G. C. Ferreira

发表

Molecular and functional analysis of the C-terminal region of human erythroid-specific 5-aminolevulinic synthase associated with X-linked dominant protoporphyria (XLDPP).

S. Ducamp, X. Schneider-Yin, F. D. de Rooij, 2013, Human molecular genetics.

Molecular enzymology of 5-aminolevulinate synthase, the gatekeeper of heme biosynthesis.

G. C. Ferreira, G. Hunter, 2011, Biochimica et biophysica acta.

Nickel(II) chelatase variants directly evolved from murine ferrochelatase: porphyrin distortion and kinetic mechanism.

Neil R. McIntyre, G. C. Ferreira, J. Shelnutt, 2011, Biochemistry.

Expression of Murine 5-Aminolevulinate Synthase Variants Causes Protoporphyrin IX Accumulation and Light-Induced Mammalian Cell Death

Erica J. Fratz, G. C. Ferreira, G. Hunter, 2014, PloS one.

Unraveling the substrate-metal binding site of ferrochelatase: an X-ray absorption spectroscopic study.

G. C. Ferreira, G. George, R. Franco, 2002, Biochemistry.

The conserved active site histidine-glutamate pair of ferrochelatase coordinately catalyzes porphyrin metalation

Fiona L. Kearns, H. Woodcock, G. C. Ferreira, 2016 .

FERROCHELATASE: THE CONVERGENCE OF THE PORPHYRIN BIOSYNTHESIS AND IRON TRANSPORT PATHWAYS.

S. Al-Karadaghi, G. C. Ferreira, G. Hunter, 2011, Journal of porphyrins and phthalocyanines.

The conserved active-site loop residues of ferrochelatase induce porphyrin conformational changes necessary for catalysis.

G. C. Ferreira, J. Shelnutt, R. Haddad, 2005, Biochemistry.

Structure and function of ferrochelatase

G. C. Ferreira, J. Moura, I. Moura, 1995, Journal of bioenergetics and biomembranes.

Iron metabolism : inorganic biochemistry and regulatory mechanisms

G. C. Ferreira, J. Moura, R. Franco, 1999 .

Anti-Correlation between the Dynamics of the Active Site Loop and C-Terminal Tail in Relation to the Homodimer Asymmetry of the Mouse Erythroid 5-Aminolevulinate Synthase

V. Uversky, G. C. Ferreira, Insung Na, 2018, International journal of molecular sciences.

Murine erythroid 5-aminolevulinate synthase: Truncation of a disordered N-terminal extension is not detrimental for catalysis.

V. Uversky, L. Breydo, G. C. Ferreira, 2016, Biochimica et biophysica acta.

Iron Hack - A symposium/hackathon focused on porphyrias, Friedreich’s ataxia, and other rare iron-related diseases

Linh M Duong, S. Fatumo, Chengqi Wang, 2019, F1000Research.

Catalytically active alkaline molten globular enzyme: Effect of pH and temperature on the structural integrity of 5-aminolevulinate synthase.

V. Uversky, L. Breydo, G. C. Ferreira, 2014, Biochimica et biophysica acta.

Macromolecular crowders and osmolytes modulate the structural and catalytic properties of alkaline molten globular 5-aminolevulinate synthase

V. Uversky, L. Breydo, G. C. Ferreira, 2016 .

Characterization of the Iron-binding Site in Mammalian Ferrochelatase by Kinetic and Mössbauer Methods (*)

G. C. Ferreira, J. Moura, I. Moura, 1995, The Journal of Biological Chemistry.

5-aminolevulinate synthase: catalysis of the first step of heme biosynthesis.

G. C. Ferreira, G. Hunter, 2009, Cellular and molecular biology.

Micro X-ray fluorescence elemental analysis of spheroid cultures of human neuroblastoma cells

D. F. Oliveira, G. C. Ferreira, M. Anjos, 2020 .

Resonance Raman Spectroscopic Examination of Ferrochelatase-induced Porphyrin Distortion.

S. Al-Karadaghi, G. C. Ferreira, R. Franco, 2011, Journal of porphyrins and phthalocyanines.

Hypoxic up-regulation of erythroid 5-aminolevulinate synthase.

M. Gassmann, R. Wenger, G. C. Ferreira, 2003, Blood.

An Extended C-Terminus, the Possible Culprit for Differential Regulation of 5-Aminolevulinate Synthase Isoforms

G. C. Ferreira, G. Hunter, 2022, Frontiers in Molecular Biosciences.

Murine erythroid 5-aminolevulinate synthase: Adenosyl-binding site Lys221 modulates substrate binding and catalysis

G. C. Ferreira, B. Stojanovski, 2015, FEBS open bio.

Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release.

V. Uversky, L. Breydo, S. Ducamp, 2015, Biochemistry.

A continuous spectrophotometric assay for 5-aminolevulinate synthase that utilizes substrate cycling.

G. C. Ferreira, G. Hunter, 1995, Analytical biochemistry.

Transcriptional regulation of the murine erythroid-specific 5-aminolevulinate synthase gene.

P. Gunaratne, G. C. Ferreira, M. F. Kramer, 2000, Gene.

Heme biosynthesis in mammalian systems: Evidence of a schiff base linkage between the pyridoxal 5′‐phosphate cofactor and a lysine residue in 5‐aminolevulinate synthase

G. C. Ferreira, H. Dailey, P. Neame, 1993, Protein science : a publication of the Protein Society.

Identification and Characterization of an Inhibitory Metal Ion-binding Site in Ferrochelatase*

G. C. Ferreira, G. Hunter, 2010, The Journal of Biological Chemistry.

Metal ion coordination sites in ferrochelatase

G. C. Ferreira, G. Hunter, 2022, Coordination Chemistry Reviews.

Cofactors and Coenzymes | Heme Synthesis

G. C. Ferreira, 2021, Encyclopedia of Biological Chemistry III.

Unstable Reaction Intermediates and Hysteresis during the Catalytic Cycle of 5-Aminolevulinate Synthase

G. C. Ferreira, D. Jahn, M. Jahn, 2014, The Journal of Biological Chemistry.

Pre-steady-state Reaction of 5-Aminolevulinate Synthase

G. C. Ferreira, G. Hunter, 1999, The Journal of Biological Chemistry.

ALAS2 acts as a modiﬁer gene in patients with congenital erythropoietic porphyria

C. Beaumont, C. Ged, S. Ducamp, 2011 .

Inhibition of lipolysis by hydrocarbons and fatty alcohols.

G. C. Ferreira, J. Patton, 1990, Journal of lipid research.

Active site of 5-aminolevulinate synthase resides at the subunit interface. Evidence from in vivo heterodimer formation.

G. C. Ferreira, D. Tan, 1996, Biochemistry.

5-Aminolevulinate synthase catalysis: The catcher in heme biosynthesis.

V. Uversky, G. C. Ferreira, R. Jiang, 2019, Molecular genetics and metabolism.

Transient State Kinetic Investigation of 5-Aminolevulinate Synthase Reaction Mechanism*

G. C. Ferreira, Junshun Zhang, 2002, The Journal of Biological Chemistry.

Lysine-313 of 5-aminolevulinate synthase acts as a general base during formation of the quinonoid reaction intermediates.

G. C. Ferreira, G. Hunter, 1999, Biochemistry.

Metallation of the transition-state inhibitor N-methyl mesoporphyrin by ferrochelatase: implications for the catalytic reaction mechanism.

S. Al-Karadaghi, G. C. Ferreira, C. Reimann, 2005, Journal of molecular biology.

Ferrochelatase π-helix: Implications from examining the role of the conserved π-helix glutamates in porphyrin metalation and product release.

G. C. Ferreira, G. Hunter, Mallory E. Gillam, 2018, Archives of biochemistry and biophysics.

Mammalian ferrochelatase, a new addition to the metalloenzyme family.

G. C. Ferreira, J. Moura, I. Moura, 1994, The Journal of biological chemistry.

Phosphate transport in mitochondria: Past accomplishments, present problems, and future challenges

P. Pedersen, G. C. Ferreira, 1993, Journal of bioenergetics and biomembranes.

Mitochondrial phosphate transport. Import of the H+/Pi symporter and role of the presequence.

P. Pedersen, G. C. Ferreira, R. Pratt, 1991, The Journal of biological chemistry.

Overexpression of higher eukaryotic membrane proteins in bacteria. Novel insights obtained with the liver mitochondrial proton/phosphate symporter.

P. Pedersen, G. C. Ferreira, 1992, The Journal of biological chemistry.

Mitochondrial proton/phosphate transporter. An antibody directed against the COOH terminus and proteolytic cleavage experiments provides new insights about its membrane topology.

P. Pedersen, G. C. Ferreira, R. Pratt, 1990, The Journal of biological chemistry.

Energy-linked anion transport. Cloning, sequencing, and characterization of a full length cDNA encoding the rat liver mitochondrial proton/phosphate symporter.

P. Pedersen, G. C. Ferreira, R. Pratt, 1989, The Journal of biological chemistry.

Porphyrin-substrate binding to murine ferrochelatase: effect on the thermal stability of the enzyme.

G. C. Ferreira, Vesna Prosinecki, G. Bai, 2005, The Biochemical journal.

Chlorophyll breakdown: Chemistry, biochemistry, and biology

Kevin M Smith, B. Kräutler, G. C. Ferreira, 2013 .

The role of tyrosine 121 in cofactor binding of 5‐aminolevulinate synthase

G. C. Ferreira, M. Barber, D. Tan, 1998, Protein science : a publication of the Protein Society.

Heme overdrive rewires pan-cancer cell metabolism

S. Sebti, G. C. Ferreira, G. Reuther, 2022, bioRxiv.

Molecular dynamics analysis of the structural and dynamic properties of the functionally enhanced hepta-variant of mouse 5-aminolevulinate synthase

V. Uversky, G. C. Ferreira, Insung Na, 2018, Journal of biomolecular structure & dynamics.

Supraphysiological concentrations of 5-aminolevulinic acid dimerize in solution to produce superoxide radical anions via a protonated dihydropyrazine intermediate.

G. C. Ferreira, G. Hunter, E. Rivera, 2005, Archives of biochemistry and biophysics.

Probing the Active Site Loop Motif of Murine Ferrochelatase by Random Mutagenesis*

G. C. Ferreira, Zhen Shi, Gloria C Ferreira, 2004, Journal of Biological Chemistry.

The First Structure from the SOUL/HBP Family of Heme-binding Proteins, Murine P22HBP*

B. Goodfellow, B. Volkman, G. C. Ferreira, 2006, Journal of Biological Chemistry.

The Structure of the Complex between Yeast Frataxin and Ferrochelatase

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

Functional asymmetry for the active sites of linked 5-aminolevulinate synthase and 8-amino-7-oxononanoate synthase.

G. C. Ferreira, G. Hunter, Junshun Zhang, 2011, Archives of biochemistry and biophysics.

Metal Ion Substrate Inhibition of Ferrochelatase*

G. C. Ferreira, M. Sampson, G. Hunter, 2008, Journal of Biological Chemistry.

A continuous anaerobic fluorimetric assay for ferrochelatase by monitoring porphyrin disappearance.

G. C. Ferreira, Zhen Shi, Gloria C Ferreira, 2003, Analytical biochemistry.

Expression of mammalian 5-aminolevulinate synthase in Escherichia coli. Overproduction, purification, and characterization.

G. C. Ferreira, H. Dailey, 1993, The Journal of biological chemistry.

Heme biosynthesis: Biochemistry, molecular biology, and relationship to disease

G. C. Ferreira, 1995, Journal of bioenergetics and biomembranes.

Organization of the terminal two enzymes of the heme biosynthetic pathway. Orientation of protoporphyrinogen oxidase and evidence for a membrane complex.

G. C. Ferreira, H. Dailey, T. Andrew, 1988, The Journal of biological chemistry.

ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria.

C. Beaumont, C. Ged, S. Ducamp, 2011, Blood.

The SOUL family of heme-binding proteins: Structure and function 15 years later

C. Birck, B. Goodfellow, F. Freire, 2021, Coordination Chemistry Reviews.

Aspartate-279 in aminolevulinate synthase affects enzyme catalysis through enhancing the function of the pyridoxal 5'-phosphate cofactor.

G. C. Ferreira, G. Hunter, J. Gong, 1998, Biochemistry.

Mutations at a glycine loop in aminolevulinate synthase affect pyridoxal phosphate cofactor binding and catalysis.

G. C. Ferreira, C. Kay, M. J. Barber, 1996, Biochemistry.

Aminolevulinate synthase: Lysine 313 is not essential for binding the pyridoxal phosphate cofactor but is essential for catalysis

G. C. Ferreira, G. Hunter, M. Barber, 1995, Protein science : a publication of the Protein Society.

Aminolevulinate synthase: functionally important residues at a glycine loop, a putative pyridoxal phosphate cofactor-binding site.

G. C. Ferreira, J. Gong, 1995, Biochemistry.

Intramembranous particles are clustered on microvillus membrane vesicles.

G. C. Ferreira, J. Patton, M. Rigler, 1985, Biochimica et biophysica acta.

Mutations in the iron-sulfur cluster ligands of the human ferrochelatase lead to erythropoietic protoporphyria

M. Dorsey, X. Schneider-Yin, J. Deybach, 2000 .

Mutations in the iron-sulfur cluster ligands of the human ferrochelatase lead to erythropoietic protoporphyria.

M. Dorsey, X. Schneider-Yin, J. Deybach, 2000, Blood.

The solution structure and heme binding of the presequence of murine 5‐aminolevulinate synthase

P. Henklein, B. Goodfellow, G. C. Ferreira, 2001, FEBS letters.

5-Aminolevulinate synthase and the first step of heme biosynthesis

G. C. Ferreira, J. Gong, 1995, Journal of bioenergetics and biomembranes.

Serine 254 Enhances an Induced Fit Mechanism in Murine 5-Aminolevulinate Synthase*

G. C. Ferreira, G. Hunter, Thomas Lendrihas, 2009, The Journal of Biological Chemistry.

Transient Kinetic Studies Support Refinements to the Chemical and Kinetic Mechanisms of Aminolevulinate Synthase*

G. C. Ferreira, G. Hunter, Junshun Zhang, 2007, Journal of Biological Chemistry.

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.

Asn-150 of Murine Erythroid 5-Aminolevulinate Synthase Modulates the Catalytic Balance between the Rates of the Reversible Reaction*

G. C. Ferreira, B. Stojanovski, 2015, The Journal of Biological Chemistry.

Arg‐85 and Thr‐430 in murine 5‐aminolevulinate synthase coordinate acyl‐CoA‐binding and contribute to substrate specificity

G. C. Ferreira, G. Hunter, Junshun Zhang, 2009, Protein science : a publication of the Protein Society.

Circular Permutation of 5-Aminolevulinate Synthase

W. Guida, G. C. Ferreira, A. Cheltsov, 2003, Journal of Biological Chemistry.

Targeting the Active Site Gate to Yield Hyperactive Variants of 5-Aminolevulinate Synthase*

G. C. Ferreira, G. Hunter, Thomas Lendrihas, 2010, The Journal of Biological Chemistry.

Conversion of 5‐aminolevulinate synthase into a more active enzyme by linking the two subunits: Spectroscopic and kinetic properties

G. C. Ferreira, A. Cheltsov, Junshun Zhang, 2005, Protein science : a publication of the Protein Society.

Isoniazid inhibits human erythroid 5-aminolevulinate synthase: Molecular mechanism and tolerance study with four X-linked protoporphyria patients.

Erica J Fratz-Berilla, V. Uversky, L. Breydo, 2017, Biochimica et biophysica acta. Molecular basis of disease.

Chromosomal localization of genes required for the terminal steps of oxidative metabolism: α and γ subunits of ATP synthase and the phosphate carrier

E. Jabs, P. Pedersen, P. Thomas, 1994, Human Genetics.

Chromosomal localization of genes required for the terminal steps of oxidative metabolism: alpha and gamma subunits of ATP synthase and the phosphate carrier.

E. Jabs, P. Pedersen, P. Thomas, 1994, Human genetics.

Chelatases: distort to select?

S. Al-Karadaghi, G. C. Ferreira, J. Shelnutt, 2006, TIBS -Trends in Biochemical Sciences. Regular ed.

Uncovering host-microbiome interactions in global systems with collaborative programming: a novel approach integrating social and data sciences

Linh M Duong, Lynn B. Martin, Khandaker Tasnim Huq, 2020, F1000Research.

Aminolaevulinic acid synthase of Rhodobacter capsulatus: high-resolution kinetic investigation of the structural basis for substrate binding and catalysis.

G. C. Ferreira, D. Jahn, M. Jahn, 2013, The Biochemical journal.

Histidine 282 in 5-aminolevulinate synthase affects substrate binding and catalysis.

G. C. Ferreira, G. Hunter, Junshun Zhang, 2007, Biochemistry.

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.

Role of arginine 439 in substrate binding of 5-aminolevulinate synthase.

G. C. Ferreira, G. Hunter, T. Harrison, 1998, Biochemistry.

Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues.

S. Al-Karadaghi, G. C. Ferreira, T. Karlberg, 2008, Journal of molecular biology.

5-Aminolevulinate Synthase: Pre-Steady State Reaction and Functional Role of Specific Active Site Residues

G. C. Ferreira, 2000 .

Porphyrin interactions with wild-type and mutant mouse ferrochelatase.

G. C. Ferreira, J. Shelnutt, Y. Lu, 2000, Biochemistry.

Circular Permutation of 5-Aminolevulinate Synthase

G. C. Ferreira, A. Cheltsov, Anton V. Cheltsov, 2001, The Journal of Biological Chemistry.

Iron Hack - A symposium/hackathon focused on porphyrias, Friedreich’s ataxia, and other rare iron-related diseases [version 1; peer review: 2 approved]

S. Fatumo, Chengqi Wang, G. C. Ferreira, 2020 .

Circular Permutation of 5-Aminolevulinate Synthase: MAPPING THE POLYPEPTIDE CHAIN TO ITS FUNCTION*

G. C. Ferreira, A. Cheltsov, M. Barber, 2015 .

Synthase Mechanism in Murine 5-Aminolevulinate Serine 254 Enhances an Induced Fit Enzyme Catalysis and Regulation :

G. C. Ferreira, G. Hunter, Thomas Lendrihas, 2010 .

Ferrochelatase binds the iron-responsive element present in the erythroid 5-aminolevulinate synthase mRNA.

G. C. Ferreira, 1995, Biochemical and biophysical research communications.

Mammalian ferrochelatase. Overexpression in Escherichia coli as a soluble protein, purification and characterization.

G. C. Ferreira, 1994, The Journal of biological chemistry.

Modulation of inhibition of ferrochelatase by N-methylprotoporphyrin.

G. C. Ferreira, Zhengtao Shi, 2006, The Biochemical journal.

Binding of protoporphyrin IX and metal derivatives to the active site of wild-type mouse ferrochelatase at low porphyrin-to-protein ratios.

G. C. Ferreira, J. Shelnutt, I. Moura, 2002, Biochemistry.