William Kronert's Home Page: Publications Section

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Publications from William Kronert

Kronert WA, Melkani GC, Melkani A, Bernstein SI. (2015) Failure to Communicate MYOSIN RESIDUES INVOLVED IN HYPERTROPHIC CARDIOMYOPATHY AFFECT INTERDOMAIN INTERACTION. J Biol Chem. 290: 29270–29280.

Kooij V, Viswanathan MC, Lee DI, Rainer PP, Schmidt W, Kronert WA, Harding SE, Kass DA, Bernstein SI, Van Eyk JE, Cammarato A. (2016) Profilin modulates sarcomeric organization and mediates cardiomyocyte hypertrophy. Cardiovasc Res. 110(2):238-48.

William A. Kronert, Girish C. Melkani, Anju Melkani, and Sanford I. Bernstein (2014) Mapping Interactions Between Myosin Relay and Converter Domains that Power Muscle Function. J Biol Chem. Mar 13

Kronert WA, Melkani GC, Melkani A, Bernstein SI. (2012) Alternative relay and converter domains tune native muscle myosin isoform function in Drosophila. J Mol Biol. 416:543-557.

Wang Y, Melkani GC, Suggs JA, Melkani A, Kronert WA, Cammarato A, Bernstein SI. (2012) Expression of the inclusion body myopathy 3 mutation in Drosophila depresses myosin function and stability and recapitulates muscle inclusions and weakness. Mol Biol Cell. 23:2057-65.

Lee, C. F., G. C. Melkani, Q. Yu, J. A. Suggs, W. A. Kronert, Y. Suzuki, L. Hipolito, M. G. Price, H. F. Epstein and S. I. Bernstein (2011) Drosophila UNC-45 accumulates in embryonic blastoderm and in muscles and is essential for muscle myosin stability. J. Cell Sci. 24: 699-705.

Kronert, W. A., G. C. Melkani, A. Melkani and S. I. Bernstein (2010) Mutating the converter-relay interface of Drosophila myosin perturbs ATPase activity, actin motility, myofibril stability and flight ability. J. Mol. Biol. 398: 625-632.

Kronert, W. A., C. M. Dambacher, A. F. Knowles, D. M. Swank and S. I. Bernstein. (2008) Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function. J. Mol. Biol. 379:443-456.

Cammarato, A., C. M. Dambacher, A. F. Knowles, W. A. Kronert, R. Bodmer, K. Ocorr and S. I. Bernstein. (2008) Myosin transducer mutations differentially affect motor function, myofibril structure and the performance of skeletal and cardiac muscles. Mol. Biol. Cell 19:553-562.

Yang, C., S. Ramanath, W. A. Kronert, S. I. Bernstein, D. W. Maughan, D. M. Swank. (2008) Alternative versions of the myosin relay domain differentially respond to load to influence Drosophila muscle kinetics. Biophys. J. 95:5228-5237.

Suggs, J. A., A. Cammarato, W. A. Kronert, M. Nikkhoy, C. M. Dambacher, A. Megighian and S. I. Bernstein. (2007) Alternative S2 hinge regions of the myosin rod differentially affect muscle function, myofibril dimensions and myosin tail length. J. Mol. Biol. 367: 1312-1329.

Liu, H., M. S. Miller, D. M. Swank, W. A. Kronert, D. W. Maughan, and S. I. Bernstein. (2005) Paramyosin phosphorylation site disruption affects indirect flight muscle stiffness and power generation in Drosophila melanogaster. Proc. Natl. Acad. Sci. U.S.A. 102: 10522-10527.

Swank, D.M., W.A. Kronert, S.I. Bernstein and D.W. Maughan. (2004) Alternative N-terminal regions of Drosophila myosin heavy chain tune cross-bridge kinetics for optimal muscle power output. Biophys. J. 87: 1805-1814.

Swank, D. M., A. F. Knowles, W. A. Kronert, J. A. Suggs, G. Morrill, M. Nikkhoy, G. G. Manipon, and S. I. Bernstein. (2003) Variable N-terminal regions of muscle myosin heavy chain modulate ATPase rate and actin sliding velocity. J. Biol. Chem. 278: 17475-17482.

Swank, D.M., L. Wells, W.A. Kronert, G.E. Morrill and S.I. Bernstein. (2000) Determining structure/function relationships for sarcomeric myosin heavy chain by genetic and transgenic manipulation of Drosophila. Microsc. Res. Tech. 50: 430-442.

Kronert, W.A., A. Acebes, A. Ferrus and S.I. Bernstein. (1999) Specific myosin heavy chain mutations suppress troponin I defects in Drosophila muscles. J. Cell Biol. 144: 989-1000.

Kronert, W.A., P.T. O'Donnell, A. Fieck, A. Lawn, J.O. Vigoreaux, J.C. Sparrow and S.I. Bernstein. (1995) Defects in the Drosophila myosin rod permit sarcomere assembly but cause flight muscle degeneration. J. Mol. Biol. 249: 111-125.

Cripps, R.M., K.D. Becker, M. Mardahl, W.A. Kronert, D. Hodges and S.I. Bernstein. (1994) Transformation of Drosophila melanogaster with the wild-type myosin heavy chain gene: rescue of mutant phenotypes and analysis of defects caused by overexpression. J. Cell Biol. 126: 689-699.

Kronert, W.A., P.T. O'Donnell and S.I. Bernstein. (1994) A charge change in an evolutionarily-conserved region of the myosin globular head prevents myosin and thick filament accumulation in Drosophila. J. Mol. Biol. 236: 697-702.

Kronert, W.A., K.A. Edwards, E.S. Roche, L. Wells and S.I. Bernstein. (1991) Muscle-specific accumulation of Drosophila myosin heavy chains: a splicing mutation in an alternative exon results in an isoform substitution. EMBO J. 10: 2479-2488.

Collier, V.L., W.A. Kronert, P.T. O'Donnell, K.A. Edwards and S.I. Bernstein. (1990) Alternative myosin hinge regions are utilized in a tissue-specific fashion that correlates with muscle contraction speed. Genes & Dev. 4: 885-895.

Hess, N., W.A. Kronert and S.I. Bernstein (1989) Transcriptional and post-transcriptional regulation of Drosophila myosin heavy chain gene expression. In: Cellular and Molecular Biology of Muscle Development (L. Kedes and F. Stockdale, eds.) A.R. Liss, New York 621-631.

Johnson, G.G., W.A. Kronert, S.I. Bernstein, V.M. Chapman and K.D. Smith. (1988) Altered turnover of allelic variants of HPRT is associated with N-terminal amino acid sequence variation. J. Biol. Chem. 263:9079-9082.

Wassenberg II, D.R., W.A. Kronert, P.T. O'Donnell and S.I. Bernstein. (1987) Analysis of the 5' end of the Drosophila muscle myosin heavy chain gene: alternatively spliced transcripts initiate at a single site and intron locations are conserved compared to myosin genes of other organisms. J. Biol. Chem. 262:10741-10747.


Note: Entrez Medline - entries for a particular Author name may correspond with multiple authors with the same initials. Also, the list is limited to entries stored in the Entrez Medline Database and may not accurately reflect the true number of publications. You may also read the abstracts to the publications from this inquire.


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