Redox-sensitive GFP fusions for monitoring the catalytic mechanism and inactivation of peroxiredoxins in living cells.

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Identification of Antioxidant Proteins With Deep Learning From Sequence Information

P2860

Q57191809-BA0FDAB2-67CA-40C4-AE9F-BD779FD420EF

P2860

Redox-sensitive GFP fusions for monitoring the catalytic mechanism and inactivation of peroxiredoxins in living cells.

Item

http://www.wikidata.org/entity/Q44187944

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

@zh-hant

name

Redox-sensitive GFP fusions fo ...... eroxiredoxins in living cells.

@en

Redox-sensitive GFP fusions fo ...... eroxiredoxins in living cells.

@nl

type

Item

label

Redox-sensitive GFP fusions fo ...... eroxiredoxins in living cells.

@en

Redox-sensitive GFP fusions fo ...... eroxiredoxins in living cells.

@nl

prefLabel

Redox-sensitive GFP fusions fo ...... eroxiredoxins in living cells.

@en

Redox-sensitive GFP fusions fo ...... eroxiredoxins in living cells.

@nl

P1476

Redox-sensitive GFP fusions fo ...... eroxiredoxins in living cells.

@en

P2093

Bruce Morgan

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

Marcel Deponte

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

Rafael Radi

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

Tobias P Dick

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

Verena Staudacher

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

P2860

Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site

Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation

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Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling

Plasmodium falciparum antioxidant protein reveals a novel mechanism for balancing turnover and inactivation of peroxiredoxins

Proximity-based protein thiol oxidation by H2O2-scavenging peroxidases.

Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: rate constants by competitive kinetics.

Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis.

Thioredoxin networks in the malarial parasite Plasmodium falciparum

Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: kinetics, acidity constants, and conformational dynamics

P304

549-556

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

P31

scholarly article

P356

10.1016/J.REDOX.2017.10.017

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

P478

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

P50

Madia Trujillo

Tim Diederichs

P577

2017-10-26T00:00:00Z

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

P698

29128826

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

P932

5684490

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Redox-sensitive GFP fusions for monitoring the catalytic mechanism and inactivation of peroxiredoxins in living cells.

about

P2860

P2860

Redox-sensitive GFP fusions for monitoring the catalytic mechanism and inactivation of peroxiredoxins in living cells.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P478

P50

P577

P698

P932