panin at tamu.edu
Mon Jun 14 08:46:40 EST 2004
Developmental glycobiology of Drosophila.
Texas A&M University, College Station, TX.
Project Description: The project is focused on characterization of the
role of glycosylation in neural and muscle development. The research is
based on a cross-disciplinary strategy using advanced approaches of
molecular genetics, bioinformatics, biochemistry, and cell biology.
Ample opportunities for professional growth and building a strong
research career in the cutting-edge field of modern biology!
Lab Description: Young and growing laboratory with the research
interests in the field of Developmental Biology, Genetics and
Glycobiology. Several novel genes involved in developmentally-regulated
glycosylation are currently in the focus of our investigation at
molecular, cellular, and organismal levels. We are using the Drosophila
model system, known for its powerful genetics, in combination with
advanced biochemical and cell biological approaches.
Place: With the student population of more than 45,000, Texas A&M is one
of the biggest and well-funded Universities in America; TAMU is famous
for its Engineering and Life Sciences research all over the world.
College Station is a nice and safe university town with low cost of
living located in the vicinity of Houston, TX.
Qualifications: Motivated researchers with experience in Molecular
Biology and/or Biochemistry and Glycobiology and/or Drosophila Genetics
Application Requirements: Names and email addresses of at least 2
Contact: Vlad Panin, Department of Biochemistry and Biophysics
Texas A&M University, 2128 TAMU College Station, TX 77843-2128 FAX
(979)845-9274 Tel:(979) 458-4630 email: panin at tamu.edu
Koles K, Irvine KD, and Panin VM (2004) Functional characterization of
Drosophila sialyltransferase J Biol Chem. 279: 4346-57
Lei L, Xu A, Panin V.M, Irvine KD (2003) An O-fucose site in the ligand
binding domain inhibits Notch activation. Development 130: 6411-21.
Panin VM, Shao L, Lei L, Moloney DJ, Irvine KD, and Haltiwanger RS
(2002) Notch ligands are substrates for protein O-fucosyltransferase-1
and Fringe J Biol Chem 277: 29945-52.
Moloney DJ, Panin VM, Johnston SH, Chen J, Shao L, Wilson R, Wang Y,
Stanley P, Irvine K D, Haltiwanger RS, and Vogt TF (2000) Fringe is a
glycosyltransferase that modifies Notch. Nature. 406: 369-375.
Vlad Panin, Ph.D.
Department of Biochemistry and Biophysics
Texas A&M University
College Station, TX 77843-2128
Tel: (979) 458-4630
e-mail: panin at tamu.edu
More information about the Dros