Using FlAsH to probe conformational changes in a large HEAT repeat protein.

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Rotamer-Restricted Fluorogenicity of the Bis-Arsenical ReAsH.Interactions of AsCy3 with cysteine-rich peptides

P2860

Q39172842-26E120AD-19EF-4969-98BC-3DF46E08EFD0 Q41871029-0E291475-4563-42BB-A080-C1CD8C2D6FCD

P2860

Using FlAsH to probe conformational changes in a large HEAT repeat protein.

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http://www.wikidata.org/entity/Q52624746

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2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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Using FlAsH to probe conformational changes in a large HEAT repeat protein.

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Using FlAsH to probe conformational changes in a large HEAT repeat protein.

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Using FlAsH to probe conformational changes in a large HEAT repeat protein.

@en

Using FlAsH to probe conformational changes in a large HEAT repeat protein.

@nl

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Using FlAsH to probe conformational changes in a large HEAT repeat protein.

@en

Using FlAsH to probe conformational changes in a large HEAT repeat protein.

@nl

P1476

Using FlAsH to probe conformational changes in a large HEAT repeat protein

@en

P2093

Maksym Tsytlonok

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

P2860

The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs

Preparation of the membrane-permeant biarsenicals FlAsH-EDT2 and ReAsH-EDT2 for fluorescent labeling of tetracysteine-tagged proteins

Monitoring protein stability in vivo

Calculation of protein extinction coefficients from amino acid sequence data

Specific covalent labeling of recombinant protein molecules inside live cells

The fluorescent toolbox for assessing protein location and function

Aggregation of a slow-folding mutant of a beta-clam protein proceeds through a monomeric nucleus.

Effects of osmolytes on protein folding and aggregation in cells.

Surveying protein structure and function using bis-arsenical small molecules

PR65, the HEAT-repeat scaffold of phosphatase PP2A, is an elastic connector that links force and catalysis

P304

1199-1205

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

P31

scholarly article

P356

10.1002/CBIC.201200012

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

P433

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

P478

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

P50

Laura Itzhaki

P577

2012-04-26T00:00:00Z

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

P5875

224855552

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P698

22539214

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Using FlAsH to probe conformational changes in a large HEAT repeat protein.

about

P2860

P2860

Using FlAsH to probe conformational changes in a large HEAT repeat protein.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698