ISG15 Inhibits Nedd4 Ubiquitin E3 Activity and Enhances the Innate Antiviral Response*

Autor: Oxana A. Malakhova, Dong-Er Zhang

Publikováno v: Journal of Biological Chemistry. 283:8783-8787

Interferons regulate diverse immune functions through the transcriptional activation of hundreds of genes involved in anti-viral responses. The interferon-inducible ubiquitin-like protein ISG15 is expressed in cells in response to a variety of stress

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8c56a28b2331965425038fd8ee0a0b5
https://doi.org/10.1074/jbc.c800030200

High-throughput Immunoblotting

Autor: Dong-Er Zhang, Oxana A. Malakhova, Ernest C. Borden, Barbara S. Jacobs, Keun Il Kim, Michael P. Malakhov

Publikováno v: Journal of Biological Chemistry. 278:16608-16613

ISG15 is a ubiquitin-like protein that conjugates to numerous proteins in cells treated with interferon or lipopolysaccharide. Dysregulation of protein ISG15 modification (ISGylation) in mice leads to decreased life expectancy, brain cell injury, and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::78e20ec8bef4b32c4d763d0153ca4225
https://doi.org/10.1074/jbc.m208435200

Disruption of the NHR4 domain structure in AML1-ETO abrogates SON binding and promotes leukemogenesis

Autor: Miao Chia Lo, Anita Boyapati, Dong-Er Zhang, Hans Beier Ommen, Oxana A. Malakhova, Robert Hines, Eun-Young Erin Ahn, Ming Yan, Peter Hokland

Publikováno v: Ahn, E-Y, Yan, M, Malakhova, O A, Lo, M-C, Boyapati, A, Ommen, H B, Hines, R, Hokland, P & Zhang, D-E 2008, ' Disruption of the NHR4 domain structure in AML1-ETO abrogates SON binding and promotes leukemogenesis. ', Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 44, pp. 17103-8 . https://doi.org/10.1073/pnas.0802696105

Udgivelsesdato: 2008-Nov-4 AML1-ETO is generated from t(8;21)(q22;q22), which is a common form of chromosomal translocation associated with development of acute myeloid leukemia (AML). Although full-length AML1-ETO alone fails to promote leukemia bec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65f861dbe7ec14746f020386c69e99a6
https://pubmed.ncbi.nlm.nih.gov/18952841

ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitin

Autor: Oxana A. Malakhova, Vladimir Papov, Keun Il Kim, Weiguo Zou, Chinh T. Dao, Dong-Er Zhang, Jun Li

Publikováno v: Biochemical and biophysical research communications. 336(1)

ISG15 was the first ubiquitin-like modifier to be identified. However, the function of ISG15 modification has been an enigma for many years. At present, no data are available about the function of ISGylation for any target. In this paper, we report t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f625ab0d70d9ee60310329ea78c6e75
https://pubmed.ncbi.nlm.nih.gov/16122702

SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins

Autor: Michael P. Malakhov, Oxana A. Malakhova, Mark Drinker, Michael R. Mattern, Stephen D. Weeks, Tauseef R Butt

Publikováno v: Journal of structural and functional genomics. 5(1-2)

SUMO (small ubiquitin-related modifier) modulates protein structure and function by covalently binding to the lysine side chains of the target proteins. Yeast cells contain two SUMO proteases, Ulp1 and Ulp2, that cleave sumoylated proteins in the cel

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c77703edb0e6ad4cd87d7350a7b5f05
https://pubmed.ncbi.nlm.nih.gov/15263846