Dual Unnatural Amino Acid Incorporation and Click-Chemistry Labeling to Enable Single-Molecule FRET Studies of p97 Folding.

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Conformational transition of FGFR kinase activation revealed by site-specific unnatural amino acid reporter and single molecule FRET.Dual modification of biomolecules.A Bifunctional Amino Acid Enables Both Covalent Chemical Capture and Isolation of in Vivo Protein-Protein Interactions.

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P2860

Dual Unnatural Amino Acid Incorporation and Click-Chemistry Labeling to Enable Single-Molecule FRET Studies of p97 Folding.

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http://www.wikidata.org/entity/Q36997177

description

2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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name

Dual Unnatural Amino Acid Inco ...... e FRET Studies of p97 Folding.

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type

Item

label

Dual Unnatural Amino Acid Inco ...... e FRET Studies of p97 Folding.

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prefLabel

Dual Unnatural Amino Acid Inco ...... e FRET Studies of p97 Folding.

@en

P1476

Dual Unnatural Amino Acid Inco ...... e FRET Studies of p97 Folding.

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P2093

Ashok A Deniz

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

Chan Hyuk Kim

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

Eli Chapman

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

Minjin Kang

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

Peter G Schultz

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

P2860

Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change

Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities

ATPase activity of p97-valosin-containing protein (VCP). D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity

Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system

The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97

Evolutionary relationships and structural mechanisms of AAA+ proteins

Single-molecule resolution of protein structure and interfacial dynamics on biomaterial surfaces

A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer

Withaferin A Analogs That Target the AAA+ Chaperone p97.

Functional chromatography reveals three natural products that target the same protein with distinct mechanisms of action.

P304

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scholarly article

P356

10.1002/CBIC.201500695

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P433

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P478

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

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Taehyung Lee

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2016-04-26T00:00:00Z

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27115850

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4904727

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Dual Unnatural Amino Acid Incorporation and Click-Chemistry Labeling to Enable Single-Molecule FRET Studies of p97 Folding.

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P2860

P2860

Dual Unnatural Amino Acid Incorporation and Click-Chemistry Labeling to Enable Single-Molecule FRET Studies of p97 Folding.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932