Results 191 to 200 of about 51,882 (244)

The CoREST Complex Regulates Alternative Splicing by the Transcriptional Regulation of RNA Processing Genes in Melanoma Cells. [PDF]

Cells
Khan AA, Aptekmann AA, Min D, Povelaitis MC, Lee S, Ryu B.   +5 more
europepmc   +1 more source

Prostaglandin F_2α stimulates the growth of human intermediate hair follicles in <i>ex vivo</i> organ culture with potential clinical relevance. [PDF]

Front Physiol
Miranda BH, Khidhir KG, Tobin DJ.
europepmc   +1 more source

Some of the next articles are maybe not open access.

Related searches:

Leukemic Transformation with Avian Myeloblastosis Virus: Present Status

Current Topics in Microbiology and Immunology, 1975
Many RNA and DNA tumor viruses induce neoplastic transformation in vitro, but few of these are leukemia viruses acting on hematopoietic target cells. The virus of avian myeloblastosis (AMV) is such an agent, capable of producing morphological changes in hematopoietic tissues grown in vitro, and thus provides an excellent model to study leukemia ...
C. Moscovici
openaire   +3 more sources

Functional expression of the reverse transcriptase αβ heterodimer from avian myeloblastosis virus in Escherichia coli.

Bioscience, biotechnology and biochemistry, 2021
The α subunit of avian myeloblastosis virus reverse transcriptase (AMV-RT) is generated from the β subunit by proteolysis, and the αβ heterodimer represents the active form. The codon optimized gene was expressed in E.
Yuriko Makino, H. Satoh, Atsushi Noguchi, T. Ide, R. Yatsunami, Satoshi Nakamura   +5 more
semanticscholar   +1 more source

Characterization of avian myeloblastosis-associated virus DNA intermediates

Journal of Virology, 1980
The major species of unintegrated linear viral DNA identified in chicken embryonic fibroblasts infected with either the avian myeloblastosis-associated viruses (MAV-1, MAV-2) or the standard avian myeloblastosis virus complex (AMV-S) has a mass of 5.3 X 10(6) daltons. An additional minor DNA component observed only in AMV-S-infected cells has a mass of
D G, Bergmann, L M, Souza, M A, Baluda
openaire   +2 more sources

Transformation of chick fibroblast cultures with avian myeloblastosis virus

Journal of Cellular Physiology, 1969
AbstractCellular transformation was induced with avian myeloblastosis virus strain BAI‐A (standard AMV) and with a strain of AMV containing subgroup B only. Cultures of muscle tissues from either chick embryo or day old chicks were used for this study. Results were similar in C/O and C/A cells.
C, Moscovici, M G, Moscovici, M, Zanetti
openaire   +2 more sources

Protein kinase and phosphoproteins of avian myeloblastosis virus

Journal of Virology, 1977
A protein kinase associated with purified virions of avian myeloblastosis virus, BAI strain A, was highly purified by ion-exchange chromatography and gel filtration. On the basis of molecular sieving on Sephadex G-200, the enzyme protein appeared to have a molecular weight of about 50,000 to 60,000; disc gel electrophoresis in sodium dodecyl sulfate ...
openaire   +2 more sources

Reverse transcriptase from avian myeloblastosis virus: A zinc metalloenzyme

Biochemical and Biophysical Research Communications, 1974
Abstract Previous postulates of a relationship between a zinc enzyme and the leukemic process (1,2) have led to the identification of the RNA dependent DNA polymerase -- reverse transcriptase -- of avian myeloblastosis virus as a zinc metalloenzyme.
D S, Auld, H, Kawaguchi, D M, Livingston, B L, Vallee   +3 more
openaire   +2 more sources

Studies on the RNA from avian myeloblastosis virus

Virology, 1969
Abstract RNA from avian myeloblastosis virus was purified and some of its properties were examined. Two RNA components were isolated from the virus. Based on the amount of methylation of the RNA and on its base ratios the small component, which sediments at 4 S, appears to be similar to host cell transfer RNA.
openaire   +2 more sources

Characterization of the adenosine triphosphatase of avian myeloblastosis virus

Archives of Biochemistry and Biophysics, 1979
Abstract The ATPase of avian myeloblastosis virus (AMV) is not a recognizable cellular enzyme. It hydrolyzes ATP, GTP, ITP, UTP, and dCTP at equal rates, is inhibited by high concentrations of dithiothreitol, and is partially inhibited by 1 × 10 −5 m p -chloromercuribenzoic acid (PCMB) and p -chloromercuribenzene sulfonate acid (PCMBS).
R P, Schneider, G S, Beaudreau
openaire   +2 more sources