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Items: 1 to 20 of 236


Desmuslin, an intermediate filament protein that interacts with alpha -dystrobrevin and desmin.

Mizuno Y, Thompson TG, Guyon JR, Lidov HG, Brosius M, Imamura M, Ozawa E, Watkins SC, Kunkel LM.

Proc Natl Acad Sci U S A. 2001 May 22;98(11):6156-61. Epub 2001 May 15.


DAMAGE, a novel alpha-dystrobrevin-associated MAGE protein in dystrophin complexes.

Albrecht DE, Froehner SC.

J Biol Chem. 2004 Feb 20;279(8):7014-23. Epub 2003 Nov 17.


Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin-associated protein complex.

Poon E, Howman EV, Newey SE, Davies KE.

J Biol Chem. 2002 Feb 1;277(5):3433-9. Epub 2001 Nov 1.


Alternative splicing of dystrobrevin regulates the stoichiometry of syntrophin binding to the dystrophin protein complex.

Newey SE, Benson MA, Ponting CP, Davies KE, Blake DJ.

Curr Biol. 2000 Oct 19;10(20):1295-8.


Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle.

Newey SE, Howman EV, Ponting CP, Benson MA, Nawrotzki R, Loh NY, Davies KE, Blake DJ.

J Biol Chem. 2001 Mar 2;276(9):6645-55. Epub 2000 Oct 25.


Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins.

Leonoudakis D, Conti LR, Anderson S, Radeke CM, McGuire LM, Adams ME, Froehner SC, Yates JR 3rd, Vandenberg CA.

J Biol Chem. 2004 May 21;279(21):22331-46. Epub 2004 Mar 15.


Syncoilin accumulation in two patients with desmin-related myopathy.

Howman EV, Sullivan N, Poon EP, Britton JE, Hilton-Jones D, Davies KE.

Neuromuscul Disord. 2003 Jan;13(1):42-8.


Dysbindin, a novel coiled-coil-containing protein that interacts with the dystrobrevins in muscle and brain.

Benson MA, Newey SE, Martin-Rendon E, Hawkes R, Blake DJ.

J Biol Chem. 2001 Jun 29;276(26):24232-41. Epub 2001 Apr 20.


Beta-dystrobrevin interacts directly with kinesin heavy chain in brain.

Macioce P, Gambara G, Bernassola M, Gaddini L, Torreri P, Macchia G, Ramoni C, Ceccarini M, Petrucci TC.

J Cell Sci. 2003 Dec 1;116(Pt 23):4847-56.


Syncoilin, an intermediate filament-like protein linked to the dystrophin associated protein complex in skeletal muscle.

Moorwood C.

Cell Mol Life Sci. 2008 Oct;65(19):2957-63. doi: 10.1007/s00018-008-8306-9. Review.


Identification of alpha-syntrophin binding to syntrophin triplet, dystrophin, and utrophin.

Yang B, Jung D, Rafael JA, Chamberlain JS, Campbell KP.

J Biol Chem. 1995 Mar 10;270(10):4975-8.


Colocalization of nestin and vimentin/desmin in skeletal muscle cells demonstrated by three-dimensional fluorescence digital imaging microscopy.

Sjöberg G, Jiang WQ, Ringertz NR, Lendahl U, Sejersen T.

Exp Cell Res. 1994 Oct;214(2):447-58.


Characterisation of alpha-dystrobrevin in muscle.

Nawrotzki R, Loh NY, Ruegg MA, Davies KE, Blake DJ.

J Cell Sci. 1998 Sep;111 ( Pt 17):2595-605.


The mouse synemin gene encodes three intermediate filament proteins generated by alternative exon usage and different open reading frames.

Xue ZG, Cheraud Y, Brocheriou V, Izmiryan A, Titeux M, Paulin D, Li Z.

Exp Cell Res. 2004 Aug 15;298(2):431-44.


Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins.

Gee SH, Madhavan R, Levinson SR, Caldwell JH, Sealock R, Froehner SC.

J Neurosci. 1998 Jan 1;18(1):128-37.


Beta-synemin localizes to regions of high stress in human skeletal myofibers.

Mizuno Y, Guyon JR, Watkins SC, Mizushima K, Sasaoka T, Imamura M, Kunkel LM, Okamoto K.

Muscle Nerve. 2004 Sep;30(3):337-46.


Beta-synemin expression in cardiotoxin-injected rat skeletal muscle.

Mizuno Y, Guyon JR, Ishii A, Hoshino S, Ohkoshi N, Tamaoka A, Okamoto K, Kunkel LM.

BMC Musculoskelet Disord. 2007 May 10;8:40.


Molecular characteristics of the novel intermediate filament protein paranemin. Sequence reveals EAP-300 and IFAPa-400 are highly homologous to paranemin.

Hemken PM, Bellin RM, Sernett SW, Becker B, Huiatt TW, Robson RM.

J Biol Chem. 1997 Dec 19;272(51):32489-99.

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