A novel mutation of human liver alanine:glyoxylate aminotransferase causes primary hyperoxaluria type 1: immunohistochemical quantification and subcellular distribution.

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Mutational analysis of AGXT in two Chinese families with primary hyperoxaluria type 1.

P2860

Q33842031-F44C8A48-0620-4151-B739-2EC860438D6A

P2860

A novel mutation of human liver alanine:glyoxylate aminotransferase causes primary hyperoxaluria type 1: immunohistochemical quantification and subcellular distribution.

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http://www.wikidata.org/entity/Q42002476

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2012 nî lūn-bûn

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2012年の論文

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2012年論文

@yue

2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

A novel mutation of human live ...... and subcellular distribution.

@en

A novel mutation of human live ...... and subcellular distribution.

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type

Item

label

A novel mutation of human live ...... and subcellular distribution.

@en

A novel mutation of human live ...... and subcellular distribution.

@nl

prefLabel

A novel mutation of human live ...... and subcellular distribution.

@en

A novel mutation of human live ...... and subcellular distribution.

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P1476

A novel mutation of human live ...... n and subcellular distribution

@en

P2093

Chikage Kawai

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Hidetaka Akiyoshi

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

Shigenobu Tone

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

Tsunatoshi Suehiro

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

Yohsuke Minatogawa

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

P2860

The Sequence of the Human Genome

Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I

Peroxisomal import of human alanine:glyoxylate aminotransferase requires ancillary targeting information remote from its C terminus

Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon

Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import.

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations

A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1

A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1

Molecular etiology of primary hyperoxaluria type 1: new directions for treatment

P304

121-129

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scholarly article

P356

10.1267/AHC.11042

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P433

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

P478

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

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Shinichi Hirose

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2012-03-10T00:00:00Z

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225290841

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22685354

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3365303

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A novel mutation of human liver alanine:glyoxylate aminotransferase causes primary hyperoxaluria type 1: immunohistochemical quantification and subcellular distribution.

about

P2860

P2860

A novel mutation of human liver alanine:glyoxylate aminotransferase causes primary hyperoxaluria type 1: immunohistochemical quantification and subcellular distribution.

description

name

type

label

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P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932