A. Rosemary Siafakas

Author

The University of Sydney

Also Known As

A. Rosemary Siafakas, Aritee R. Siafakas, Aritee Rosemary Siafakas

Publications

900

Citations

H-Index

Concepts

All Affiliations

The University of Sydney Nagoya University Westmead Institute The University of Melbourne Florey Institute of Neuroscience and Mental Health

About

A. Rosemary Siafakas is an author at The University of Sydney specializing in oxidative stress, metabolism, and medicine.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Medicine	2	2	53
2	Natural Sciences	2	2	53
3	Biochemistry	2	2	53
4	Metabolism	2	2	53
5	Molecular Biology	2	2	53

A. Rosemary Siafakas

Publications

355

Citations

H-Index

Page 1

	Year	Citations
Lipid Rafts in <i>Cryptococcus neoformans</i> Concentrate the Virulence Determinants Phospholipase B1 and Cu/Zn Superoxide Dismutase A. Rosemary Siafakas, Lesley C. Wright, Tania C. Sorrell, Eukaryotic Cell	2006	104
Cell Wall-linked Cryptococcal Phospholipase B1 Is a Source of Secreted Enzyme and a Determinant of Cell Wall Integrity A. Rosemary Siafakas, Tania C. Sorrell, Lesley C. Wright, Journal of Biological Chemistry	2007	85
Role and mechanism of phosphatidylinositol‐specific phospholipase C in survival and virulence of <i>Cryptococcus neoformans</i> Methee Chayakulkeeree, Tania C. Sorrell, A. Rosemary Siafakas, Molecular Microbiology	2008	69
Cellular Iron Depletion and the Mechanisms Involved in the Iron-dependent Regulation of the Growth Arrest and DNA Damage Family of Genes Federica Saletta, Yohan Suryo Rahmanto, A. Rosemary Siafakas, Journal of Biological Chemistry	2011	44
Coupling of the polyamine and iron metabolism pathways in the regulation of proliferation: Mechanistic links to alterations in key polyamine biosynthetic and catabolic enzymes Darius J.R. Lane, Dong-Hun Bae, A. Rosemary Siafakas, Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease Aldo-keto ReductaseBiochemistryIron MetabolismNatural SciencesCatabolic Enzymes	2018	39
Acireductone dioxygenase 1 (ADI1) is regulated by cellular iron by a mechanism involving the iron chaperone, PCBP1, with PCBP2 acting as a potential co-chaperone Dong-Hun Bae, Darius J.R. Lane, A. Rosemary Siafakas, Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease Redox SignalingReductive StressAldo-keto ReductaseBiochemistryIron Metabolism	2020	14

Page 1