O. Gakh

发表

Zinc and the iron donor frataxin regulate oligomerization of the scaffold protein to form new FeS cluster assembly centers

J. Thompson, G. Isaya, B. K. Galeano, 2017 .

Zinc and the iron donor frataxin regulate oligomerization of the scaffold protein to form new Fe–S cluster assembly centers

J. Thompson, J. Thompson, G. Isaya, 2017, Metallomics : integrated biometal science.

Defining the Architecture of the Core Machinery for the Assembly of Fe-S Clusters in Human Mitochondria.

J. Thompson, Douglas S. Smith, G. Isaya, 2017, Methods in enzymology.

Architecture of the Yeast Mitochondrial Iron-Sulfur Cluster Assembly Machinery

S. Al-Karadaghi, J. Thompson, Christopher A G Söderberg, 2016, The Journal of Biological Chemistry.

Architecture of the Human Mitochondrial Iron-Sulfur Cluster Assembly Machinery*

S. Al-Karadaghi, J. Thompson, G. Isaya, 2016, The Journal of Biological Chemistry.

Physical evidence that yeast frataxin is an iron storage protein.

J. Adamec, R. Twesten, W. Owen, 2002, Biochemistry.

Protein import and processing reconstituted with isolated rat liver mitochondria and recombinant mitochondrial processing peptidase.

P. Cavadini, G. Isaya, O. Gakh, 2002, Methods.

Chapter 107 – Mitochondrial Intermediate Peptidase

O. Gakh, 2013 .

Oligomeric Yeast Frataxin Drives Assembly of Core Machinery for Mitochondrial Iron-Sulfur Cluster Synthesis*

Hongqiao Li, G. Isaya, O. Gakh, 2009, The Journal of Biological Chemistry.

Supramolecular assemblies of human frataxin are formed via subunit-subunit interactions mediated by a non-conserved amino-terminal region.

Heather A. O'Neill, G. Isaya, O. Gakh, 2005, Journal of molecular biology.

Signatures of cell stress and altered bioenergetics in skin fibroblasts from patients with multiple sclerosis

C. Lucchinetti, C. Howe, J. Wilkins, 2020, Aging.

Mammalian pitrilysin: substrate specificity and mitochondrial targeting.

L. Hersh, L. Juliano, M. Juliano, 2009, Biochemistry.

The Structure of the Complex between Yeast Frataxin and Ferrochelatase

S. Al-Karadaghi, G. C. Ferreira, G. Hunter, 2016, The Journal of Biological Chemistry.

The structures of frataxin oligomers reveal the mechanism for the delivery and detoxification of iron.

E. Garman, U. Ryde, S. Al-Karadaghi, 2006, Structure.

High-throughput immunoassay for the biochemical diagnosis of Friedreich ataxia in dried blood spots and whole blood.

D. Lynch, P. Rinaldo, D. Matern, 2013, Clinical chemistry.

Lateral-flow immunoassay for the frataxin protein in Friedreich's ataxia patients and carriers.

J. Willis, R. Capaldi, M. Marusich, 2008, Molecular genetics and metabolism.

Mitochondrial processing peptidases.

P. Cavadini, G. Isaya, O. Gakh, 2002, Biochimica et biophysica acta.

Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity.

G. C. Ferreira, J. Imlay, G. Isaya, 2006, Human molecular genetics.

Assembly of human frataxin is a mechanism for detoxifying redox-active iron.

Heather A. O'Neill, S. Mooney, G. C. Ferreira, 2005, Biochemistry.

The Ferroxidase Activity of Yeast Frataxin*

S. Mooney, G. Isaya, Sungjo Park, 2002, The Journal of Biological Chemistry.

Cleavage Site Selection within a Folded Substrate by the ATP-dependent Lon Protease*[boxs]

Z. Granot, Hong Li, J. Orly, 2005, Journal of Biological Chemistry.

PMPCA mutations cause abnormal mitochondrial protein processing in patients with non-progressive cerebellar ataxia.

S. Scherer, C. Marshall, T. Paton, 2015, Brain : a journal of neurology.

Normal and Friedreich Ataxia Cells Express Different Isoforms of Frataxin with Complementary Roles in Iron-Sulfur Cluster Assembly*

D. Berkholz, G. Isaya, T. Bedekovics, 2010, The Journal of Biological Chemistry.

Two-step Processing of Human Frataxin by Mitochondrial Processing Peptidase

J. Adamec, F. Taroni, P. Cavadini, 2000, The Journal of Biological Chemistry.

Assembly of the Iron-binding Protein Frataxin in Saccharomyces cerevisiae Responds to Dynamic Changes in Mitochondrial Iron Influx and Stress Level*

G. Isaya, O. Gakh, Douglas Y. Smith, 2008, Journal of Biological Chemistry.

Yeast Frataxin Sequentially Chaperones and Stores Iron by Coupling Protein Assembly with Iron Oxidation*

Heather A. O'Neill, G. C. Ferreira, G. Isaya, 2003, Journal of Biological Chemistry.

Functional studies of frataxin

G. Isaya, O. Gakh, HA O'Neill, 2004, Acta paediatrica (Oslo, Norway : 1992). Supplement.

Complementation between mitochondrial processing peptidase (MPP) subunits from different species.

J. Adamec, F. Kalousek, J. Spížek, 1999, Archives of biochemistry and biophysics.

Structural basis of the iron storage function of frataxin from single-particle reconstruction of the iron-loaded oligomer.

S. Al-Karadaghi, H. Elmlund, H. Hebert, 2008, Biochemistry.

Molecular and functional characterization of a human frataxin mutation found in hypertrophic cardiomyopathy.

S. Ommen, M. Ackerman, S. V. Van Driest, 2005, Molecular genetics and metabolism.

Substrate evokes translocation of both domains in the mitochondrial processing peptidase alpha-subunit during which the C-terminus acts as a stabilizing element.

E. Amler, M. Kubala, J. Janata, 2004, Biochemical and biophysical research communications.

Substrate binding changes conformation of the α-, but not the β-subunit of mitochondrial processing peptidase

J. Adamec, T. Obsil, E. Amler, 2001 .

Substrate binding changes conformation of the alpha-, but not the beta-subunit of mitochondrial processing peptidase.

J. Adamec, T. Obsil, E. Amler, 2001, Archives of biochemistry and biophysics.

SAXS and stability studies of iron-induced oligomers of bacterial frataxin CyaY

S. Al-Karadaghi, Przemysław Grela, M. Tchórzewski, 2017, PloS one.

The Molecular Basis of Iron-induced Oligomerization of Frataxin and the Role of the Ferroxidation Reaction in Oligomerization*

Dmitri I. Svergun, Alexander V. Shkumatov, D. Svergun, 2013, The Journal of Biological Chemistry.

Oligomerization propensity and flexibility of yeast frataxin studied by X-ray crystallography and small-angle X-ray scattering.

D. Svergun, A. Shkumatov, S. Al-Karadaghi, 2011, Journal of molecular biology.

The Molecular Basis of Iron-induced Oligomerization of Frataxin and the Role of the Ferroxidation Reaction in Oligomerization*

D. Svergun, A. Shkumatov, S. Al-Karadaghi, 2013, The Journal of Biological Chemistry.

Missense Mutations Linked to Friedreich Ataxia Have Different but Synergistic Effects on Mitochondrial Frataxin Isoforms*

Hongqiao Li, G. Isaya, W. Ranatunga, 2012, The Journal of Biological Chemistry.

The Molecular Basis of Iron-induced Oligomerization of Frataxin and the Role of the Ferroxidation Reaction in

D. Svergun, A. Shkumatov, S. Al-Karadaghi, 2013 .

Normal and Friedreich Ataxia Cells Express Different Isoforms of Frataxin with Complementary Roles in Iron-Sulfur Cluster Assembly*

D. Berkholz, G. Isaya, T. Bedekovics, 2010, Journal of Biological Chemistry.

Oligomerization propensity and flexibility of yeast frataxin studied by X-ray crystallography and small-angle X-ray scattering.

D. Svergun, A. Shkumatov, S. Al-Karadaghi, 2011, Journal of molecular biology.

Structure of frataxin iron cores: an X-ray absorption spectroscopic study.

Heather A. O'Neill, H. Nichol, G. George, 2003, Biochemistry.