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Biochimica Et Biophysica Acta|May 5, 2012
Structure, function, and assembly of heme centers in mitochondrial respiratory complexesHyung J Kim, Oleh Khalimonchuk, Pamela M Smith, et al.
Chemistry & Biodiversity|October 31, 2008
X-ray absorption spectroscopy of cuprous-thiolate clusters in Saccharomyces cerevisiae metallothioneinLimei Zhang, Ingrid J Pickering, Dennis R Winge, et al.
The Journal of Biological Chemistry|October 9, 2012
Flavinylation and assembly of succinate dehydrogenase are dependent on the C-terminal tail of the flavoprotein subunitHyung J Kim, Mi-Young Jeong, Un Na, et al.
The Journal of Biological Chemistry|January 20, 2004
Yeast contain a non-proteinaceous pool of copper in the mitochondrial matrixPaul A Cobine, Luis D Ojeda, Kevin M Rigby, et al.
Metallomics : Integrated Biometal Science|July 8, 2017
Oxygen-dependent activation of Cu,Zn-superoxide dismutase-1Morgan M Fetherolf, Stefanie D Boyd, Duane D Winkler, et al.
The Journal of Biological Chemistry|June 7, 2012
Oligomerization of heme o synthase in cytochrome oxidase biogenesis is mediated by cytochrome oxidase assembly factor Coa2Oleh Khalimonchuk, Hyung Kim, Talina Watts, et al.
The Journal of Biological Chemistry|January 6, 2012
Selective Oma1 protease-mediated proteolysis of Cox1 subunit of cytochrome oxidase in assembly mutantsOleh Khalimonchuk, Mi-Young Jeong, Talina Watts, et al.
Molecular and Cellular Biology|July 14, 2010
Analysis of Leigh syndrome mutations in the yeast SURF1 homolog reveals a new member of the cytochrome oxidase assembly factor familyMegan Bestwick, Mi-Young Jeong, Oleh Khalimonchuk, et al.
Molecular and Cellular Biology|June 11, 2008
Coa2 is an assembly factor for yeast cytochrome c oxidase biogenesis that facilitates the maturation of Cox1Fabien Pierrel, Oleh Khalimonchuk, Paul A Cobine, et al.
The Journal of Biological Chemistry|November 24, 2006
Regulation of the yeast TSA1 peroxiredoxin by ZAP1 is an adaptive response to the oxidative stress of zinc deficiencyChang-Yi Wu, Amanda J Bird, Dennis R Winge, et al.
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