Search Results - (Author, Cooperation:R. Prinjha)
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1P. Ntziachristos ; A. Tsirigos ; G. G. Welstead ; T. Trimarchi ; S. Bakogianni ; L. Xu ; E. Loizou ; L. Holmfeldt ; A. Strikoudis ; B. King ; J. Mullenders ; J. Becksfort ; J. Nedjic ; E. Paietta ; M. S. Tallman ; J. M. Rowe ; G. Tonon ; T. Satoh ; L. Kruidenier ; R. Prinjha ; S. Akira ; P. Van Vlierberghe ; A. A. Ferrando ; R. Jaenisch ; C. G. Mullighan ; I. Aifantis
Nature Publishing Group (NPG)
Published 2014Staff ViewPublication Date: 2014-08-19Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Benzazepines/pharmacology ; Epigenesis, Genetic/drug effects ; Histone Demethylases/genetics/*metabolism ; Histones/chemistry/metabolism ; Jumonji Domain-Containing Histone Demethylases/antagonists & ; inhibitors/*metabolism ; Lysine/metabolism ; Methylation/drug effects ; Mice ; Precursor Cell Lymphoblastic Leukemia-Lymphoma/drug ; therapy/*enzymology/genetics/pathology ; Pyrimidines/pharmacology ; Tumor Suppressor Proteins/genetics/metabolismPublished by: -
2Prinjha, R. K. ; Shapland, C. E. ; Hsuan, J. J. ; Totty, N. F. ; Mason, I. J. ; Lawson, D.
New York, NY : Wiley-Blackwell
Published 1994Staff ViewISSN: 0886-1544Keywords: cytoskeleton ; actin binding ; transgelin sequence ; gelation ; gene family ; Life and Medical Sciences ; Cell & Developmental BiologySource: Wiley InterScience Backfile Collection 1832-2000Topics: BiologyMedicineNotes: We have used degenerate oligonucleotides, derived from the amino acid sequence of transgelin peptides [Shapland et al., 1993: J. Cell Biol. 121:1065-1073], to isolate and sequence overlapping cDNA clones encoding this actin gelling protein. Primers with 5′ restriction enzyme sites directed against the N and C terminal amino acids present in these clones were then used to amplify and clone the entire transgelin coding region from reverse transcribed rat small intestine cDNA (RT-PCR). These studies have shown that transgelin is the product of a single gene which is conserved between yeast, Drosophila, molluscs, and humans. Transgelin is expressed as a single message that is regulated at the level of transcription in SV40 transformed 3T3 cells. Our data have shown that transgelin and several other proteins of unknown function, SM22α [Pearlstone et al., 1987: J. Biol. Chem. 262:5985-5991], mouse p27 [Almendral et al., 1989: Exp. Cell Res. 181:518-530], and human WS3-10 [Thweatt et al., 1992: Biochem. Biophys. Res. Commun. 187:1-7], share extensive homology. More limited regions of homology shared between transgelin and other proteins such as rat NP25 (unpublished), chicken calponins α and β [Takahashi and Nadal-Ginard, 1991: J. Biol. Chem. 266:13284-13288], and Drosophila mp20 [Ayme-Southgate et al., 1989: J. Cell Biol. 108:521-531] suggest that all of these proteins may be classified as members of a new transgelin multigene family. © 1994 Wiley-Liss, Inc.Additional Material: 9 Ill.Type of Medium: Electronic ResourceURL: -
3Dobenecker, M.-W., Park, J. S., Marcello, J., McCabe, M. T., Gregory, R., Knight, S. D., Rioja, I., Bassil, A. K., Prinjha, R. K., Tarakhovsky, A.
Rockefeller University Press
Published 2018Staff ViewPublication Date: 2018-04-03Publisher: Rockefeller University PressPrint ISSN: 0022-1007Electronic ISSN: 1540-9538Topics: MedicineKeywords: AutoimmunityPublished by: -
4Staff View
Publication Date: 2018-07-03Publisher: Rockefeller University PressPrint ISSN: 0022-1007Electronic ISSN: 1540-9538Topics: MedicineKeywords: Infectious Disease and Host DefensePublished by: