O
Oxana A. Malakhova
Researcher at Scripps Research Institute
Publications - 18
Citations - 2772
Oxana A. Malakhova is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: ISG15 & Fusion protein. The author has an hindex of 14, co-authored 18 publications receiving 2554 citations. Previous affiliations of Oxana A. Malakhova include University of California, San Diego.
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Journal ArticleDOI
SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins
Michael P. Malakhov,Michael R. Mattern,Oxana A. Malakhova,Mark Drinker,Stephen D. Weeks,Tauseef R Butt +5 more
TL;DR: Enhanced expression and solubility of proteins fused to SUMO combined with broad specificity and highly efficient cleavage properties of the SUMO protease 1 indicates that SUMO-fusion technology will become a useful tool in purification of proteins and peptides.
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UBP43 (USP18) Specifically Removes ISG15 from Conjugated Proteins
TL;DR: It is postulate that UBP43 is necessary to maintain a critical cellular balance of ISG15-conjugated proteins in both healthy and stressed organisms.
Journal ArticleDOI
UBP43 is a novel regulator of interferon signaling independent of its ISG15 isopeptidase activity.
Oxana A. Malakhova,Keun Il Kim,Jiann-Kae Luo,Weiguo Zou,K.G. Suresh Kumar,Serge Y. Fuchs,Ke Shuai,Dong-Er Zhang +7 more
TL;DR: It is shown that Ubp43 negatively regulates IFN signaling independent of its isopeptidase activity towards ISG15, and this data implicate Ubp 43 as a novel in vivo inhibitor of signal transduction pathways that are specifically triggered by type I IFN.
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Protein ISGylation modulates the JAK-STAT signaling pathway
Oxana A. Malakhova,Ming Yan,Michael P. Malakhov,Youzhong Yuan,Kenneth J. Ritchie,Keun Il Kim,Luke F. Peterson,Ke Shuai,Dong-Er Zhang +8 more
TL;DR: It is reported that mice lacking UBP43, a protease that removes ISG15 from ISGylated proteins, are hypersensitive to type I IFN, and the involvement of proteinISGylation in the regulation of the JAK-STAT pathway is suggested.
Journal ArticleDOI
High-throughput Immunoblotting UBIQUITIN-LIKE PROTEIN ISG15 MODIFIES KEY REGULATORS OF SIGNAL TRANSDUCTION
Michael P. Malakhov,Keun Il Kim,Oxana A. Malakhova,Barbara S. Jacobs,Ernest C. Borden,Dong-Er Zhang +5 more
TL;DR: A role for ISG15 in the regulation of multiple signal transduction pathways is suggested and attractive models to further elucidate the biochemical function of ISGylation are offered.