Dipak K. Dube

SUNY Upstate Medical University

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Syamalima Dube

SUNY Upstate Medical University

Bernard J. Poiesz

SUNY Upstate Medical University

Larry F. Lemanski

Texas A&M University – Commerce

Robert W. Zajdel

SUNY Upstate Medical University

Jean M. Sanger

SUNY Upstate Medical University

Joseph W. Sanger

SUNY Upstate Medical University

Lynn Abbott

SUNY Upstate Medical University

Jushuo Wang

SUNY Upstate Medical University

Yingli Fan

SUNY Upstate Medical University

Sharon L. Lemanski

Temple University

Cooperative Institutions

SUNY Upstate Medical University

State University of New York

Syracuse University

University of Calcutta

University of Pennsylvania

University of Washington

National Institutes of Health

Fox Chase Cancer Center

Florida Atlantic University

University of Cincinnati Medical Center

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Selection of new biological activities from random nucleotide sequences: evolutionary and practical considerations

Genome (1989)

Marshall S. Horwitz Dipak K. Dube Lawrence A. Loeb

Recent advances in the selection of biologically active DNA sequences from random populations are reviewed. Within the framework of evolution, forces are considered that have precluded the testing of all possible DNA sequences, purely with regard to their functionality as genetic regulatory elements or protein coding sequences. Examples are drawn from cassette mutagenesis of enzyme active sites, protein domain replacement by fusion with random genomic digests, and the selection of bacterial promoters from random DNA. Efforts to derive new activities are examined, and the likelihood of future success is evaluated.Key words: active DNA, nucleotide permutation, DNA evolution.

Molecular evolution

10.1139/g89-021

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Citations (17)

Molecular and immunohistochemical analyses of cardiac troponin T during cardiac development in the Mexican axolotl, Ambystoma mexicanum

Journal of Cellular Biochemistry (2008)

C. Zhang Kristian Pietras Gian Franco Sferrazza Pingping Jia Gagani Athauda

Abstract The article to which this erratum refers was published in J. Cell. Biochem. 100:1–15. (2007), 2008 Wiley‐Liss, Inc.

Ambystoma mexicanum

10.1002/jcb.21718

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Citations (0)

Sheep heart RNA stimulates myofibril formation and beating in cardiac mutant axolotl hearts in organ culture

Anatomy and Embryology (2003)

Chi Zhang Sherrie M. LaFrance Sharon L. Lemanski Xupei Huang Dipak K. Dube

Myofibril

Ambystoma mexicanum

Embryonic heart

10.1007/s00429-002-0307-0

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Citations (2)

The Heart of Metamorphosing Mexican Axolotl but Not That of the Cardiac Mutant Is Associated with the Upregulation ofHox A5

Biochemical and Biophysical Research Communications (1998)

Arun Gaur Rajula Bhatia Elinor Spring-Mills Larry F. Lemanski Dipak K. Dube

10.1006/bbrc.1998.8514

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Citations (5)

Assembly and Maintenance of Myofibrils in Striated Muscle

Handbook of experimental pharmacology (2016)

Joseph W. Sanger Jushuo Wang Yingli Fan Jennifer White Lei Mi‐Mi

Myofibril

Myofilament

10.1007/164_2016_53

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Citations (80)

Clock is not a component of Z‐bands

Cytoskeleton (2012)

Jushuo Wang Dipak K. Dube Jennifer White Yingli Fan Jean M. Sanger

Abstract The process of Z‐band assembly begins with the formation of small Z‐bodies composed of a complex of proteins rich in alpha‐actinin. As additional proteins are added to nascent myofibrils, Z‐bodies are transformed into continuous bands that form coherent discs of interacting proteins at the boundaries of sarcomeres. The steps controlling the transition of Z‐bodies to Z‐bands are not known. The report that a circadian protein, Clock, was localized in the Z‐bands of neonatal rat cardiomyocytes raised the question whether this transcription factor could be involved in Z‐band assembly. We found that the anti‐Clock antibody used in the reported study also stained the Z‐bands and Z‐bodies of mouse and avian cardiac and skeletal muscle cells. YFP constructs of Clock that were assembled, however, did not localize to the Z‐bands of muscle cells. Controls of Clock's activity showed that cotransfection of muscle cells with pYFP‐Clock and pCeFP‐BMAL1 led to the expected nuclear localization of YFP‐Clock with its binding partner CeFP‐BMAL1. Neither CeFP‐BMAL1 nor antibodies directed against BMAL1 localized to Z‐bands. A bimolecular fluorescence complementation assay (VC–BMAL1 and VN–Clock) confirmed the absence of Clock and BMAL1 from Z‐bands, and their nuclear colocalization. A second anti‐Clock antibody stained nuclei, but not Z‐bands, of cells cotransfected with Clock and BMAL1 plasmids. Western blots of reactions of muscle extracts and purified alpha‐actinins with the two anti‐Clock antibodies showed that the original antibody cross‐reacted with alpha‐actinin and the second did not. These results cannot confirm Clock as an active component of Z‐bands. © 2012 Wiley Periodicals, Inc

Colocalization

10.1002/cm.21058

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Citations (14)

Expression of Myotilin During Chicken Development

The Anatomical Record (2014)

Dipak K. Dube Jushuo Wang Christopher D. Pellenz Yingli Fan Syamalima Dube

ABSTRACT Several missense mutations in the Z‐band protein, myotilin, have been implicated in human muscle diseases such as myofibrillar myopathy, spheroid body myopathy, and distal myopathy. Recently, we have reported the cloning of chicken myotilin cDNA. In this study, we have investigated the expression of myotilin in cross‐striated muscles from developing chicken by qRT‐PCR and in situ hybridizations. In situ hybridization of embryonic stages shows myotilin gene expression in heart, somites, neural tissue, eyes and otocysts. RT‐PCR and qRT‐PCR data, together with in situ hybridization results point to a biphasic transcriptional pattern for MYOT gene during early heart development with maximum expression level in the adult. In skeletal muscle, the expression level starts decreasing after embryonic day 20 and declines in the adult skeletal muscles. Western blot assays of myotilin in adult skeletal muscle reveal a decrease in myotilin protein compared with levels in embryonic skeletal muscle. Our results suggest that MYOT gene may undergo transcriptional activation and repression that varies between tissues in developing chicken. We believe this is the first report of the developmental regulation on myotilin expression in non‐mammalian species. Anat Rec, 297:1596–1603, 2014. © 2014 Wiley Periodicals, Inc.

10.1002/ar.22778

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Citations (3)

Downregulation of N1 gene expression inhibits the initial heartbeating and heart development in axolotls

Tissue and Cell (2004)

C Zhang Fanyin Meng Xupei Huang Robert W. Zajdel Sharon L. Lemanski

Embryonic heart

10.1016/j.tice.2003.10.003

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Citations (4)

Analysis of Milk-Based Infant Formula. Phase IV. Iodide, Linoleic Acid, and Vitamins D and K: U.S. Food and Drug Administration-Infant Formula Council: Collaborative Study

Journal of AOAC International (1993)

James T. Tanner Stephen Barnett Mardi K Mountford Stephen Barnett J.L. Beare-Rogers

Abstract In 1982, the U.S. Food and Drug Administration, the Infant Formula Council and its member companies, contract laboratories, and other government laboratories began a study of analytical methods for the nutrients listed in the Infant Formula Act of 1980. Phases I, II, III, and V have been completed. The present report provides data on Phase IV, in which 13 laboratories collaboratively studied an ion-selective electrode method for analyzing iodide, a gas chromatographic method for linoleic acid, and 2 liquid chromatographic (LC) methods each for vitamins D and K. Data were insufficient to evaluate one each of the LC methods studied for vitamins K and D. The relative standard deviations (RSD) are sufficient for the nutrient levels found in infant formula. RSDs (%) for repeatability (RSDr) and reproducibility (RSDR), respectively, were as follows: iodide, 4.0-11.4 and 13.5-18.2; linoleic acid, 1.0-1.6 and 3.5-5.1; vitamin K1, 3.2-16.0 and 6.2-19.4; and vitamin D3,4.2 and 35.0. The recommendation to adopt the method for vitamin D was supported by the results of a ministudy. All laboratories were capable of using these methods with little training. The methods for determination of iodide, linoleic acid, and vitamins D and K in ready-to-feed milkbased infant formula have been adopted first action by AOAC International.

Repeatability

10.1093/jaoac/76.5.1042

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Citations (14)

Extracellular cellulolytic enzyme system of Aspergillus japonicus: 1. Effect of different carbon sources

Enzyme and Microbial Technology (1988)

Arunik Sanyal Ramendra K. Kundu Sandip N. Sinha Dipak K. Dube

Carbon fibers

10.1016/0141-0229(88)90003-8

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Citations (14)