(Q43559464)

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Biochemical basis for the dominant inheritance of hypermethioninemia associated with the R264H mutation of the MAT1A gene. A monomeric methionine adenosyltransferase with tripolyphosphatase activity

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Europe PubMed Central

PubMed publication ID

24 November 2017

Biochemical basis for the dominant inheritance of hypermethioninemia associated with the R264H mutation of the MAT1A gene. A monomeric methionine adenosyltransferase with tripolyphosphatase activity (English)

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

author name string

Pérez Mato I

1

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Sanchez del Pino MM

2

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Europe PubMed Central

PubMed publication ID

24 November 2017

Chamberlin ME

3

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Mudd SH

4

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Europe PubMed Central

PubMed publication ID

24 November 2017

Mato JM

5

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Corrales FJ

6

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Europe PubMed Central

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24 November 2017

language of work or name

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publication date

30 January 2001

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Europe PubMed Central

PubMed publication ID

24 November 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

24 November 2017

276

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Europe PubMed Central

PubMed publication ID

24 November 2017

17

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

13803-13809

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Isolation of a cDNA encoding the rat liver S-adenosylmethionine synthetase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Analysis of the 5' non-coding region of rat liver S-adenosylmethionine synthetase mRNA and comparison of the Mr deduced from the cDNA sequence and the purified enzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Characterization of a full-length cDNA encoding human liver S-adenosylmethionine synthetase: tissue-specific gene expression and mRNA levels in hepatopathies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Labile methyl group balances in the human: The role of sarcosine

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Methionine adenosyltransferase deficiency: new enzymatic defect associated with hypermethioninemia.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Persistent hypermethioninaemia with dominant inheritance.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Normal brain myelination in a patient homozygous for a mutation that encodes a severely truncated methionine adenosyltransferase I/III.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Methionine adenosyltransferase I/III deficiency: novel mutations and clinical variations

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Crystal structure of S-adenosylmethionine synthetase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Site-directed mutagenesis of rat liver S-adenosylmethionine synthetase. Identification of a cysteine residue critical for the oligomeric state

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Methionine adenosyltransferase S-nitrosylation is regulated by the basic and acidic amino acids surrounding the target thiol.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Hysteretic behavior of methionine adenosyltransferase III. Methionine switches between two conformations of the enzyme with different specific activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

An improved assay for nanomole amounts of inorganic phosphate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

The crystal structure of tetrameric methionine adenosyltransferase from rat liver reveals the methionine-binding site

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Energetics of S-adenosylmethionine synthetase catalysis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009017200

21 January 2018

Identifiers

10.1074/JBC.M009017200

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PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

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