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Articles 31 - 35 of 35
Full-Text Articles in Cell and Developmental Biology
The Drosophila Melanogaster Rad54 Homolog, Dmrad54, Is Involved In The Repair Of Radiation Damage And Recombination, Rolf Kooistra, José B. M. Zonneveld, Anja De Jong, Jan C. J. Eeken, Chris J. Osgood, Jean-Marie Buerstedde, Paul H. M. Lohman, Albert Pastink
The Drosophila Melanogaster Rad54 Homolog, Dmrad54, Is Involved In The Repair Of Radiation Damage And Recombination, Rolf Kooistra, José B. M. Zonneveld, Anja De Jong, Jan C. J. Eeken, Chris J. Osgood, Jean-Marie Buerstedde, Paul H. M. Lohman, Albert Pastink
Biological Sciences Faculty Publications
The RAD54 gene of Saccharomyces cerevisiae plays a crucial role in recombinational repair of double-strand breaks in DNA. Here the isolation and functional characterization of the RAD54 homolog of the fruit fly Drosophila melanogaster, DmRAD54, are described. The putative Dmrad54 protein displays 46 to 57% identity to its homologs from yeast and mammals. DmRAD54 RNA was detected at all stages of fly development, but an increased level was observed in early embryos and ovarian tissue. To determine the function of DmRAD54, a null mutant was isolated by random mutagenesis. DmRAD54-deficient flies develop normally, but the females …
Phosphorylation Within The Amino-Terminal Acidic Domain I Of The Phosphoprotein Of Vesicular Stomatitis Virus Is Required For Transcription But Not For Replication, Asit K. Pattnaik, Leroy Hwang, Tong Le, Nathan Englund, Manjula Mathur, Tapas Das, Amiya Banerjee
Phosphorylation Within The Amino-Terminal Acidic Domain I Of The Phosphoprotein Of Vesicular Stomatitis Virus Is Required For Transcription But Not For Replication, Asit K. Pattnaik, Leroy Hwang, Tong Le, Nathan Englund, Manjula Mathur, Tapas Das, Amiya Banerjee
School of Veterinary and Biomedical Sciences: Faculty Publications
Phosphorylation by casein kinase II at three specific residues (S-60, T-62, and S-64) within the acidic domain I of the P protein of Indiana serotype vesicular stomatitis virus has been shown to be critical for in vitro transcription activity of the viral RNA polymerase (P-L) complex. To examine the role of phosphorylation of P protein in transcription as well as replication in vivo, we used a panel of mutant P proteins in which the phosphate acceptor sites in domain I were substituted with alanines or other amino acids. Analyses of the alanine-substituted mutant P proteins for the ability to support …
Assignment Of Fragile Site 8e (Fra8e) To Human Chromosome Band 8q24.11 Adjacent To The Hereditary Multiple Exostoses 1 Gene And Two Overlapping Langer-Giedion Syndrome Deletion Endpoints, April L. Hill, Y. Harada, E. Takahashi, J. Hou, M. J. Wagner, D. E. Wells
Assignment Of Fragile Site 8e (Fra8e) To Human Chromosome Band 8q24.11 Adjacent To The Hereditary Multiple Exostoses 1 Gene And Two Overlapping Langer-Giedion Syndrome Deletion Endpoints, April L. Hill, Y. Harada, E. Takahashi, J. Hou, M. J. Wagner, D. E. Wells
Biology Faculty Publications
The distamycin A inducible fragile site, FRA8E, Fra(8) (q24.11) has been previously mapped to 8q24.11, proximal to the MYC gene, by fluorescent in situ hybridization (Takahasi et al., 1991). This fragile site has been shown to be present in about 1 out of every 140 healthy Japanese individuals (Takahasi et al., 1988). To more precisely map FRA8E, we have used cosmids isolated from the Langer-Giedion chromosomal region (LGCR) for FISH analysis. Langer-Giedion syndrome (LGS) is a contiguous gene syndrome characterized by chromosome deletions in Sq24.11 (Ludecke et al., 1991). One of the genes known to be involved in the etiology …
Interleukin-2 Fusion Protein: An Investigational Therapy For Interleukin-2 Receptor Expressing Malignancies, Jean Nichols, Foss Francine, Kuzel Timothy, Lemaistre Charles Fred, Platanias Leonidas, Ratain Mark, Rook Alain, Mansoor Saleh, Schwartz Gary
Interleukin-2 Fusion Protein: An Investigational Therapy For Interleukin-2 Receptor Expressing Malignancies, Jean Nichols, Foss Francine, Kuzel Timothy, Lemaistre Charles Fred, Platanias Leonidas, Ratain Mark, Rook Alain, Mansoor Saleh, Schwartz Gary
Haematology and Oncology, East Africa
DAB3s91L-2 is an interleukin-2 receptor (IL-2R) specific fusion protein with a molecular weight of 58 kD containing the enzymatic and translocation domains of diphtheria toxin (DT) and human IL-2. This fusion protein is able to direct the cytocidal action of the DT enzymatic region only to cells which bear the IL-2R. The human IL-2R exists in three forms: low, intermediate and high affinity. The high-affinity form is believed to be the biologically relevant form on mature, activated T-lymphocytes, B-lymphocytes and monocytes. DAB3sgIL-2 is able to bind selectively to the high-affinity IL-2R in a concentration-dependent manner, and once bound is internalised …
Connexin32 And X-Linked Charcot-Marie-Tooth Disease, Kenneth H. Fischbeck, Suzanne M. Deschênes, Linda Jo Bone, Steven S. Scherer
Connexin32 And X-Linked Charcot-Marie-Tooth Disease, Kenneth H. Fischbeck, Suzanne M. Deschênes, Linda Jo Bone, Steven S. Scherer
Biology Faculty Publications
This paper deals with the genetic defect responsible for the X-linked form of Charcot-Marie-Tooth disease.Mutations in the gap junction geneconnexin32(Cx32) cause the X-linked form of Charcot–Marie–Tooth disease, an inherited demyelinating neuropathy.