Molecular cloning and transcript mapping of the dihydroorotate dehydrogenase dhod locus of Drosophila melanogaster

1989 ◽  
Vol 219 (3) ◽  
pp. 397-403 ◽  
Author(s):  
W. Keith Jones ◽  
Russell Kirkpatrick ◽  
John M. Rawls
Keyword(s):  
Drosophila Melanogaster ◽  
Molecular Cloning ◽  
Dihydroorotate Dehydrogenase ◽  
Transcript Mapping

Molecular Cloning and Expression of Stromalin Protein from Drosophila melanogaster: Homologous to Mammalian Stromalin Family of Nuclear Proteins

1998 ◽  
Vol 17 (8) ◽  
pp. 699-706 ◽  
Author(s):  
ANA VALDEOLMILLOS ◽  
RICARDO VILLARES ◽  
JOSÉ M. BUESA ◽  
SERGIO GONZÁLEZ-CRESPO ◽  
CARLOS MARTÍNEZ-A. ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Molecular Cloning ◽  
Cloning And Expression ◽  
Nuclear Proteins

Molecular cloning of mei-41, a gene that influences both somatic and germline chromosome metabolism of Drosophila melanogaster

1995 ◽  
Vol 246 (2) ◽  
pp. 148-155 ◽  
Author(s):  
Satnam S. Banga ◽  
Akihiko H. Yamamoto ◽  
James M. Mason ◽  
James B. Boyd
Keyword(s):  
Drosophila Melanogaster ◽  
Molecular Cloning

scholarly journals Molecular cloning and analysis of small optic lobes, a structural brain gene of Drosophila melanogaster.

1991 ◽  
Vol 88 (16) ◽  
pp. 7214-7218 ◽  
Author(s):  
S. J. Delaney ◽  
D. C. Hayward ◽  
F. Barleben ◽  
K. F. Fischbach ◽  
G. L. Miklos
Keyword(s):  
Drosophila Melanogaster ◽  
Molecular Cloning ◽  
Optic Lobes ◽  
Structural Brain

Molecular cloning of the pawn locus from Drosophila melanogaster

Gene ◽  
2003 ◽  
Vol 310 ◽  
pp. 169-173 ◽  
Author(s):  
Susan E. Arruda ◽  
Patrick J. Dolph
Keyword(s):  
Drosophila Melanogaster ◽  
Molecular Cloning

Molecular cloning and characterization of the inositol 1,4,5-triphosphate receptor in Drosophila melanogaster

1992 ◽  
Vol 17 ◽  
pp. 140 ◽  
Author(s):  
Shingo Yoshikawa ◽  
Teiichi Tanimura ◽  
Atsushi Miyawaki ◽  
Makoto Nakamura ◽  
Michisuke Yuzaki ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Molecular Cloning

Molecular Cloning, Genomic Organization, and Expression of a B-Type (Cricket-Type) Allatostatin Preprohormone from Drosophila melanogaster

2001 ◽  
Vol 281 (2) ◽  
pp. 544-550 ◽  
Author(s):  
Michael Williamson ◽  
Camilla Lenz ◽  
M.E. Winther ◽  
Dick R. Nässel ◽  
Cornelis J.P. Grimmelikhuijzen
Keyword(s):  
Drosophila Melanogaster ◽  
Molecular Cloning ◽  
Genomic Organization

Molecular Cloning, Genomic Organization, and Expression of a C-Type (Manduca sexta-Type) Allatostatin Preprohormone from Drosophila melanogaster

2001 ◽  
Vol 282 (1) ◽  
pp. 124-130 ◽  
Author(s):  
Michael Williamson ◽  
Camilla Lenz ◽  
Åsa M.E. Winther ◽  
Dick R. Nässel ◽  
Cornelis J.P. Grimmelikhuijzen
Keyword(s):  
Drosophila Melanogaster ◽  
Molecular Cloning ◽  
Manduca Sexta ◽  
Genomic Organization

scholarly journals Identification of multifunctional ATP-citrate lyase kinase as the α-isoform of glycogen synthase kinase-3

1992 ◽  
Vol 288 (1) ◽  
pp. 309-314 ◽  
Author(s):  
K Hughes ◽  
S Ramakrishna ◽  
W B Benjamin ◽  
J R Woodgett
Keyword(s):  
Drosophila Melanogaster ◽  
Protein Kinase ◽  
Molecular Cloning ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Atp Citrate Lyase ◽  
Multifunctional Protein ◽  
Citrate Lyase ◽  
Biochemical Analyses

Multifunctional ATP-citrate lyase kinase (ACLK) exhibits several properties that are similar to glycogen-synthase kinase-3 (GSK-3). The molecular cloning of two distinct mammalian GSK-3 cDNAs and a Drosophila melanogaster (fruitfly) homologue, zeste-white3sgg, has established the existence of a GSK-3 subfamily. A multifunctional protein kinase first identified as an ACLK has recently been shown to exhibit several similarities to the alpha- and beta-forms of GSK-3. Here we have used immunological and biochemical analyses to directly compare these enzymes. Thus purified preparations of ACLK isolated from brain and liver preferentially cross-react with anti-GSK-3 alpha antisera and phosphorylate previously defined substrates of GSK-3 at identical sites. Conversely, both alpha- and beta-forms of GSK-3 phosphorylated ATP-citrate lyase at the same site(s) targeted by ACLK. These, and other similarities, demonstrate ACLK to be identical with, or highly related to, GSK-3 alpha, the implications of which are discussed.

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