Copeland O - Search Results

1

The effect of mutations in alpha-tropomyosin (E40K and E54K) that cause familial dilated cardiomyopathy on the regulatory mechanism of cardiac muscle thin filaments.

Mirza M, Robinson P, Kremneva E, Copeland O, Nikolaeva O, Watkins H, Levitsky D, Redwood C, El-Mezgueldi M, Marston S. Mirza M, et al. Among authors: copeland o. J Biol Chem. 2007 May 4;282(18):13487-97. doi: 10.1074/jbc.M701071200. Epub 2007 Mar 13. J Biol Chem. 2007. PMID: 17360712 Free article.

2

Molecular mechanism of the E99K mutation in cardiac actin (ACTC Gene) that causes apical hypertrophy in man and mouse.

Song W, Dyer E, Stuckey DJ, Copeland O, Leung MC, Bayliss C, Messer A, Wilkinson R, Tremoleda JL, Schneider MD, Harding SE, Redwood CS, Clarke K, Nowak K, Monserrat L, Wells D, Marston SB. Song W, et al. Among authors: copeland o. J Biol Chem. 2011 Aug 5;286(31):27582-93. doi: 10.1074/jbc.M111.252320. Epub 2011 May 26. J Biol Chem. 2011. PMID: 21622575 Free PMC article.

3

Investigation of changes in skeletal muscle alpha-actin expression in normal and pathological human and mouse hearts.

Copeland O, Nowak KJ, Laing NG, Ravenscroft G, Messer AE, Bayliss CR, Marston SB. Copeland O, et al. J Muscle Res Cell Motil. 2010 Sep;31(3):207-14. doi: 10.1007/s10974-010-9224-7. Epub 2010 Aug 13. J Muscle Res Cell Motil. 2010. PMID: 20706863

4

The dilated cardiomyopathy-causing mutation ACTC E361G in cardiac muscle myofibrils specifically abolishes modulation of Ca(2+) regulation by phosphorylation of troponin I.

Vikhorev PG, Song W, Wilkinson R, Copeland O, Messer AE, Ferenczi MA, Marston SB. Vikhorev PG, et al. Among authors: copeland o. Biophys J. 2014 Nov 18;107(10):2369-80. doi: 10.1016/j.bpj.2014.10.024. Biophys J. 2014. PMID: 25418306 Free PMC article.

5

OBSCN Mutations Associated with Dilated Cardiomyopathy and Haploinsufficiency.

Marston S, Montgiraud C, Munster AB, Copeland O, Choi O, Dos Remedios C, Messer AE, Ehler E, Knöll R. Marston S, et al. Among authors: copeland o. PLoS One. 2015 Sep 25;10(9):e0138568. doi: 10.1371/journal.pone.0138568. eCollection 2015. PLoS One. 2015. PMID: 26406308 Free PMC article.

6

The inhibitory complex of smooth muscle caldesmon with actin and tropomyosin involves three interacting segments of the C-terminal domain 4.

Fraser ID, Copeland O, Bing W, Marston SB. Fraser ID, et al. Among authors: copeland o. Biochemistry. 1997 May 6;36(18):5483-92. doi: 10.1021/bi962969z. Biochemistry. 1997. PMID: 9154931

7

Structure-activity studies of the regulatory interaction of the 10 kilodalton C-terminal fragment of caldesmon with actin and the effect of mutation of caldesmon residues 691-696.

Huber PA, Gao Y, Fraser ID, Copeland O, EL-Mezgueldi M, Slatter DA, Keane NE, Marston SB, Levine BA. Huber PA, et al. Among authors: copeland o. Biochemistry. 1998 Feb 24;37(8):2314-26. doi: 10.1021/bi971727b. Biochemistry. 1998. PMID: 9485378

8

Characterization of the functional properties of smooth muscle caldesmon domain 4a: evidence for an independent inhibitory actin-tropomyosin binding domain.

El-Mezgueldi M, Copeland O, Fraser ID, Marston SB, Huber PA. El-Mezgueldi M, et al. Among authors: copeland o. Biochem J. 1998 Jun 1;332 ( Pt 2)(Pt 2):395-401. doi: 10.1042/bj3320395. Biochem J. 1998. PMID: 9601068 Free PMC article.

9

Structural interactions between actin, tropomyosin, caldesmon and calcium binding protein and the regulation of smooth muscle thin filaments.

Marston S, Burton D, Copeland O, Fraser I, Gao Y, Hodgkinson J, Huber P, Levine B, el-Mezgueldi M, Notarianni G. Marston S, et al. Among authors: copeland o. Acta Physiol Scand. 1998 Dec;164(4):401-14. doi: 10.1111/j.1365-201x.1998.tb10696.x. Acta Physiol Scand. 1998. PMID: 9887964 Review.

10

The interface between caldesmon domain 4b and subdomain 1 of actin studied by nuclear magnetic resonance spectroscopy.

Gao Y, Patchell VB, Huber PA, Copeland O, El-Mezgueldi M, Fattoum A, Calas B, Thorsted PB, Marston SB, Levine BA. Gao Y, et al. Among authors: copeland o. Biochemistry. 1999 Nov 23;38(47):15459-69. doi: 10.1021/bi991383k. Biochemistry. 1999. PMID: 10569928

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