Associated Papers
Chaperone therapy for homocystinuria: the rescue of CBS mutations by heme arginate.
Melenovská P et al.
Journal of Inherited Metabolic Disease, 2015
The role of surface electrostatics on the stability, function and regulation of human cystathionine β-synthase, a complex multidomain and oligomeric protein.
Pey AL et al.
Biochimica Et Biophysica Acta, 2014
Human cystathionine β-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): complex regulation of CBS activity and stability by SAM.
Pey AL et al.
The Biochemical Journal, 2013
Conformational properties of nine purified cystathionine β-synthase mutants.
Hnízda A et al.
Biochemistry, 2012
Hypermethioninemias of genetic and non-genetic origin: A review.
Mudd SH
American Journal of Medical Genetics. Part C, Seminars in Medical Genetics, 2011
Rescue of cystathionine beta-synthase (CBS) mutants with chemical chaperones: purification and characterization of eight CBS mutant enzymes.
Majtan T et al.
The Journal of Biological Chemistry, 2010
Expression study of mutant cystathionine beta-synthase found in Japanese patients with homocystinuria.
Katsushima F et al.
Molecular Genetics and Metabolism, 2006
The p.T191M mutation of the CBS gene is highly prevalent among homocystinuric patients from Spain, Portugal and South America.
Urreizti R et al.
Journal of Human Genetics, 2006
Structural insights into mutations of cystathionine beta-synthase.
Meier M et al.
Biochimica Et Biophysica Acta, 2003
Cystathionine beta-synthase mutations in homocystinuria.
Kraus JP et al.
Human Mutation, 1999
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