scholarly journals Identification of the amino‐terminal fragment of Ara h 1 as a major target of the IgE‐binding activity in the basic peanut protein fraction

2020 ◽  
Vol 50 (3) ◽  
pp. 401-405 ◽  
Author(s):  
Rob C. Aalberse ◽  
Geoffrey A. Mueller ◽  
Ninotska I. L. Derksen ◽  
Joost A. Aalberse ◽  
Lori L. Edwards ◽  
...  
Keyword(s):  
Protein Fraction ◽  
Binding Activity ◽  
Peanut Protein ◽  
Amino Terminal ◽  
Ige Binding ◽  
Terminal Fragment ◽  
Ara H 1 ◽  
Amino Terminal Fragment ◽  
Major Target

scholarly journals The adenovirus E1A-regulated transcription factor E4F is generated from the human homolog of nuclear factor phiAP3.

1997 ◽  
Vol 17 (4) ◽  
pp. 1890-1903 ◽  
Author(s):  
E R Fernandes ◽  
R J Rooney
Keyword(s):  
Dna Binding ◽  
Transcriptional Activation ◽  
Binding Activity ◽  
Full Length ◽  
Nuclear Factor ◽  
Human Homolog ◽  
Amino Terminal ◽  
Dna Binding Activity ◽  
Terminal Fragment ◽  
Amino Terminal Fragment

A 50-kDa cellular factor, E4F, has been implicated in mediating trans activation of the adenovirus E4 gene by the 289R E1A(13S) protein. Previous experiments demonstrated an E1A-dependent increase in E4F DNA binding activity, dependent on phosphorylation, that correlated with the activation of E4 transcription. Using expression screening, we isolated a cDNA clone encoding the E4F protein, as judged by DNA binding characteristics, transcriptional activation, and immunological criteria. The E4F-1 cDNA encodes a 783-amino-acid polypeptide that has 86% sequence identity with the murine nuclear factor phiAP3, a GLI-krüppel-related protein. E4F DNA binding activity is encoded within an amino-terminal region of E4F-1 that contains a zinc finger domain and, as with endogenous E4F, is phosphatase sensitive. We found that E4F was generated from the full-length E4F-1-encoded protein as a 50-kDa amino-terminal fragment. Moreover, E1A(13S) expression induced the phosphorylation of both forms of E4F-1 but differentially regulated their DNA binding activities, stimulating the 50-kDa fragment while reducing the activity of the full-length protein. In transient-transfection assays, the E4F-1 amino-terminal fragment stimulated the adenovirus E4 promoter in the presence of E1A(13S), whereas the full-length protein repressed the promoter in the absence, but not the presence, of E1A. The results indicate that the 50-kDa polypeptide responsible for E4F DNA binding activity is a fragment generated from the human homolog of phiAP3 and that the two forms of the E4F-1 protein are differentially regulated by E1A through phosphorylation.

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

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
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