Membrane chaperoning by members of the PspA/IM30 protein family.

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Membrane chaperoning by members of the PspA/IM30 protein family.

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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年学术文章

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2017年學術文章

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2017年學術文章

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2017年學術文章

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Membrane chaperoning by members of the PspA/IM30 protein family.

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Membrane chaperoning by members of the PspA/IM30 protein family.

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Item

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Membrane chaperoning by members of the PspA/IM30 protein family.

@en

Membrane chaperoning by members of the PspA/IM30 protein family.

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Membrane chaperoning by members of the PspA/IM30 protein family.

@en

Membrane chaperoning by members of the PspA/IM30 protein family.

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P1476

Membrane chaperoning by members of the PspA/IM30 protein family.

@en

P2093

Adrien Thurotte

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

Dirk Schneider

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

Thomas Brüser

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

Thorsten Mascher

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P2860

Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding

Recent findings about the Yersinia enterocolitica phage shock protein response

PspF-binding domain PspA1-144 and the PspA·F complex: New insights into the coiled-coil-dependent regulation of AAA+ proteins

AMPs and OMPs: Is the folding and bilayer insertion of β-stranded outer membrane proteins governed by the same biophysical principles as for α-helical antimicrobial peptides?

Changes in Psp protein binding partners, localization and behaviour upon activation of the Yersinia enterocolitica phage shock protein response

Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway.

A small heat shock protein enables Escherichia coli to grow at a lethal temperature of 50°C conceivably by maintaining cell envelope integrity.

Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides.

Lipid composition determines the effects of arbutin on the stability of membranes

Chaperone function of sHsps.

P31

scholarly article

P356

10.1080/19420889.2016.1264546

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P433

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

P478

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

P577

2017-02-19T00:00:00Z

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P921

protein family

molecular chaperones

P932

5333519

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