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Adrian Minty

Researcher at Pasteur Institute

Publications -  41
Citations -  6920

Adrian Minty is an academic researcher from Pasteur Institute. The author has contributed to research in topics: Actin & Interleukin 13. The author has an hindex of 24, co-authored 41 publications receiving 6780 citations.

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Monoallelically expressed gene related to p53 at 1p36, a region frequently deleted in neuroblastoma and other human cancers.

TL;DR: The demonstration that p73 is monoallelically expressed supports the notion that it is a candidate gene in neuroblastoma and proposes that the disregulation of p73 contributes to tumorigenesis and that p53-related proteins operate in a network of developmental and cell cycle controls.
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Interleukin-13 is a new human lymphokine regulating inflammatory and immune responses.

TL;DR: Recombinant IL-13 protein inhibits inflammatory cytokine production induced by lipopolysaccharide in human peripheral blood monocytes, and synergizes with IL-2 in regulating interferon-γ synthesis in large granular lymphocytes.
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Comparison of three actin-coding sequences in the mouse; Evolutionary relationships between the actin genes of warm-blooded vertebrates

TL;DR: Analysis of codon usage in these coding sequences in different vertebrate species indicates two tendencies: increases in bias toward the use of G and C in the third codon position in paralogous comparisons, and in orthologous comparisons.
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Upstream regions of the human cardiac actin gene that modulate its transcription in muscle cells: presence of an evolutionarily conserved repeated motif

TL;DR: These regulatory regions upstream of the cap site of the human cardiac actin gene show remarkably high sequence conservation with the equivalent regions of the mouse and chick genes and there is an evolutionarily conserved repeated motif that may be important in the transcriptional regulation of actin and other contractile protein genes.
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Covalent Modification of p73α by SUMO-1 TWO-HYBRID SCREENING WITH p73 IDENTIFIES NOVEL SUMO-1-INTERACTING PROTEINS AND A SUMO-1 INTERACTION MOTIF

TL;DR: It is shown here that p73alpha, but not p73beta, can be covalently modified by SUMO-1, and is more rapidly degraded by the proteasome than unmodified p73, although SUMo-1 modification is not required for p73 degradation.