Human cytomegalovirus UL97 open reading frame encodes a protein that phosphorylates the antiviral nucleoside analogue ganciclovir
Article Abstract:
UL97tr is a protein kinase enzyme produced by the human cytomegalovirus (HCMV) that allows the virus to phosphorylate the nucleoside analogue ganciclovir. HCMV is an opportunistic pathogen that typically attacks people whose immune systems are weak due to acquired immunodeficiency syndrome or other causes. Ganciclovir is an antiviral drug often used to treat HCMV infection. The identification of an HCMV enzyme that affects the selectivity of ganciclovir may help in designing more potent antiviral agents with which to combat HCMV.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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A protein kinase homologue controls phosphorylation of ganciclovir in human cytomegalovirus-infected cells
Article Abstract:
UL97, identified as a gene of the human cytomegalovirus (HCMV), is responsible for the phosphorylation that is making HCMV increasingly resistant to the antiviral drug ganciclovir. HCMV most often attacks people whose immune systems are weak due to acquired immune deficiency syndrome or other causes. The UL97 gene probably produces the phosphorylation by encoding a protein kinase or enzyme. This discovery of why HCMV is becoming less treatable with ganciclovir may assist in developing more effective antiviral drugs.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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JNK phosphorylates paxillin and regulates cell migration
Article Abstract:
Results show that the focal adhesion adaptor, paxillin, enables cells move rapidly and functions as an adhesion molecule. Mutations in paxillin inhibits cell migration. Furthemore, phosphorylation of serine 178 on paxillin by the c-Jun amino-terminal kinase (JNK) maintains the labile adhesion essenial for rapid cell migration.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2003
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