Oligomeric status of human cystathionine beta-synthase modulates AdoMet binding.

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Potential Pharmacological Chaperones for Cystathionine Beta-Synthase-Deficient Homocystinuria.

P2860

Q47422775-B9819EE3-EB02-4AC6-B776-71E5E3FC4E39

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Oligomeric status of human cystathionine beta-synthase modulates AdoMet binding.

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年學術文章

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Oligomeric status of human cystathionine beta-synthase modulates AdoMet binding.

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Oligomeric status of human cystathionine beta-synthase modulates AdoMet binding.

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Item

label

Oligomeric status of human cystathionine beta-synthase modulates AdoMet binding.

@en

Oligomeric status of human cystathionine beta-synthase modulates AdoMet binding.

@nl

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Oligomeric status of human cystathionine beta-synthase modulates AdoMet binding.

@en

Oligomeric status of human cystathionine beta-synthase modulates AdoMet binding.

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P1476

Oligomeric status of human cystathionine beta-synthase modulates AdoMet binding

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P2093

Jan P Kraus

http://www.w3.org/2001/XMLSchema#string

Tomas Majtan

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P2860

Human cystathionine β-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): complex regulation of CBS activity and stability by SAM

Structural basis of regulation and oligomerization of human cystathionine -synthase, the central enzyme of transsulfuration

The Role of Protein Denaturation Energetics and Molecular Chaperones in the Aggregation and Mistargeting of Mutants Causing Primary Hyperoxaluria Type I

Domain organization, catalysis and regulation of eukaryotic cystathionine beta-synthases

Rescue of cystathionine beta-synthase (CBS) mutants with chemical chaperones: purification and characterization of eight CBS mutant enzymes.

The role of surface electrostatics on the stability, function and regulation of human cystathionine β-synthase, a complex multidomain and oligomeric protein

Structural insight into the molecular mechanism of allosteric activation of human cystathionine β-synthase by S-adenosylmethionine

Inter-domain communication of human cystathionine β-synthase: structural basis of S-adenosyl-L-methionine activation.

Folding and activity of mutant cystathionine β-synthase depends on the position and nature of the purification tag: characterization of the R266K CBS mutant

Purification, crystallization and preliminary crystallographic analysis of human cystathionine β-synthase.

P304

4461-4471

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scholarly article

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10.1002/1873-3468.12488

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English

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http://www.w3.org/2001/XMLSchema#string

P478

590

http://www.w3.org/2001/XMLSchema#string

P50

Angel L. Pey

Luis Alfonso Martínez-Cruz

P577

2016-11-23T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

27861796

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Oligomeric status of human cystathionine beta-synthase modulates AdoMet binding.

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P2860

P2860

Oligomeric status of human cystathionine beta-synthase modulates AdoMet binding.

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P356

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P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698