Prevalence and molecular characterization of meq in feather follicular epithelial cells of Korean broiler chickens

Virus Genes ◽  
2007 ◽  
Vol 35 (2) ◽  
pp. 339-345 ◽  
Author(s):  
Jung-Won Kang ◽  
Sun-Hee Cho ◽  
In-Pil Mo ◽  
Dong-Woo Lee ◽  
Hyuk-Joon Kwon
Keyword(s):  
Epithelial Cells ◽  
Molecular Characterization ◽  
Broiler Chickens ◽  
Follicular Epithelial

scholarly journals 1044 Molecular characterization of radiation-induced transformation of human prostate epithelial cells

1995 ◽  
Vol 32 ◽  
pp. 245
Author(s):  
Michael Kuettel ◽  
Peter Thraves ◽  
Sarada Prasad ◽  
Susan Varghese ◽  
Anatoly Dritschilo
Keyword(s):  
Epithelial Cells ◽  
Molecular Characterization ◽  
Human Prostate ◽  
Prostate Epithelial Cells ◽  
Radiation Induced

scholarly journals Molecular Characterization of an Apical Early Endosomal Glycoprotein from Developing Rat Intestinal Epithelial Cells

1995 ◽  
Vol 270 (4) ◽  
pp. 1583-1588 ◽  
Author(s):  
Becky A. Speelman ◽  
Katrina Allen ◽  
Tamara L. Grounds ◽  
Marian R. Neutra ◽  
Tomas Kirchhausen ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Molecular Characterization ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial ◽  
Developing Rat

scholarly journals Molecular characterization of gene regulatory networks in primary human tracheal and bronchial epithelial cells

2018 ◽  
Vol 17 (4) ◽  
pp. 444-453 ◽  
Author(s):  
Austin E. Gillen ◽  
Rui Yang ◽  
Calvin U. Cotton ◽  
Aura Perez ◽  
Scott H. Randell ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Molecular Characterization ◽  
Gene Regulatory Networks ◽  
Regulatory Networks ◽  
Bronchial Epithelial Cells ◽  
Bronchial Epithelial ◽  
Gene Regulatory

scholarly journals Molecular characterization of chicken astroviruses in gout-affected commercial broiler chickens in Haryana, India

VirusDisease ◽  
2019 ◽  
Vol 30 (4) ◽  
pp. 551-561 ◽  
Author(s):  
Sumitra Panigrahi ◽  
Naresh Jindal ◽  
Pawan Kumar ◽  
Sanjay Barua ◽  
Naveen Kumar ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Broiler Chickens ◽  
Commercial Broiler

scholarly journals Identification and molecular characterization of E-MAP-115, a novel microtubule-associated protein predominantly expressed in epithelial cells.

1993 ◽  
Vol 123 (2) ◽  
pp. 357-371 ◽  
Author(s):  
D Masson ◽  
T E Kreis
Keyword(s):  
Epithelial Cells ◽  
Molecular Characterization ◽  
Hela Cells ◽  
Binding Proteins ◽  
Cdna Expression Library ◽  
Expression Library ◽  
Microtubule Binding ◽  
Terminal Domain

A novel microtubule-associated protein (MAP) of M(r) 115,000 has been identified by screening of a HeLa cell cDNA expression library with an anti-serum raised against microtubule-binding proteins from HeLa cells. Monoclonal and affinity-purified polyclonal antibodies were generated for the further characterization of this MAP. It is different from the microtubule-binding proteins of similar molecular weights, characterized so far, by its nucleotide-insensitive binding to microtubules and different sedimentation behavior. Since it is predominantly expressed in cells of epithelial origin (Caco-2, HeLa, MDCK), and rare (human skin, A72) or not detectable (Vero) in fibroblastic cells, we name it E-MAP-115 (epithelial MAP of 115 kD). In HeLa cells, E-MAP-115 is preferentially associated with subdomains or subsets of perinuclear microtubules. In Caco-2 cells, labeling for E-MAP-115 increases when they polarize and form blisters. The molecular characterization of E-MAP-115 reveals that it is a novel protein with no significant homologies to other known proteins. The secondary structure predicted from its sequence indicates two domains connected by a putative hinge region rich in proline and alanine (PAPA region). E-MAP-115 has two highly charged regions with predicted alpha-helical structure, one basic with a pI of 10.9 in the NH2-terminal domain and one neutral with a pI of 7.6 immediately following the PAPA region in the acidic COOH-terminal half of the molecule. A novel microtubule-binding site has been localized to the basic alpha-helical region in the NH2-terminal domain using in vitro microtubule-binding assays and expression of mutant polypeptides in vivo. Overexpression of this domain of E-MAP-115 by transfection of fibroblasts lacking significant levels of this protein with its cDNA renders microtubules stable to nocodazole. We conclude that E-MAP-115 is a microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells.

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