The arsenic hyperaccumulating Pteris vittata expresses two arsenate reductases.

about

Evidence for exocellular Arsenic in Fronds of Pteris vittata.Isolation and identification of flavonoids components from Pteris vittata L.An Endophytic Bacterial Consortium modulates multiple strategies to improve Arsenic Phytoremediation Efficacy in Solanum nigrum.

P2860

Q33767087-44C60949-CC26-4C3E-B12D-567AEE87282B Q39181186-01A19492-46DF-409C-8BF8-1FC387F515C4 Q55114447-8EFD5EDA-2B5F-45CF-B523-09B7E7986773

P2860

The arsenic hyperaccumulating Pteris vittata expresses two arsenate reductases.

Item

http://www.wikidata.org/entity/Q40494347

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年学术文章

@wuu

2015年学术文章

@zh-cn

2015年学术文章

@zh-hans

2015年学术文章

@zh-my

2015年学术文章

@zh-sg

2015年學術文章

@yue

2015年學術文章

@zh

2015年學術文章

@zh-hant

name

The arsenic hyperaccumulating Pteris vittata expresses two arsenate reductases.

@en

type

Item

label

The arsenic hyperaccumulating Pteris vittata expresses two arsenate reductases.

@en

prefLabel

The arsenic hyperaccumulating Pteris vittata expresses two arsenate reductases.

@en

P1476

The arsenic hyperaccumulating Pteris vittata expresses two arsenate reductases.

@en

P2093

Chiara Cattaneo

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

Graziella Berta

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

P2860

Characterization of arsenate reductase in the extract of roots and fronds of Chinese brake fern, an arsenic hyperaccumulator

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Mechanisms of arsenic hyperaccumulation in Pteris vittata. Uptake kinetics, interactions with phosphate, and arsenic speciation

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

A Revised Medium for Rapid Growth and Bio Assays with Tobacco Tissue Cultures

Probability-based protein identification by searching sequence databases using mass spectrometry data

A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain.

Purification and characterization of ACR2p, the Saccharomyces cerevisiae arsenate reductase.

Detoxification of arsenic by phytochelatins in plants

Genome-wide association mapping identifies a new arsenate reductase enzyme critical for limiting arsenic accumulation in plants

P2888

srep14525

P304

14525

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

P31

scholarly article

P356

10.1038/SREP14525

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

P407

English

P478

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

P50

Maria Cavaletto

Elisa Bona

Patrizia Cesaro

P577

2015-09-28T00:00:00Z

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

P5875

282290844

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

P6179

1009179133

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

P698

26412036

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

P932

4585942

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

The arsenic hyperaccumulating Pteris vittata expresses two arsenate reductases.

about

P2860

P2860

The arsenic hyperaccumulating Pteris vittata expresses two arsenate reductases.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

P577

P5875

P6179

P698

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

P577

P5875

P6179

P698

P932