Enzyme sub-functionalization driven by regulation.

about

Enzyme sub-functionalization driven by regulation.

Item

http://www.wikidata.org/entity/Q36405739

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh

2017年學術文章

@zh-hant

name

Enzyme sub-functionalization driven by regulation.

@ast

Enzyme sub-functionalization driven by regulation.

@en

type

Item

label

Enzyme sub-functionalization driven by regulation.

@ast

Enzyme sub-functionalization driven by regulation.

@en

prefLabel

Enzyme sub-functionalization driven by regulation.

@ast

Enzyme sub-functionalization driven by regulation.

@en

P1476

Enzyme sub-functionalization driven by regulation.

@en

P2860

Subfunctionalization of duplicated genes as a transition state to neofunctionalization

An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily

Efficient, crosswise catalytic promiscuity among enzymes that catalyze phosphoryl transfer

Darwinian evolution can follow only very few mutational paths to fitter proteins

Escape from Adaptive Conflict follows from weak functional trade-offs and mutational robustness

Evolutionary biochemistry: revealing the historical and physical causes of protein properties.

Models for gene duplication when dosage balance works as a transition state to subsequent neo-or sub-functionalization

Intersecting transcription networks constrain gene regulatory evolution

P304

1043-1045

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

P31

scholarly article

P356

10.15252/EMBR.201744383

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

P433

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

P478

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

P50

Erich Bornberg-Bauer

Bert van Loo

P577

2017-06-14T00:00:00Z

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

P698

28615289

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

P932

5494500

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