New member of the hormone-sensitive lipase family from the permafrost microbial community

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New member of the hormone-sensitive lipase family from the permafrost microbial community

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http://www.wikidata.org/entity/Q36165836

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

New member of the hormone-sensitive lipase family from the permafrost microbial community

@ast

New member of the hormone-sensitive lipase family from the permafrost microbial community

@en

type

Item

label

New member of the hormone-sensitive lipase family from the permafrost microbial community

@ast

New member of the hormone-sensitive lipase family from the permafrost microbial community

@en

prefLabel

New member of the hormone-sensitive lipase family from the permafrost microbial community

@ast

New member of the hormone-sensitive lipase family from the permafrost microbial community

@en

P1476

New member of the hormone-sensitive lipase family from the permafrost microbial community

@en

P2093

Ekaterina V Durdenko

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

Ksenia A Novototskaya-Vlasova

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

Lada E Petrovskaya

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

Sultan Sh Gapizov

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

P2860

Structure and activity of the cold-active and anion-activated carboxyl esterase OLEI01171 from the oil-degrading marine bacterium Oleispira antarctica

Structural Basis for Dimerization and Catalysis of a Novel Esterase from the GTSAG Motif Subfamily of the Bacterial Hormone-sensitive Lipase Family

Microbial life in permafrost.

Cloning and characterization of a new cold-active lipase from a deep-sea sediment metagenome.

Characterization and its potential application of two esterases derived from the arctic sediment metagenome.

Identification of a new subfamily of salt-tolerant esterases from a metagenomic library of tidal flat sediment.

Function and biotechnology of extremophilic enzymes in low water activity.

Interdomain hydrophobic interactions modulate the thermostability of microbial esterases from the hormone-sensitive lipase family

Expression and characterization of a new esterase with GCSAG motif from a permafrost metagenomic library.

Lipases: an overview.

P304

420-423

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

P31

scholarly article

P356

10.1080/21655979.2016.1230571

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

P433

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

P478

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

P50

Elizaveta Rivkina

Elena Spirina

P577

2016-10-18T00:00:00Z

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

P698

27753534

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

P921

permafrost

P932

5553336

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