terminal domain is sufficient only for dystrophin-glycoprotein complex assembly, but to prevent
52 ophin deficiencies result in the loss of the dystrophin-glycoprotein complex at the plasma membrane,
53 ly consistent with the 1:24 stoichiometry of dystrophin-glycoprotein complex binding to F-actin previ
57 at dysferlin-null mice maintain a functional dystrophin-glycoprotein complex but nevertheless develop
58 in the dysferlin gene and disruption of the dystrophin-glycoprotein complex can lead to the accumula
59 ions in the genes encoding components of the dystrophin-glycoprotein complex cause muscular dystrophy
60 ay, we demonstrated that perturbation of the dystrophin-glycoprotein complex caused extensive fiber d
61 Binding of laminin to dystroglycan in the dystrophin glycoprotein complex causes signaling through
63 cule laminin alpha2 chain interacts with the dystrophin-glycoprotein complex, contributes to normal m
64 cospan co-localizes and co-purifies with the dystrophin-glycoprotein complex, demonstrating that it i
65 ystrophin loss also leads to the loss of the dystrophin glycoprotein complex (DGC) from the sarcolemm
69 cular dystrophy due to the disruption of the dystrophin glycoprotein complex (DGC), which anchors neu
72 n, that provides the key linkage between the dystrophin-glycoprotein complex (DGC) and laminin in ske
73 e, defects in processing and assembly of the dystrophin-glycoprotein complex (DGC) are associated wit
75 s and the major components of the junctional dystrophin-glycoprotein complex (DGC) colocalized with a
76 nin alpha4 chain did not alter the levels of dystrophin-glycoprotein complex (DGC) components or affe
77 pan is an integral membrane component of the dystrophin-glycoprotein complex (DGC) found at the sarco
78 tations of genes that encode proteins in the dystrophin-glycoprotein complex (DGC) frequently involve
79 ult in the loss of dystrophin and the entire dystrophin-glycoprotein complex (DGC) from the sarcolemm
81 tic defects in a number of components of the dystrophin-glycoprotein complex (DGC) lead to distinct f
85 rophin and are components of a transmembrane dystrophin-glycoprotein complex (DGC) that links the cyt
87 lt from genetic defects in components of the dystrophin-glycoprotein complex (DGC), a multimeric comp
88 Dystroglycan is a central component of the dystrophin-glycoprotein complex (DGC), a protein assembl
90 cle isoform of dystrophin that assembles the dystrophin-glycoprotein complex (DGC), but lacks actin-b
91 skeleton to the extracellular matrix via the dystrophin-glycoprotein complex (DGC), exhibit muscular
92 a result of a genetic disruption within the dystrophin-glycoprotein complex (DGC), is thought to ind
93 hy is frequently caused by disruption of the dystrophin-glycoprotein complex (DGC), which links muscl
102 more, high speed cosedimentation analysis of dystrophin-glycoprotein complex digested with calpain re
103 (DTNBP1) and may thus be associated with the dystrophin glycoprotein complex found at certain postsyn
104 myopathic changes; (ii) an exclusion of the dystrophin-glycoprotein complex from lipid raft domains;
105 is not clear if the remaining members of the dystrophin-glycoprotein complex further protect laminin
106 fragments of dystrophin or calpain-digested dystrophin-glycoprotein complex had no effect on F-actin
108 yopathy is a multifactorial disease, and the dystrophin-glycoprotein complex has been implicated in t
109 Dystroglycan is a central component of the dystrophin-glycoprotein complex implicated in the pathog
110 cription and, consequently, stability of the Dystrophin-glycoprotein complex important for cardiomyoc
111 ystroglycan is a member of the transmembrane dystrophin glycoprotein complex in muscle that binds to
112 Recent insights into the involvement of the dystrophin glycoprotein complex in muscular dystrophy su
113 ed membrane integrity and restoration of the dystrophin glycoprotein complex in vitro and in vivo.
114 troglycan (DAG1) gene results in loss of the dystrophin-glycoprotein complex in differentiated muscle
115 anscription, expression, and function of the dystrophin-glycoprotein complex in skeletal and cardiac
121 that the native molecular weight of purified dystrophin-glycoprotein complex is only large enough (Mr
122 mice reveals that AQP4 is lost even when the dystrophin-glycoprotein complex is present, suggesting t
123 s pathway, but either integrin alpha7 or the dystrophin-glycoprotein complex is required in conjuncti
124 ly only alpha-dystroglycan (alpha-DG) of the dystrophin-glycoprotein complex is well characterized as
125 tracellular and transmembrane protein of the dystrophin-glycoprotein complex, is at the center of mol
126 sarcolemma through its interactions with the dystrophin-glycoprotein complex, is dramatically reduced
127 obrevin (DB), a cytoplasmic component of the dystrophin-glycoprotein complex, is found throughout the
128 phic symptoms or membrane instability in the dystrophin-glycoprotein complex-lacking Scgd (delta-sarc
129 dystrophin results in disruption of a large dystrophin glycoprotein complex, leading to pathological
130 uct which optimally restores proteins of the dystrophin glycoprotein complex may have therapeutic app
131 ows striking similarities with phenotypes of dystrophin glycoprotein complex mutants, including patie
133 sh lacking either a primary component of the dystrophin-glycoprotein complex or integrin alpha7.
134 AD+ supplementation ameliorates dystrophy in dystrophin-glycoprotein complex- or integrin alpha7-defi
135 res of striated muscle and copurify with the dystrophin-glycoprotein complex, perhaps through the int
136 arcoglycans, a subset of proteins within the dystrophin-glycoprotein complex, produce a limb-girdle m
137 acked alpha-dystrobrevin, a component of the dystrophin-glycoprotein complex, rates of AChR turnover,
139 ature of dystrobrevin's association with the dystrophin glycoprotein complex remains unclear, it is k
140 ferent approaches, we also demonstrated that dystrophin-glycoprotein complex significantly protected
141 highly glycosylated component of the muscle dystrophin-glycoprotein complex that is also expressed i
142 s are known as an integral subcomplex of the dystrophin glycoprotein complex, the function of which i
143 ctivity by tightly binding the transmembrane dystrophin-glycoprotein complex to the extracellular mat
145 nt in alpha-dystrobrevin, a component of the dystrophin glycoprotein complex, we found that the densi
146 diomyopathy associated with mutations of the dystrophin-glycoprotein complex, we analyzed genetically
147 s were functional in vivo, as members of the dystrophin glycoprotein complex were restored in muscle
148 cross-linking properties of skeletal muscle dystrophin-glycoprotein complex were examined using high
149 letal muscle as an integral component of the dystrophin glycoprotein complex, which is critical for m
150 oglycans are transmembrane components of the dystrophin-glycoprotein complex, which links the cytoske
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