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Different obscurin isoforms localize to distinct sites at sarcomeres

dc.contributor.authorBowman, Amber L.en_US
dc.contributor.authorKontrogianni-Konstantopoulos, Aikaterinien_US
dc.contributor.authorHirsch, Sara S.en_US
dc.contributor.authorGeisler, Sarah B.en_US
dc.contributor.authorGonzalez-Serratos, Hugoen_US
dc.contributor.authorRussell, Mark W.en_US
dc.contributor.authorBloch, Robert J.en_US
dc.date.accessioned2016-01-04T20:51:45Z
dc.date.available2016-01-04T20:51:45Z
dc.date.issued2007-04-17en_US
dc.identifier.citationBowman, Amber L.; Kontrogianni-Konstantopoulos, Aikaterini; Hirsch, Sara S.; Geisler, Sarah B.; Gonzalez-Serratos, Hugo; Russell, Mark W.; Bloch, Robert J. (2007). "Different obscurin isoforms localize to distinct sites at sarcomeres." FEBS Letters 581(8): 1549-1554.en_US
dc.identifier.issn0014-5793en_US
dc.identifier.issn1873-3468en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/116335
dc.publisherWiley Periodicals, Inc.en_US
dc.subject.otherObscurinen_US
dc.subject.otherI-banden_US
dc.subject.otherZ-disken_US
dc.subject.otherM-lineen_US
dc.subject.otherStretchen_US
dc.titleDifferent obscurin isoforms localize to distinct sites at sarcomeresen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Pediatrics and Communicable Diseases, University of Michigan, Ann Arbor, MI, USAen_US
dc.contributor.affiliationotherDepartment of Physiology, University of Maryland School of Medicine, 655 W. Baltimore St, MD 21201, USAen_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/116335/1/feb2s0014579307002669.pdf
dc.identifier.doi10.1016/j.febslet.2007.03.011en_US
dc.identifier.sourceFEBS Lettersen_US
dc.identifier.citedreferenceJ.V. Frangioni, B.G. Neel, Solubilization and purification of enzymatically active glutathione S -transferase (pGEX) fusion proteins. Anal. Biochem., 210,( 1993 ), 179 – 187.en_US
dc.identifier.citedreferenceP. Young, E. Ehler, M. Gautel, Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly. J. Cell Biol., 154,( 2001 ), 123 – 136.en_US
dc.identifier.citedreferenceM.W. Russell, M.O. Raeker, K.A. Korytkowski, K.J. Sonneman, Identification, tissue expression and chromosomal localization of human Obscurin-MLCK, a member of the titin and Dbl families of myosin light chain kinases. Gene, 282,( 2002 ), 237 – 246.en_US
dc.identifier.citedreferenceM.L. Bang, T. Centner, F. Fornoff, A.J. Geach, M. Gotthardt, M. McNabb, C.C. Witt, D. Labeit, C.C. Gregorio, H. Granzier, S. Labeit, The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system. Circ. Res., 89,( 2001 ), 1065 – 1072.en_US
dc.identifier.citedreferenceA. Fukuzawa, S. Idowu, M. Gautel, Complete human gene structure of obscurin: implications for isoform generation by differential splicing. J. Muscle Res. Cell Motil., 26,( 2006 ), 427 – 434.en_US
dc.identifier.citedreferenceA. Kontrogianni-Konstantopoulos, R.J. Bloch, Obscurin: a multitasking muscle giant. J. Muscle Res. Cell Motil., 26,( 2006 ), 419 – 426.en_US
dc.identifier.citedreferenceS.B. Sutter, M.O. Raeker, A.B. Borisov, M.W. Russell, Orthologous relationship of obscurin and Unc-89: phylogeny of a novel family of tandem myosin light chain kinases. Dev. Genes Evol., 214,( 2004 ), 352 – 359.en_US
dc.identifier.citedreferenceP. Bagnato, V. Barone, E. Giacomello, D. Rossi, V. Sorrentino, Binding of an ankyrin-1 isoform to obscurin suggests a molecular link between the sarcoplasmic reticulum and myofibrils in striated muscles. J. Cell Biol., 160,( 2003 ), 245 – 253.en_US
dc.identifier.citedreferenceA.B. Borisov, A. Kontrogianni-Konstantopoulos, R.J. Bloch, M.V. Westfall, M.W. Russell, Dynamics of obscurin localization during differentiation and remodeling of cardiac myocytes: obscurin as an integrator of myofibrillar structure. J. Histochem. Cytochem., 52,( 2004 ), 1117 – 1127.en_US
dc.identifier.citedreferenceA. Kontrogianni-Konstantopoulos, E.M. Jones, D.B. Van Rossum, R.J. Bloch, Obscurin is a ligand for small ankyrin 1 in skeletal muscle. Mol. Biol. Cell, 14,( 2003 ), 1138 – 1148.en_US
dc.identifier.citedreferenceA.B. Borisov, M.O. Raeker, A. Kontrogianni-Konstantopoulos, K. Yang, D.M. Kurnit, R.J. Bloch, M.W. Russell, Rapid response of cardiac obscurin gene cluster to aortic stenosis: differential activation of Rho-GEF and MLCK and involvement in hypertrophic growth. Biochem. Biophys. Res. Commun., 310,( 2003 ), 910 – 918.en_US
dc.identifier.citedreferenceA. Kontrogianni-Konstantopoulos, D.H. Catino, J.C. Strong, R.J. Bloch, De novo myofibrillogenesis in C2C12 cells: evidence for the independent assembly of M bands and Z disks. Am. J. Physiol. Cell Physiol., 290,( 2006 ), C626 – C637.en_US
dc.identifier.citedreferenceA. Kontrogianni-Konstantopoulos, D.H. Catino, J.C. Strong, S. Sutter, A.B. Borisov, D.W. Pumplin, M.W. Russell, R.J. Bloch, Obscurin modulates the assembly and organization of sarcomeres and the sarcoplasmic reticulum. FASEB J., 20,( 2006 ), 2102 – 2111.en_US
dc.identifier.citedreferenceT.M. Small, K.M. Gernert, D.B. Flaherty, K.B. Mercer, M. Borodovsky, G.M. Benian, Three new isoforms of Caenorhabditis elegans UNC-89 containing MLCK-like protein kinase domains. J. Mol. Biol., 342,( 2004 ), 91 – 108.en_US
dc.identifier.citedreferenceM.E. Mercado-Pimentel, N.C. Jordan, G.O. Aisemberg, Affinity purification of GST fusion proteins for immunohistochemical studies of gene expression. Protein Exp. Purif., 26,( 2002 ), 260 – 265.en_US
dc.identifier.citedreferenceM.O. Raeker, F. Su, S.B. Geisler, A.B. Borisov, A. Kontrogianni-Konstantopoulos, S.E. Lyons, M.W. Russell, Obscurin is required for the lateral alignment of striated myofibrils in zebrafish. Dev. Dyn., 235,( 2006 ), 2018 – 2029.en_US
dc.identifier.citedreferenceA. Kontrogianni-Konstantopoulos, D.H. Catino, J.C. Strong, W.R. Randall, R.J. Bloch, Obscurin regulates the organization of myosin into A bands. Am. J. Physiol. Cell Physiol., 287,( 2004 ), C209 – C217.en_US
dc.identifier.citedreferenceL.M. Brown, H. Gonzalez-Serratos, A.F. Huxley, Sarcomere and filament lengths in passive muscle fibres with wavy myofibrils. J. Muscle Res. Cell Motil., 5,( 1984 ), 293 – 314.en_US
dc.identifier.citedreferenceL.M. Brown, H. Gonzalez-Serratos, A.F. Huxley, Structural studies of the waves in striated muscle fibres shortened passively below their slack length. J. Muscle Res. Cell Motil., 5,( 1984 ), 273 – 292.en_US
dc.identifier.citedreferenceA.B. Borisov, S.B. Sutter, A. Kontrogianni-Konstantopoulos, R.J. Bloch, M.V. Westfall, M.W. Russell, Essential role of obscurin in cardiac myofibrillogenesis and hypertrophic response: evidence from small interfering RNA-mediated gene silencing. Histochem. Cell Biol., 125,( 2006 ), 227 – 238.en_US
dc.identifier.citedreferenceW.A. Linke, M. Ivemeyer, N. Olivieri, B. Kolmerer, J.C. Ruegg, S. Labeit, Towards a molecular understanding of the elasticity of titin. J. Mol. Biol., 261,( 1996 ), 62 – 71.en_US
dc.identifier.citedreferenceG. Faulkner, G. Lanfranchi, G. Valle, Telethonin and other new proteins of the Z-disc of skeletal muscle. IUBMB Life, 51,( 2001 ), 275 – 282.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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