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Hypusine modification of the ribosome-binding protein eIF5A, a target for new anti-inflammatory drugs: Understanding the action of the inhibitor GC7 on a murine macrophage cell line
(2014-01-30)
Inflammation is part of an important mechanism triggered by the innate immune response that rapidly responds to invading microorganisms and tissue injury. One important elicitor of the inflammatory response is the Gram-negative ...
Hypusine Modification of the Ribosome-binding Protein eIF5A, a Target for New Anti-Inflammatory Drugs: Understanding the Action of the Inhibitor GC7 on a Murine Macrophage Cell Line
(Bentham Science Publ Ltd, 2014-01-01)
Inflammation is part of an important mechanism triggered by the innate immune response that rapidly responds to invading microorganisms and tissue injury. One important elicitor of the inflammatory response is the Gram-negative ...
Inhibition of eukaryotic translation initiation factor 5A (eIF5A) hypusination impairs melanoma growth
(2007-01-01)
The eukaryotic translation initiation factor 5A (eIF5A) undergoes a specific post-translational modification called hypusination. This modification is required for the functionality of this protein. The compound ...
Inhibition of eukaryotic translation initiation factor 5A (eIF5A) hypusination impairs melanoma growth
(2007-01-01)
The eukaryotic translation initiation factor 5A (eIF5A) undergoes a specific post-translational modification called hypusination. This modification is required for the functionality of this protein. The compound ...
eIF5A interacts functionally with eEF2
(Springer, 2012-02-01)
eIF5A is highly conserved from archaea to mammals, essential for cell viability and the only protein known to contain the essential amino acid residue hypusine, generated by a unique posttranslational modification. eIF5A ...
eIF5A interacts functionally with eEF2
(Springer, 2012-02-01)
eIF5A is highly conserved from archaea to mammals, essential for cell viability and the only protein known to contain the essential amino acid residue hypusine, generated by a unique posttranslational modification. eIF5A ...
eIF5A interacts functionally with eEF2
(Springer, 2014)