Expression and Characterization of Cysteine-Modified Variants of an Amino-Terminal Fragment of Bactericidal/Permeability-Increasing Protein

1996 ◽  
Vol 8 (1) ◽  
pp. 28-40 ◽  
Author(s):  
Arnold H. Horwitz ◽  
Scott D. Leigh ◽  
Susan Abrahamson ◽  
Hélène Gazzano-Santoro ◽  
Pei-Syan Liu ◽  
...  
Keyword(s):  
Amino Terminal ◽  
Terminal Fragment ◽  
Amino Terminal Fragment

scholarly journals Characterization of amino-terminal fragment liberated from bovine prothrombin by activated factor X

FEBS Letters ◽  
1973 ◽  
Vol 36 (3) ◽  
pp. 313-317 ◽  
Author(s):  
Takashi Morita ◽  
Sadaaki Iwanaga ◽  
Tomoji Suzuki ◽  
Kazuo Fujikawa
Keyword(s):  
Factor X ◽  
Amino Terminal ◽  
Terminal Fragment ◽  
Amino Terminal Fragment

scholarly journals Evolution of the hedgehog Gene Family

Genetics ◽  
1996 ◽  
Vol 142 (3) ◽  
pp. 965-972 ◽  
Author(s):  
Sudhir Kumar ◽  
Kristi A Balczarek ◽  
Zhi-Chun Lai
Keyword(s):  
Intercellular Communication ◽  
Short Range ◽  
Gene Duplications ◽  
Future Directions ◽  
Amino Terminal ◽  
Terminal Fragment ◽  
Carboxyl Terminal ◽  
Multicellular Organisms ◽  
Amino Terminal Fragment

Abstract Effective intercellular communication is an important feature in the development of multicellular organisms. Secreted hedgehog (hh) protein is essential for both long- and short-range cellular signaling required for body pattern formation in animals. In a molecular evolutionary study, we find that the vertebrate homologs of the Drosophila hh gene arose by two gene duplications: the first gave rise to Desert hh, whereas the second produced the Indian and Sonic hh genes. Both duplications occurred before the emergence of vertebrates and probably before the evolution of chordates. The amino-terminal fragment of the hh precursor, crucial in long- and short-range intercellular communication, evolves two to four times slower than the carboxyl-terminal fragment in both Drosophila hh and its vertebrate homologues, suggesting conservation of mechanism of hh action in animals. A majority of amino acid substitutions in the amino- and carboxyl-terminal fragments are conservative, but the carboxyl-terminal domain has undergone extensive insertion-deletion events while maintaining its autocleavage protease activity. Our results point to similarity of evolutionary constraints among sites of Drosophila and vertebrate hh homologs and suggest some future directions for understanding the role of hh genes in the evolution of developmental complexity in animals.

The amino‐terminal fragment of human urokinase directs a recombinant chimeric toxin to target cells: internalization is toxin mediated

1997 ◽  
Vol 11 (13) ◽  
pp. 1169-1176 ◽  
Author(s):  
M. Serena Fabbrini ◽  
Daniela Carpani ◽  
Iraldo Bello‐Rivero ◽  
Marco R. Soria
Keyword(s):  
Target Cells ◽  
Amino Terminal ◽  
Terminal Fragment ◽  
Amino Terminal Fragment
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